Q9JHU4

SS
Gene name
Dync1h1 (Dhc1, Dnch1, Dnchc1, Dyhc)
Protein name
Cytoplasmic dynein 1 heavy chain 1
Names
Cytoplasmic dynein heavy chain 1 , Dynein heavy chain, cytosolic
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:13424
EC number
Protein Class

Descriptions

Cytoplasmic dynein (dynein hereafter) is an AAA+ motor responsible for nearly all motility and force generation towards the microtubule (MT) minus-end and involved in a wide variety of cellular functions, such as positioning of intracellular organelles, breakdown of the nuclear envelope and assembly of the mitotic spindle. The partial loss of dynein function has been implicated in a range of neurodegenerative and neurodevelopmental conditions, including spinal muscular atrophy, amyotrophic lateral sclerosis, Alzheimer's disease, and schizophrenia. <br>The core of the dynein complex is a homodimer of two heavy chains, the C-terminal motor domain of which is a catalytic ring of six AAA modules (AAA1-6). Dynein's MT binding domain is separated from the catalytic domain by a coiled-coil stalk. When dynein is not bound to its cargo, it forms two distinct conformations, the phi-particle, and open conformations, both of which move poorly along MTs. Formation of a dynein-dynactin-cargo adaptor complex aligns the dynein motor domains in a parallel conformation and activates processive motility along MTs. <br>Lissencephaly-1 (Lis-1) promotes the formation of the active complex with dynactin and also favors the recruitment of two dyneins to dynactin, resulting in increased velocity, higher force production and more effective competition against kinesin. Lis-1 binds to release dynein from its autoinhibited state and dissociates form motile complexes, indicating that its primary role is to orchestrate the assembly of the transport machinery.

Autoinhibitory domains (AIDs)

240-830 (Dynein Tail) SS

Target domain

1899-3093 (Motor domain)

Relief mechanism

Partner binding

Assay

1319-1717 (Dynein heavy chain linker) SS

Target domain

1899-3093 (Motor domain)

Relief mechanism

Partner binding

Assay

1866-4219 (Motor domain) SS

Target domain

1866-4219 (Motor domain in other dynein-1)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

7 structures for Q9JHU4

Entry ID Method Resolution Chain Position Source
3ERR X-ray 227 A A/B 3260-3427 PDB
3J1T EM 970 A A 3264-3427 PDB
3J1U EM 970 A A 3264-3427 PDB
3WUQ X-ray 350 A A 3207-3483 PDB
5AYH X-ray 301 A A 3207-3475 PDB
6RZA EM 540 A PDB
6RZB EM 500 A C 3270-3418 PDB

219 variants for Q9JHU4

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389259422 95 E>* No EVA
rs3389191781 123 I>N No EVA
rs3389270517 130 S>* No EVA
rs3389233043 132 Q>R No EVA
rs3389275060 141 D>E No EVA
rs3389275008 178 P>H No EVA
rs3389262897 206 P>Q No EVA
rs240870455 219 Y>H No EVA
rs3389191750 223 E>Q No EVA
rs244357461 232 D>E No EVA
rs3389259019 250 W>* No EVA
rs3389228848 251 I>N No EVA
rs3389267808 303 K>R No EVA
rs3389255954 311 T>N No EVA
rs3389220242 313 S>G No EVA
rs3389258952 365 I>N No EVA
rs3389246192 390 L>P No EVA
rs3389257673 394 L>M No EVA
rs3389255890 429 Q>* No EVA
rs3389258990 462 D>Y No EVA
rs33345603 517 A>T No EVA
580 F>Y LOA [UniProt] No
rs3389253756 607 I>L No EVA
rs3389191698 621 F>L No EVA
rs3389274983 655 Q>* No EVA
rs3389275043 681 K>M No EVA
rs3389253744 690 K>M No EVA
rs3389220264 748 V>I No EVA
rs3389259426 790 C>Y No EVA
rs3389267807 802 L>I No EVA
rs3389253780 824 S>F No EVA
rs3389220244 837 T>S No EVA
rs3389220172 853 E>K No EVA
rs3389262879 886 L>Q No EVA
rs3389261605 897 W>* No EVA
rs3389255887 945 H>Q No EVA
rs3389220099 956 V>M No EVA
rs263635107 986 A>S No EVA
rs3389257626 990 V>F No EVA
rs3389274981 995 P>S No EVA
1055 Y>C CRA1 [UniProt] No
rs33347673 1075 N>H No EVA
rs3389259418 1097 K>E No EVA
rs3389262850 1104 V>M No EVA
rs3389259335 1106 D>V No EVA
rs3389220211 1113 K>M No EVA
rs3389255903 1274 A>D No EVA
rs3389246191 1279 T>S No EVA
rs3389246199 1392 M>T No EVA
rs3389259390 1394 I>T No EVA
rs3403832724 1396 M>V No EVA
rs3389191738 1397 L>S No EVA
rs3389275015 1404 E>K No EVA
rs3389233076 1455 M>K No EVA
rs3389267804 1521 W>G No EVA
rs3389259376 1524 K>R No EVA
rs3389255965 1532 F>L No EVA
rs3389257600 1569 I>V No EVA
rs3389261593 1585 L>R No EVA
rs3389233108 1610 Q>* No EVA
rs3389246208 1642 S>G No EVA
rs3389262862 1695 K>Q No EVA
rs3389275007 1699 W>R No EVA
rs3389191713 1739 W>R No EVA
rs3389246239 1754 I>K No EVA
rs3389233089 1756 W>R No EVA
rs3389246176 1800 P>H No EVA
rs3389228860 1804 R>L No EVA
rs222239631 1831 A>S No EVA
rs3389262845 1835 E>G No EVA
rs3389259369 1844 F>Y No EVA
rs3389255958 1854 Q>* No EVA
rs3389246218 1868 F>S No EVA
rs3389275028 1884 D>H No EVA
rs3389257654 1903 F>S No EVA
rs3389255934 1905 P>H No EVA
rs3389233024 1924 F>L No EVA
rs3389191708 1933 T>P No EVA
rs3389270438 1969 V>I No EVA
rs3389191745 2031 K>* No EVA
rs3403009898 2033 L>R No EVA
rs3403060400 2035 R>L No EVA
rs3403743100 2035 R>W No EVA
rs3412945730 2072 K>R No EVA
rs3404044280 2117 G>E No EVA
rs3389267799 2177 R>Q No EVA
rs3389228842 2182 K>N No EVA
rs3403735066 2217 G>C No EVA
rs3403713929 2217 G>V No EVA
rs3389246210 2232 W>S No EVA
rs3389267821 2253 D>E No EVA
rs3389275045 2257 I>N No EVA
rs3389233061 2283 R>* No EVA
rs3389261092 2285 I>N No EVA
rs3389220195 2288 N>I No EVA
rs3389259360 2288 N>K No EVA
rs3389261613 2340 M>V No EVA
rs3389233053 2362 F>L No EVA
rs3389193050 2362 F>Y No EVA
rs3389259394 2373 F>L No EVA
rs3389262899 2402 E>K No EVA
rs3389253819 2414 Q>K No EVA
rs3389255883 2424 Y>* No EVA
rs3389261138 2434 A>T No EVA
rs3389233094 2504 S>N No EVA
rs3389274995 2509 R>S No EVA
rs3404044760 2517 R>L No EVA
rs3389261081 2521 T>P No EVA
rs3389275054 2530 V>L No EVA
rs3389220209 2533 I>T No EVA
rs3389253798 2534 D>H No EVA
rs3389255878 2558 H>Q No EVA
rs3389257606 2561 A>T No EVA
rs3389261598 2561 A>V No EVA
rs3389253814 2574 R>G No EVA
rs3389259355 2580 Y>* No EVA
rs3389270489 2592 C>Y No EVA
rs3550078755 2658 V>G No EVA
rs3389261104 2665 N>I No EVA
rs3389246168 2675 Q>H No EVA
rs3389263758 2707 V>A No EVA
rs3389257611 2711 N>K No EVA
rs3389257643 2722 S>L No EVA
rs3389257641 2763 Y>* No EVA
rs3389275049 2774 F>I No EVA
rs3389261073 2789 H>L No EVA
rs3389260101 2823 W>* No EVA
rs3389255933 2929 G>C No EVA
rs3389261643 2930 H>L No EVA
rs3389260021 2932 L>I No EVA
rs3389263718 2969 D>E No EVA
rs3389233097 2970 F>Y No EVA
rs3389267770 2971 D>E No EVA
rs3389260044 2972 E>D No EVA
rs3389234565 2981 S>T No EVA
rs3389263725 3048 L>F No EVA
rs3389270474 3083 L>P No EVA
rs3389261085 3126 V>F No EVA
rs3389261127 3128 Y>* No EVA
rs3389260082 3154 Q>* No EVA
rs3389270492 3158 R>L No EVA
rs3389275053 3203 L>P No EVA
rs3389246201 3275 S>N No EVA
rs3389228818 3313 A>T No EVA
rs3412177896 3359 D>E No EVA
rs3389261621 3368 N>K No EVA
rs3389193124 3375 Y>H No EVA
rs3403060404 3406 R>L No EVA
rs3403060404 3406 R>LIPQGLHSL* No EVA
rs3389261563 3424 N>Y No EVA
rs3389253774 3442 I>T No EVA
rs3389257631 3474 T>S No EVA
rs3389228812 3494 F>L No EVA
rs3389246226 3494 F>S No EVA
rs3389228857 3532 H>Q No EVA
rs3389260077 3543 T>I No EVA
rs3389270432 3549 E>K No EVA
rs3389228832 3553 N>S No EVA
rs3389246203 3557 R>C No EVA
rs3389253811 3572 T>I No EVA
rs3389263742 3595 T>I No EVA
rs3389234645 3627 F>I No EVA
rs3389220246 3640 D>Y No EVA
rs3389267744 3692 S>F No EVA
rs3389257665 3702 T>I No EVA
rs3389220251 3714 V>A No EVA
rs3389275047 3721 D>E No EVA
rs3389263719 3742 Q>H No EVA
rs3389255908 3763 T>N No EVA
rs3389220132 3785 T>I No EVA
rs3389260043 3791 E>* No EVA
rs3389261106 3812 T>S No EVA
rs3389193102 3839 Y>F No EVA
rs29181736 3856 I>V No EVA
rs3389260086 3874 L>Q No EVA
rs3389274999 3887 R>S No EVA
rs3389275037 3909 G>W No EVA
rs248062748 3919 T>A No EVA
rs3389220213 3921 K>I No EVA
rs3403833595 3947 A>G No EVA
rs3389270488 3979 T>I No EVA
rs3389275041 3982 G>R No EVA
rs3389260069 4009 T>A No EVA
rs3403060403 4011 L>I No EVA
rs3389234606 4017 S>T No EVA
rs3389257661 4019 M>K No EVA
rs3389234647 4060 Q>H No EVA
rs3389275035 4093 M>I No EVA
rs3403909151 4128 I>M No EVA
rs3402355053 4129 N>I No EVA
rs3389257642 4138 R>H No EVA
rs3389253801 4139 A>V No EVA
rs3389234610 4143 F>S No EVA
rs3389257640 4211 R>Q No EVA
rs3389255953 4217 V>A No EVA
rs3389260091 4222 D>N No EVA
rs3389261152 4245 M>L No EVA
rs3389234572 4261 R>H No EVA
rs3403743084 4265 T>S No EVA
rs1132395785 4267 L>Q No EVA
rs3389228789 4292 I>L No EVA
rs3389220185 4311 P>S No EVA
rs3389228774 4312 D>N No EVA
rs3403909161 4333 Q>* No EVA
rs3403507095 4333 Q>L No EVA
rs3389270501 4339 S>N No EVA
rs3389261140 4352 D>V No EVA
rs33352852 4383 S>F No EVA
rs3389253794 4388 L>I No EVA
rs3389270113 4389 I>T No EVA
rs3389263709 4398 R>H No EVA
rs3389260048 4413 R>K No EVA
rs3389260025 4435 V>M No EVA
rs3389220217 4463 S>P No EVA
rs3389220184 4464 H>L No EVA
rs3389260090 4475 Q>E No EVA
rs3389246190 4516 E>A No EVA
rs3389193097 4534 L>M No EVA
rs3389261622 4611 F>Y No EVA

2 associated diseases with Q9JHU4

Without disease ID

15 regional properties for Q9JHU4

Type Name Position InterPro Accession
domain AAA+ ATPase domain 1899 - 2043 IPR003593-1
domain AAA+ ATPase domain 2214 - 2365 IPR003593-2
domain AAA+ ATPase domain 2585 - 2735 IPR003593-3
domain AAA+ ATPase domain 2927 - 3093 IPR003593-4
domain Dynein heavy chain region D6 P-loop domain 4035 - 4142 IPR004273
domain Dynein heavy chain, tail 240 - 830 IPR013594
domain Dynein heavy chain, linker 1320 - 1717 IPR013602
domain Dynein heavy chain, AAA module D4 2906 - 3184 IPR024317
domain Dynein heavy chain, coiled coil stalk 3199 - 3530 IPR024743
domain Dynein heavy chain, hydrolytic ATP-binding dynein motor region 1866 - 2229 IPR035699
domain Dynein heavy chain, ATP-binding dynein motor region 3559 - 3778 IPR035706
domain Dynein heavy chain, C-terminal domain 4332 - 4642 IPR041228
domain Dynein heavy chain, AAA 5 extension domain 2422 - 2547 IPR041466
domain Dynein heavy chain AAA lid domain 4175 - 4325 IPR041658
domain Dynein 2 heavy chain 1, cytoplasmic, ATPase lid domain 2749 - 2841 IPR054354

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytoskeleton
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

13 GO annotations of cellular component

Name Definition
axon The long process of a neuron that conducts nerve impulses, usually away from the cell body to the terminals and varicosities, which are sites of storage and release of neurotransmitter.
axon cytoplasm Any cytoplasm that is part of a axon.
axonemal dynein complex A dynein complex found in eukaryotic cilia and flagella; the motor domain heads interact with adjacent microtubules to generate a sliding force which is converted to a bending motion.
cell cortex The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins.
centrosome A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoplasmic dynein complex Any dynein complex with a homodimeric dynein heavy chain core that catalyzes movement along a microtubule. Cytoplasmic dynein complexes participate in many cytoplasmic transport activities in eukaryotes, such as mRNA localization, intermediate filament transport, nuclear envelope breakdown, apoptosis, transport of centrosomal proteins, mitotic spindle assembly, virus transport, kinetochore functions, and movement of signaling and spindle checkpoint proteins. Some complexes participate in intraflagellar transport. Subunits associated with the dynein heavy chain mediate association between dynein heavy chain and cargoes, and may include light chains and light intermediate chains.
cytoplasmic microtubule Any microtubule in the cytoplasm of a cell.
dynein complex Any of several large complexes that contain two or three dynein heavy chains and several light chains, and have microtubule motor activity.
filopodium Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft.
manchette A tubular array of microtubules that extends from the perinuclear ring surrounding the spermatid nucleus to the flagellar axoneme. The manchette may also contain F-actin filaments.
neuronal cell body The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
nuclear envelope The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction
dynein intermediate chain binding Binding to an intermediate chain of the dynein complex.
dynein light intermediate chain binding Binding to a light intermediate chain of the dynein complex.
minus-end-directed microtubule motor activity A motor activity that generates movement along a microtubule toward the minus end, driven by ATP hydrolysis.

14 GO annotations of biological process

Name Definition
cell division The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
cilium movement The directed, self-propelled movement of a cilium.
cytoplasmic microtubule organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of structures formed of microtubules and associated proteins in the cytoplasm of a cell.
establishment of spindle localization The directed movement of the spindle to a specific location in the cell.
mitotic spindle organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle.
nuclear migration The directed movement of the nucleus to a specific location within a cell.
P-body assembly The aggregation, arrangement and bonding together of proteins and RNA molecules to form a cytoplasmic mRNA processing body.
positive regulation of cold-induced thermogenesis Any process that activates or increases the frequency, rate or extent of cold-induced thermogenesis.
positive regulation of intracellular transport Any process that activates or increases the frequency, rate or extent of the directed movement of substances within cells.
positive regulation of spindle assembly Any process that activates or increases the frequency, rate or extent of spindle assembly.
regulation of metaphase plate congression Any process that modulates the rate, frequency, or extent of metaphase plate congression, the alignment of chromosomes at the metaphase plate, a plane halfway between the poles of the spindle.
regulation of mitotic spindle organization Any process that modulates the rate, frequency or extent of the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle.
retrograde axonal transport The directed movement of organelles or molecules along microtubules from the cell periphery toward the cell body in nerve cell axons.
stress granule assembly The aggregation, arrangement and bonding together of proteins and RNA molecules to form a stress granule.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P36022 DYN1 Dynein heavy chain, cytoplasmic Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) EV
P37276 Dhc64C Dynein heavy chain, cytoplasmic Drosophila melanogaster (Fruit fly) SS
Q14204 DYNC1H1 Cytoplasmic dynein 1 heavy chain 1 Homo sapiens (Human) EV
P38650 Dync1h1 Cytoplasmic dynein 1 heavy chain 1 Rattus norvegicus (Rat) SS
Q19020 dhc-1 Dynein heavy chain, cytoplasmic Caenorhabditis elegans SS
10 20 30 40 50 60
MSEPGGGEDG SAGLEVSAVQ NVADVAVLQK HLRKLVPLLL EDGGDAPAAL EAALEEKSAL
70 80 90 100 110 120
EQMRKFLSDP QVHTVLVERS TLKEDVGDEG EEEKEFISYN INIDIHYGVK SNSLAFIKRA
130 140 150 160 170 180
PVIDADKPVS SQLRVLTLSE DSPYETLHSF ISNAVAPFFK SYIRESGKAD RDGDKMAPSV
190 200 210 220 230 240
EKKIAELEMG LLHLQQNIEI PEISLPIHPI ITNVAKQCYE RGEKPKVTDF GDKVEDPTFL
250 260 270 280 290 300
NQLQSGVNRW IREIQKVTKL DRDPASGTAL QEISFWLNLE RALYRIQEKR ESPEVLLTLD
310 320 330 340 350 360
ILKHGKRFHA TVSFDTDTGL KQALETVNDY NPLMKDFPLN DLLSATELDK IRQALVAIFT
370 380 390 400 410 420
HLRKIRNTKY PIQRALRLVE AISRDLSSQL LKVLGTRKLM HVAYEEFEKV MVACFEVFQT
430 440 450 460 470 480
WDDEYEKLQV LLRDIVKRKR EENLKMVWRI NPAHRKLQAR LDQMRKFRRQ HEQLRAVIVR
490 500 510 520 530 540
VLRPQVTAVA QQNQGEAPEP QDMKVAEVLF DAADANAIEE VNLAYENVKE VDGLDVSKEG
550 560 570 580 590 600
TEAWEAAMKR YDERIDRVET RITARLRDQL GTAKNANEMF RIFSRFNALF VRPHIRGAIR
610 620 630 640 650 660
EYQTQLIQRV KDDIESLHDK FKVQYPQSQA CKMSHVRDLP PVSGSIIWAK QIDRQLTAYM
670 680 690 700 710 720
KRVEDVLGKG WENHVEGQKL KQDGDSFRMK LNTQEIFDDW ARKVQQRNLG VSGRIFTIES
730 740 750 760 770 780
ARVRGRTGNV LKLKVNFLPE IITLSKEVRN LKWLGFRVPL AIVNKAHQAN QLYPFAISLI
790 800 810 820 830 840
ESVRTYERTC EKVEERNTIS LLVAGLKKEV QALIAEGIAL VWESYKLDPY VQRLAETVFN
850 860 870 880 890 900
FQEKVDDLLI IEEKIDLEVR SLETCMYDHK TFSEILNRVQ KAVDDLNLHS YSNLPIWVNK
910 920 930 940 950 960
LDMEIERILG VRLQAGLRAW TQVLLGQAED KAEVDMDTDA PQVSHKPGGE PKIKNVVHEL
970 980 990 1000 1010 1020
RITNQVIYLN PPIEECRYKL YQEMFAWKMV VLSLPRIQSQ RYQVGVHYEL TEEEKFYRNA
1030 1040 1050 1060 1070 1080
LTRMPDGPVA LEESYSAVMG IVTEVEQYVK VWLQYQCLWD MQAENIYNRL GEDLNKWQAL
1090 1100 1110 1120 1130 1140
LVQIRKARGT FDNAETKKEF GPVVIDYGKV QSKVNLKYDS WHKEVLSKFG QMLGSNMTEF
1150 1160 1170 1180 1190 1200
HSQISKSRQE LEQHSVDTAS TSDAVTFITY VQSLKRKIKQ FEKQVELYRN GQRLLEKQRF
1210 1220 1230 1240 1250 1260
QFPPSWLYID NIEGEWGAFN DIMRRKDSAI QQQVANLQMK IVQEDRAVES RTTDLLTDWE
1270 1280 1290 1300 1310 1320
KTKPVTGNLR PEEALQALTI YEGKFGRLKD DREKCAKAKE ALELTDTGLL SGSEERVQVA
1330 1340 1350 1360 1370 1380
LEELQDLKGV WSELSKVWEQ IDQMKEQPWV SVQPRKLRQN LDGLLNQLKN FPARLRQYAS
1390 1400 1410 1420 1430 1440
YEFVQRLLKG YMKINMLVIE LKSEALKDRH WKQLMKRLHV NWVVSELTLG QIWDVDLQKN
1450 1460 1470 1480 1490 1500
EAVVKDVLLV AQGEMALEEF LKQIREVWNT YELDLVNYQN KCRLIRGWDD LFNKVKEHIN
1510 1520 1530 1540 1550 1560
SVSAMKLSPY YKVFEEDALS WEDKLNRIMA LFDVWIDVQR RWVYLEGIFT GSADIKHLLP
1570 1580 1590 1600 1610 1620
VETQRFQSIS TEFLALMKKV SKSPLVMDVL NIQGVQRSLE RLADLLGKIQ KALGEYLERE
1630 1640 1650 1660 1670 1680
RSSFPRFYFV GDEDLLEIIG NSKNVAKLQK HFKKMFAGVS SIILNEDNSV VLGISSREGE
1690 1700 1710 1720 1730 1740
EVMFKTPVSI TEHPKINEWL TLVEKEMRVT LAKLLAESVT EVEIFGKATS IDPNTYITWI
1750 1760 1770 1780 1790 1800
DKYQAQLVVL SAQIAWSENV ENALSNVGGG GDVGPLQSVL SNVEVTLNVL ADSVLMEQPP
1810 1820 1830 1840 1850 1860
LRRRKLEHLI TELVHQRDVT RSLIKSKIDN AKSFEWLSQM RFYFDPKQTD VLQQLSIQMA
1870 1880 1890 1900 1910 1920
NAKFNYGFEY LGVQDKLVQT PLTDRCYLTM TQALEARLGG SPFGPAGTGK TESVKALGHQ
1930 1940 1950 1960 1970 1980
LGRFVLVFNC DETFDFQAMG RIFVGLCQVG AWGCFDEFNR LEERMLSAVS QQVQCIQEAL
1990 2000 2010 2020 2030 2040
REHSNPNYDK TSAPITCELL NKQVKVSPDM AIFITMNPGY AGRSNLPDNL KKLFRSLAMT
2050 2060 2070 2080 2090 2100
KPDRQLIAQV MLYSQGFRTA EVLANKIVPF FKLCDEQLSS QSHYDFGLRA LKSVLVSAGN
2110 2120 2130 2140 2150 2160
VKRERIQKIK REKEERGEAV DEGEIAENLP EQEILIQSVC ETMVPKLVAE DIPLLFSLLS
2170 2180 2190 2200 2210 2220
DVFPGVQYHR GEMTALREEL KKVCQEMYLT YGDGEEVGGM WVEKVLQLYQ ITQINHGLMM
2230 2240 2250 2260 2270 2280
VGPSGSGKSM AWRVLLKALE RLEGVEGVAH IIDPKAISKD HLYGTLDPNT REWTDGLFTH
2290 2300 2310 2320 2330 2340
VLRKIIDNVR GELQKRQWIV FDGDVDPEWV ENLNSVLDDN KLLTLPNGER LSLPPNVRIM
2350 2360 2370 2380 2390 2400
FEVQDLKYAT LATVSRCGMV WFSEDVLSTD MIFNNFLARL RSIPLDEGED EAQRRRKGKE
2410 2420 2430 2440 2450 2460
DEGEEAASPM LQIQRDAATI MQPYFTSNGL VTKALEHAFK LEHIMDLTRL RCLGSLFSML
2470 2480 2490 2500 2510 2520
HQACRNVAQY NANHPDFPMQ IEQLERYIQR YLVYAILWSL SGDSRLKMRA ELGEYIRRIT
2530 2540 2550 2560 2570 2580
TVPLPTAPNV PIIDYEVSIS GEWSPWQAKV PQIEVETHKV AAPDVVVPTL DTVRHEALLY
2590 2600 2610 2620 2630 2640
TWLAEHKPLV LCGPPGSGKT MTLFSALRAL PDMEVVGLNF SSATTPELLL KTFDHYCEYR
2650 2660 2670 2680 2690 2700
RTPNGVVLAP VQLGKWLVLF CDEINLPDMD KYGTQRVISF IRQMVEHGGF YRTSDQTWVK
2710 2720 2730 2740 2750 2760
LERIQFVGAC NPPTDPGRKP LSHRFLRHVP VVYVDYPGPA SLTQIYGTFN RAMLRLIPSL
2770 2780 2790 2800 2810 2820
RTYAEPLTAA MVEFYTMSQE RFTQDTQPHY IYSPREMTRW VRGIFEALRP LETLPVEGLI
2830 2840 2850 2860 2870 2880
RIWAHEALRL FQDRLVEDEE RRWTDENIDM VALKHFPNID KEKAMSRPIL YSNWLSKDYI
2890 2900 2910 2920 2930 2940
PVDQEELRDY VKARLKVFYE EELDVPLVLF NEVLDHVLRI DRIFRQPQGH LLLIGVSGAG
2950 2960 2970 2980 2990 3000
KTTLSRFVAW MNGLSVYQIK VHRKYTGEDF DEDLRTVLRR SGCKNEKIAF IMDESNVLDS
3010 3020 3030 3040 3050 3060
GFLERMNTLL ANGEVPGLFE GDEYATLMTQ CKEGAQKEGL MLDSHEELYK WFTSQVIRNL
3070 3080 3090 3100 3110 3120
HVVFTMNPSS EGLKDRAATS PALFNRCVLN WFGDWSTEAL YQVGKEFTSK MDLEKPNYIV
3130 3140 3150 3160 3170 3180
PDYMPVVYDK LPQPPTHREA IVNSCVFVHQ TLHQANARLA KRGGRTMAIT PRHYLDFINH
3190 3200 3210 3220 3230 3240
YANLFHEKRS ELEEQQMHLN VGLRKIKETV DQVEELRRDL RIKSQELEVK NAAANDKLKK
3250 3260 3270 3280 3290 3300
MVKDQQEAEK KKVMSQEIQE QLHKQQEVIA DKQMSVKEDL DKVEPAVIEA QNAVKSIKKQ
3310 3320 3330 3340 3350 3360
HLVEVRSMAN PPAAVKLALE SICLLLGEST TDWKQIRSII MRENFIPTIV NFSAEEISDA
3370 3380 3390 3400 3410 3420
IREKMKKNYM SNPSYNYEIV NRASLACGPM VKWAIAQLNY ADMLKRVEPL RNELQKLEDD
3430 3440 3450 3460 3470 3480
AKDNQQKANE VEQMIRDLEA SIARYKEEYA VLISEAQAIK ADLAAVEAKV NRSTALLKSL
3490 3500 3510 3520 3530 3540
SAERERWEKT SETFKNQMST IAGDCLLSAA FIAYAGYFDQ QMRQNLFTTW SHHLQQANIQ
3550 3560 3570 3580 3590 3600
FRTDIARTEY LSNADERLRW QASSLPADDL CTENAIMLKR FNRYPLIIDP SGQATEFIMN
3610 3620 3630 3640 3650 3660
EYKDRKITRT SFLDDAFRKN LESALRFGNP LLVQDVESYD PVLNPVLNRE VRRTGGRVLI
3670 3680 3690 3700 3710 3720
TLGDQDIDLS PSFVIFLSTR DPTVEFPPDL CSRVTFVNFT VTRSSLQSQC LNEVLKAERP
3730 3740 3750 3760 3770 3780
DVDEKRSDLL KLQGEFQLRL RQLEKSLLQA LNEVKGRILD DDTIITTLEN LKREAAEVTR
3790 3800 3810 3820 3830 3840
KVEETDIVMQ EVETVSQQYL PLSTACSSIY FTMESLKQVH FLYQYSLQFF LDIYHNVLYE
3850 3860 3870 3880 3890 3900
NPNLKGATDH TQRLSIITKD LFQVAFNRVA RGMLHQDHIT FAMLLARIKL KGTVGEPTYD
3910 3920 3930 3940 3950 3960
AEFQHFLRGK EIVLSAGSTP KIQGLTVEQA EAVVRLSCLP AFKDLIAKVQ ADEQFGIWLD
3970 3980 3990 4000 4010 4020
SSSPEQTVPY LWSEETPTTP IGQAIHRLLL IQAFRPDRLL AMAHMFVSTN LGESFMSIME
4030 4040 4050 4060 4070 4080
QPLDLTHIVG TEVKPNTPVL MCSVPGYDAS GHVEDLAAEQ NTQITSIAIG SAEGFNQADK
4090 4100 4110 4120 4130 4140
AINTAVKSGR WVMLKNVHLA PGWLMQLEKK LHSLQPHACF RLFLTMEINP KVPVNLLRAG
4150 4160 4170 4180 4190 4200
RIFVFEPPPG VKANMLRTFS SIPVSRICKS PNERARLYFL LAWFHAIIQE RLRYAPLGWS
4210 4220 4230 4240 4250 4260
KKYEFGESDL RSACDTVDTW LDDTAKGRQN ISPDKIPWSA LKTLMAQSIY GGRVDNEFDQ
4270 4280 4290 4300 4310 4320
RLLNTFLERL FTTRSFDSEF KLACKVDGHK DIQMPDGIRR EEFVQWVELL PDAQTPSWLG
4330 4340 4350 4360 4370 4380
LPNNAERVLL TTQGVDMISK MLKMQMLEDE DDLAYAETEK KARTDSTSDG RPAWMRTLHT
4390 4400 4410 4420 4430 4440
TASNWLHLIP QTLSPLKRTV ENIKDPLFRF FEREVKMGAK LLQDVRQDLA DVVQVCEGKK
4450 4460 4470 4480 4490 4500
KQTNYLRTLI NELVKGILPR SWSHYTVPAG MTVIQWVSDF SERIKQLQNI SQAAASGGAK
4510 4520 4530 4540 4550 4560
ELKNIHVCLG GLFVPEAYIT ATRQYVAQAN SWSLEELCLE VNVTASQSAT LDACSFGVTG
4570 4580 4590 4600 4610 4620
LKLQGATCSN NKLSLSNAIS TVLPLTQLRW VKQTSAEKKA SVVTLPVYLN FTRADLIFTV
4630 4640
DFEIATKEDP RSFYERGVAV LCTE