Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

4 structures for Q62261

Entry ID Method Resolution Chain Position Source
1BTN X-ray 200 A A 2199-2304 PDB
1MPH NMR - A 2199-2304 PDB
6M3P X-ray 331 A A/B 1591-1910 PDB
AF-Q62261-F1 Predicted AlphaFoldDB

134 variants for Q62261

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389142740 22 N>S No EVA
rs3389122360 43 S>T No EVA
rs3389140583 50 D>E No EVA
rs3402092595 97 G>A No EVA
rs3401998282 97 G>R No EVA
rs3389110646 113 L>M No EVA
rs1133979608 209 N>I No EVA
rs3402278517 257 S>R No EVA
rs3400804937 259 D>V No EVA
rs3389118849 297 A>T No EVA
rs3389118821 303 M>I No EVA
rs3389142714 304 I>N No EVA
rs3389157057 308 E>D No EVA
rs3389149777 336 G>E No EVA
rs3401430662 361 N>Y No EVA
rs3389134530 365 L>P No EVA
rs3389140615 407 E>G No EVA
rs3389145432 421 E>D No EVA
rs3400804959 513 L>F No EVA
rs3389110645 586 G>S No EVA
rs3389086840 603 P>A No EVA
rs3402092641 617 E>A No EVA
rs3389134556 633 R>P No EVA
rs3389122416 703 D>H No EVA
rs3389149821 723 R>L No EVA
rs3389153878 753 A>D No EVA
rs3389142682 754 D>G No EVA
rs3389140641 760 M>L No EVA
rs3402728406 775 D>V No EVA
rs213662865 802 T>A No EVA
rs3389159362 818 P>S No EVA
rs3389086819 821 K>T No EVA
rs3389146531 825 A>V No EVA
rs3389122434 863 L>P No EVA
rs3389145451 866 D>N No EVA
rs3402010736 882 E>D No EVA
rs3401917740 885 E>Q No EVA
rs3402017729 887 I>L No EVA
rs3389142716 890 R>G No EVA
rs3389118786 907 V>M No EVA
rs3389149845 911 I>F No EVA
rs3389140632 929 Q>K No EVA
rs3389142699 936 R>M No EVA
rs3389110701 949 D>E No EVA
rs3401430681 953 S>A No EVA
rs3402157014 953 S>Y No EVA
rs3401657430 955 L>Q No EVA
rs3410353345 956 S>G No EVA
rs3401792935 957 I>S No EVA
rs3389159351 970 W>C No EVA
rs3389086873 973 E>D No EVA
rs256713181 982 Q>H No EVA
rs3389110647 1004 D>A No EVA
rs3389153827 1030 A>V No EVA
rs3402109883 1037 L>P No EVA
rs3389145471 1085 I>F No EVA
rs3389145470 1088 E>D No EVA
rs3389145448 1109 N>H No EVA
rs3389140573 1109 N>I No EVA
rs3389118838 1134 D>N No EVA
rs3389122347 1140 L>P No EVA
rs3389149399 1156 K>R No EVA
rs3389146506 1167 Q>H No EVA
rs3389157046 1178 T>I No EVA
rs3389159334 1192 L>F No EVA
rs3389086883 1192 L>S No EVA
rs3389122383 1196 E>D No EVA
rs3389118802 1213 D>E No EVA
rs3389149442 1217 T>I No EVA
rs3389157005 1228 V>SDG* No EVA
rs3389146671 1237 S>N No EVA
rs3389157092 1247 Q>R No EVA
rs26875745 1249 K>R No EVA
rs3389142741 1255 D>N No EVA
rs3400804984 1269 M>* No EVA
rs3400804958 1273 D>V No EVA
rs3402278506 1276 D>H No EVA
rs3389149795 1303 Y>C No EVA
rs3389159326 1337 G>V No EVA
rs3389149822 1355 L>V No EVA
rs3389122423 1356 T>N No EVA
rs3389153915 1361 M>T No EVA
rs3389157008 1364 V>I No EVA
rs3389134504 1373 A>V No EVA
rs3389122378 1381 K>M No EVA
rs3389086824 1403 I>F No EVA
rs3389110697 1407 D>N No EVA
rs3389086861 1433 K>R No EVA
rs3389157076 1461 L>P No EVA
rs3389134467 1469 E>V No EVA
rs3389110710 1475 S>T No EVA
rs3389149837 1572 Q>* No EVA
rs3389145497 1598 Y>* No EVA
rs3389142768 1611 Q>E No EVA
rs3389140556 1616 M>L No EVA
rs3412161923 1668 R>H No EVA
rs3389146527 1698 H>Y No EVA
rs3401998319 1709 D>E No EVA
rs3389159390 1722 G>D No EVA
rs3389118822 1734 T>M No EVA
rs3389122364 1818 F>Y No EVA
rs3389157058 1832 L>F No EVA
rs13459831 1898 D>G No EVA
rs3389142748 1908 V>E No EVA
rs3389159371 1967 F>S No EVA
rs3389159352 2003 I>T No EVA
rs3389145467 2012 W>C No EVA
rs3389142688 2013 L>F No EVA
rs3389086866 2048 S>* No EVA
rs3389157080 2050 D>E No EVA
rs3389134524 2053 E>G No EVA
rs3389146561 2053 E>K No EVA
rs3389145463 2073 F>I No EVA
rs3389146530 2101 P>H No EVA
rs3389118801 2138 P>L No EVA
rs13473735 2171 L>S No EVA
rs255747867 2172 D>N No EVA
rs242852230 2181 A>S No EVA
rs3389157012 2182 Q>E No EVA
rs3389146701 2201 G>R No EVA
rs3389157013 2202 F>V No EVA
rs3389149191 2203 L>P No EVA
rs3389140611 2207 H>N No EVA
rs3389086849 2207 H>Q No EVA
rs3389153831 2209 W>* No EVA
rs3389159391 2213 N>D No EVA
rs3389147914 2216 A>T No EVA
rs3389145483 2219 R>S No EVA
rs3402070452 2224 V>I No EVA
rs3402277692 2225 Y>H No EVA
rs3401394566 2227 V>A No EVA
rs3389146689 2237 K>E No EVA
rs3389146730 2259 A>S No EVA
rs3389086811 2282 N>Y No EVA

2 associated diseases with Q62261

[MIM: 614893]: Immunodeficiency 32A (IMD32A)

An immunologic disorder characterized by abnormal peripheral blood myeloid phenotype with a marked loss of CD11C-positive/CD1C dendritic cells, resulting in selective susceptibility to mycobacterial infections. {ECO:0000269|PubMed:21524210}. Note=The disease is caused by variants affecting the gene represented in this entry.

[MIM: 226990]: Immunodeficiency 32B (IMD32B)

An autosomal recessive primary immunodeficiency characterized by monocyte and dendritic cell deficiency, myeloproliferation, and susceptibility to severe opportunistic infections, including disseminated BCG infection and oral candidiasis. {ECO:0000269|PubMed:21524210, ECO:0000269|PubMed:25122610}. Note=The disease is caused by variants affecting the gene represented in this entry.

Without disease ID
  • An immunologic disorder characterized by abnormal peripheral blood myeloid phenotype with a marked loss of CD11C-positive/CD1C dendritic cells, resulting in selective susceptibility to mycobacterial infections. {ECO:0000269|PubMed:21524210}. Note=The disease is caused by variants affecting the gene represented in this entry.
  • An autosomal recessive primary immunodeficiency characterized by monocyte and dendritic cell deficiency, myeloproliferation, and susceptibility to severe opportunistic infections, including disseminated BCG infection and oral candidiasis. {ECO:0000269|PubMed:21524210, ECO:0000269|PubMed:25122610}. Note=The disease is caused by variants affecting the gene represented in this entry.

2 regional properties for Q62261

Type Name Position InterPro Accession
domain Pancreatic trypsin inhibitor Kunitz domain 33 - 87 IPR002223
conserved_site Proteinase inhibitor I2, Kunitz, conserved site 64 - 82 IPR020901

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytoskeleton
  • Endomembrane system
  • Cytoplasm, myofibril, sarcomere, M line
  • Cytoplasm, cytosol
  • Cell membrane
  • Colocalizes with ANK2 in a distinct intracellular compartment of neonatal cardiomyocytes
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

19 GO annotations of cellular component

Name Definition
axolemma The portion of the plasma membrane surrounding an axon; it is a specialized trilaminar random mosaic of protein molecules floating within a fluid matrix of highly mobile phospholipid molecules, 7-8 nm in thickness.
cell junction A cellular component that forms a specialized region of connection between two or more cells, or between a cell and the extracellular matrix, or between two membrane-bound components of a cell, such as flagella.
cell projection A prolongation or process extending from a cell, e.g. a flagellum or axon.
cortical actin cytoskeleton The portion of the actin cytoskeleton, comprising filamentous actin and associated proteins, that lies just beneath the plasma membrane.
cortical cytoskeleton The portion of the cytoskeleton that lies just beneath the plasma membrane.
cuticular plate A dense network of actin filaments found beneath the apical cell surface of hair cells, and into which stereocilia are inserted.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
endomembrane system A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles.
glutamatergic synapse A synapse that uses glutamate as a neurotransmitter.
M band The midline of aligned thick filaments in a sarcomere; location of specific proteins that link thick filaments. Depending on muscle type the M band consists of different numbers of M lines.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
postsynapse The part of a synapse that is part of the post-synaptic cell.
postsynaptic density An electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
spectrin Membrane associated dimeric protein (240 and 220 kDa) of erythrocytes. Forms a complex with ankyrin, actin and probably other components of the membrane cytoskeleton, so that there is a mesh of proteins underlying the plasma membrane, potentially restricting the lateral mobility of integral proteins.

7 GO annotations of molecular function

Name Definition
actin filament binding Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
ankyrin binding Binding to ankyrin, a 200 kDa cytoskeletal protein that attaches other cytoskeletal proteins to integral membrane proteins.
calmodulin binding Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
GTPase binding Binding to a GTPase, any enzyme that catalyzes the hydrolysis of GTP.
phospholipid binding Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester.
protein-containing complex binding Binding to a macromolecular complex.
structural constituent of cytoskeleton The action of a molecule that contributes to the structural integrity of a cytoskeletal structure.

14 GO annotations of biological process

Name Definition
actin cytoskeleton organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
actin filament capping The binding of a protein or protein complex to the end of an actin filament, thus preventing the addition, exchange or removal of further actin subunits.
central nervous system development The process whose specific outcome is the progression of the central nervous system over time, from its formation to the mature structure. The central nervous system is the core nervous system that serves an integrating and coordinating function. In vertebrates it consists of the brain and spinal cord. In those invertebrates with a central nervous system it typically consists of a brain, cerebral ganglia and a nerve cord.
central nervous system formation The process that gives rise to the central nervous system. This process pertains to the initial formation of a structure from unspecified parts. The central nervous system is the core nervous system that serves an integrating and coordinating function. In vertebrates it consists of the brain, spinal cord and spinal nerves. In those invertebrates with a central nervous system it typically consists of a brain, cerebral ganglia and a nerve cord.
common-partner SMAD protein phosphorylation The process of introducing a phosphate group on to a common-partner SMAD protein. A common partner SMAD protein binds to pathway-restricted SMAD proteins forming a complex that translocates to the nucleus.
Golgi to plasma membrane protein transport The directed movement of proteins from the Golgi to the plasma membrane in transport vesicles that move from the trans-Golgi network to the plasma membrane.
membrane assembly The aggregation, arrangement and bonding together of a set of components to form a membrane.
mitotic cytokinesis A cell cycle process that results in the division of the cytoplasm of a cell after mitosis, resulting in the separation of the original cell into two daughter cells.
plasma membrane organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the plasma membrane.
positive regulation of interleukin-2 production Any process that activates or increases the frequency, rate, or extent of interleukin-2 production.
positive regulation of protein localization to plasma membrane Any process that activates or increases the frequency, rate or extent of protein localization to plasma membrane.
protein localization to plasma membrane A process in which a protein is transported to, or maintained in, a specific location in the plasma membrane.
regulation of protein localization to plasma membrane Any process that modulates the frequency, rate or extent of protein localization to plasma membrane.
regulation of SMAD protein signal transduction Any process that modulates the rate, frequency or extent of SMAD protein signal transduction. Pathway-restricted SMAD proteins and common-partner SMAD proteins are involved in the transforming growth factor beta receptor signaling pathways.

9 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O15020 SPTBN2 Spectrin beta chain, non-erythrocytic 2 Homo sapiens (Human) PR
P11277 SPTB Spectrin beta chain, erythrocytic Homo sapiens (Human) PR
Q01082 SPTBN1 Spectrin beta chain, non-erythrocytic 1 Homo sapiens (Human) PR
Q9JI91 Actn2 Alpha-actinin-2 Mus musculus (Mouse) SS
O88990 Actn3 Alpha-actinin-3 Mus musculus (Mouse) SS
P57780 Actn4 Alpha-actinin-4 Mus musculus (Mouse) SS
Q7TPR4 Actn1 Alpha-actinin-1 Mus musculus (Mouse) SS
P15508 Sptb Spectrin beta chain, erythrocytic Mus musculus (Mouse) PR
Q9QWN8 Sptbn2 Spectrin beta chain, non-erythrocytic 2 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD EREAVQKKTF
70 80 90 100 110 120
TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL PKPTKGRMRI HCLENVDKAL
130 140 150 160 170 180
QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI WTIILRFQIQ DISVETEDNK EKKSAKDALL
190 200 210 220 230 240
LWCQMKTAGY PNVNIHNFTT SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL
250 260 270 280 290 300
AEQHLGLTKL LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET
310 320 330 340 350 360
EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV EKPPKFTEKG
370 380 390 400 410 420
NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE KAEHERELAL RNELIRQEKL
430 440 450 460 470 480
EQLARRFDRK AAMRETWLSE NQRLVSQDNF GFDLPAVEAA TKKHEAIETD IAAYEERVQA
490 500 510 520 530 540
VVAVARELEA ENYHDIKRIT ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI
550 560 570 580 590 600
MDWMDEMKVL LLSQDYGKHL LGVEDLLQKH ALVEADIAIQ AERVRGVNAS AQKFATDGEG
610 620 630 640 650 660
YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE EGWIREKEKI
670 680 690 700 710 720
LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE GEDMIAEEHF GSEKIRERII
730 740 750 760 770 780
YIREQWANLE QLSAIRKKRL EEASLLHQFQ ADADDIDAWM LDILKIVSSN DVGHDEYSTQ
790 800 810 820 830 840
SLVKKHKDVA EEITNYRPTI DTLHEQASAL PQAHAESPDV KGRLAGIEER CKEMAELTRL
850 860 870 880 890 900
RKQALQDTLA LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN
910 920 930 940 950 960
QASRVAVVNQ IARQLMHNGH PSEKEIRAQQ DKLNTRWSQF RELVDRKKDA LLSALSIQNY
970 980 990 1000 1010 1020
HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG MERDLVAIEA KLSDLQKEAE
1030 1040 1050 1060 1070 1080
KLESEHPDQA QAILSRLAEI SDVWEEMKTT LKNREASLGE ASKLQQFLRD LDDFQSWLSR
1090 1100 1110 1120 1130 1140
TQTAIASEDM PNTLTEAEKL LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL
1150 1160 1170 1180 1190 1200
RQRLQALDTG WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT
1210 1220 1230 1240 1250 1260
LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV DSIDDRHRKN
1270 1280 1290 1300 1310 1320
REAASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD MSYDEARNLH SKWLKHQAFM
1330 1340 1350 1360 1370 1380
AELASNKEWL DKIEKEGMQL ISEKPETEAV VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN
1390 1400 1410 1420 1430 1440
KAELFTQSCA DLDKWLHGLE SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ
1450 1460 1470 1480 1490 1500
SQAQALSQEG KSTDEVDSKR LTVQTKFMEL LEPLSERKHN LLASKEIHQF NRDVEDEILW
1510 1520 1530 1540 1550 1560
VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN IITDSSSLNA
1570 1580 1590 1600 1610 1620
EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHKAQQYYFD AAEAEAWMSE QELYMMSEEK
1630 1640 1650 1660 1670 1680
AKDEQSAVSM LKKHQILEQA VEDYAETVHQ LSKTSRALVA DSHPESERIS MRQSKVDKLY
1690 1700 1710 1720 1730 1740
AGLKDLAEER RGKLDERHRL FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF
1750 1760 1770 1780 1790 1800
REFARDTGNI GQERVDTVNN MADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI
1810 1820 1830 1840 1850 1860
LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE HDIQALGTQV
1870 1880 1890 1900 1910 1920
RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC EGRRVRLVDT GDKFRFFSMV
1930 1940 1950 1960 1970 1980
RDLMLWMEDV IRQIEAQEKP RDVSSVELLM NNHQGIKAEI DARNDSFTAC IELGKSLLAR
1990 2000 2010 2020 2030 2040
KHYASEEIKE KLLQLTEKRK EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL
2050 2060 2070 2080 2090 2100
SSREIGQSVD EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP
2110 2120 2130 2140 2150 2160
PSPDPNTKVS EEAESQQWDT SKGDQVSQNG LPAEQGSPRM AGTMETSEMV NGAAEQRTSS
2170 2180 2190 2200 2210 2220
KESSPVPSPT LDRKAKSALP AQSAATLPAR TLETPAAQME GFLNRKHEWE AHNKKASSRS
2230 2240 2250 2260 2270 2280
WHNVYCVINN QEMGFYKDAK SAASGIPYHS EVPVSLKEAI CEVALDYKKK KHVFKLRLSD
2290 2300 2310 2320 2330 2340
GNEYLFQAKD DEEMNTWIQA ISSAISSDKH DTSASTQSTP ASSRAQTLPT SVVTITSESS
2350 2360
PGKREKDKEK DKEKRFSLFG KKK