Q02357

SS
Gene name
Ank1 (Ank-1)
Protein name
Ankyrin-1
Names
ANK-1 , Erythrocyte ankyrin
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:11733
EC number
Protein Class

Descriptions

Ankyrin-R (AnkR) is a scaffold protein involved in connecting various ion channels and cell adhesion molecules to the spectrin-based cytoskeleton. It plays essential roles in maintaining plasma membrane integrity and coordinating physiological activities in the nervous and cardiovascular systems. AnkR undergoes autoinhibition through a 48-residue autoinhibitory segment within its C-terminal regulatory domain, which binds to the N-terminal ankyrin repeat (ANK) domain, preventing interactions with membrane targets. This autoinhibition is relieved by LF mutation in site-3 that releases the autoinhibitory segment from the ANK repeats, allowing AnkR to bind to its targets.

Autoinhibitory domains (AIDs)

1573-1619 (autoinhibitory segment) SS

Target domain

3-823 (ANK domain)

Relief mechanism

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q02357

Entry ID Method Resolution Chain Position Source
AF-Q02357-F1 Predicted AlphaFoldDB

No variants for Q02357

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q02357

No associated diseases with Q02357

16 regional properties for Q02357

Type Name Position InterPro Accession
domain Death domain 1389 - 1483 IPR000488
domain ZU5 domain 907 - 1064 IPR000906-1
domain ZU5 domain 1066 - 1212 IPR000906-2
repeat Ankyrin repeat 7 - 105 IPR002110-1
repeat Ankyrin repeat 106 - 138 IPR002110-2
repeat Ankyrin repeat 139 - 167 IPR002110-3
repeat Ankyrin repeat 168 - 233 IPR002110-4
repeat Ankyrin repeat 234 - 266 IPR002110-5
repeat Ankyrin repeat 267 - 365 IPR002110-6
repeat Ankyrin repeat 366 - 431 IPR002110-7
repeat Ankyrin repeat 432 - 497 IPR002110-8
repeat Ankyrin repeat 498 - 593 IPR002110-9
repeat Ankyrin repeat 597 - 629 IPR002110-10
repeat Ankyrin repeat 630 - 728 IPR002110-11
repeat Ankyrin repeat 729 - 761 IPR002110-12
domain Ankyrin, UPA domain 1232 - 1360 IPR040745

Functions

Description
EC Number
Subcellular Localization
  • [Isoform Er1]: Cytoplasm, cytoskeleton
  • Probably the other erythrocyte (Er) isoforms, are located near the surface of erythrocytic plasma membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

13 GO annotations of cellular component

Name Definition
A band The dark-staining region of a sarcomere, in which myosin thick filaments are present; the center is traversed by the paler H zone, which in turn contains the M line.
ankyrin-1 complex A complex composed of ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPA, GYPB and AQP1, that functions in the stability and shape of the erythrocyte membrane in human.
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.
cortical cytoskeleton The portion of the cytoskeleton that lies just beneath the plasma membrane.
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 and attached to it.
neuron projection A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
postsynaptic membrane A specialized area of membrane facing the presynaptic membrane on the tip of the nerve ending and separated from it by a minute cleft (the synaptic cleft). Neurotransmitters cross the synaptic cleft and transmit the signal to the postsynaptic membrane.
sarcolemma The outer membrane of a muscle cell, consisting of the plasma membrane, a covering basement membrane (about 100 nm thick and sometimes common to more than one fiber), and the associated loose network of collagen fibers.
sarcoplasmic reticulum A fine reticular network of membrane-limited elements that pervades the sarcoplasm of a muscle cell; continuous over large portions of the cell and with the nuclear envelope; that part of the endoplasmic reticulum specialized for calcium release, uptake and storage.
spectrin-associated cytoskeleton The part of the cytoskeleton composed of spectrin, protein 4.1 and ankyrin. Spectrin-associated cytoskeleton is associated with the plasma membrane.
Z disc Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.

3 GO annotations of molecular function

Name Definition
cytoskeletal anchor activity The binding activity of a protein that brings together a cytoskeletal protein (either a microtubule or actin filament, spindle pole body, or protein directly bound to them) and one or more other molecules, permitting them to function in a coordinated way.
spectrin binding Binding to spectrin, a protein that is the major constituent of the erythrocyte cytoskeletal network. It associates with band 4.1 (see band protein) and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. It is composed of nonhomologous chains, alpha and beta, which aggregate side-to-side in an antiparallel fashion to form dimers, tetramers, and higher polymers.
transmembrane transporter binding Binding to a transmembrane transporter, a protein or protein complex that enables the transfer of a substance, usually a specific substance or a group of related substances, from one side of a membrane to the other.

7 GO annotations of biological process

Name Definition
erythrocyte development The process whose specific outcome is the progression of an erythrocyte over time, from its formation to the mature structure.
inorganic cation transmembrane transport A process in which an inorganic cation is transported from one side of a membrane to the other by means of some agent such as a transporter or pore.
multicellular organismal-level iron ion homeostasis A chemical homeostatic process involved in the maintenance of a steady state level of iron within extracellular body fluids, such as blood, xylem or phloem, of a multicellular organism. This is distinct from maintenance of cellular homeostasis, which occurs within a cell.
porphyrin-containing compound biosynthetic process The chemical reactions and pathways resulting in the formation of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
positive regulation of organelle organization Any process that increases the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of an organelle.
protein localization to plasma membrane A process in which a protein is transported to, or maintained in, a specific location in the plasma membrane.
signal transduction The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.

12 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
F1N6G5 HACE1 E3 ubiquitin-protein ligase HACE1 Bos taurus (Bovine) SS
E1C656 HACE1 E3 ubiquitin-protein ligase HACE1 Gallus gallus (Chicken) SS
Q8IYU2 HACE1 E3 ubiquitin-protein ligase HACE1 Homo sapiens (Human) EV
Q12955 ANK3 Ankyrin-3 Homo sapiens (Human) SS
Q01484 ANK2 Ankyrin-2 Homo sapiens (Human) EV
P16157 ANK1 Ankyrin-1 Homo sapiens (Human) EV
Q3U0D9 Hace1 E3 ubiquitin-protein ligase HACE1 Mus musculus (Mouse) SS
Q8C8R3 Ank2 Ankyrin-2 Mus musculus (Mouse) SS
D3ZBM7 Hace1 E3 ubiquitin-protein ligase HACE1 Rattus norvegicus (Rat) SS
O70511 Ank3 Ankyrin-3 Rattus norvegicus (Rat) EV
Q28BK1 hace1 E3 ubiquitin-protein ligase HACE1 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) SS
F8W2M1 hace1 E3 ubiquitin-protein ligase HACE1 Danio rerio (Zebrafish) (Brachydanio rerio) SS
10 20 30 40 50 60
MGFCKADAAT SFLRAARSGN LDKALDHLRN GVDINTCNQN GLNGLHLASK EGHVKMVVEL
70 80 90 100 110 120
LHKEIILETT TKKGNTALHI AALAGQDEVV RELVNYGANV NAQSQKGFTP LYMAAQENHL
130 140 150 160 170 180
EVVKFLLENG ANQNVATEDG FTPLAVALQQ GHENVVAHLI NYGTKGKVRL PALHIAARND
190 200 210 220 230 240
DTRTAAVLLQ NDPNPDVLSK TGFTPLHIAA HYENLNVAQL LLNRGASVNF TPQNGITPLH
250 260 270 280 290 300
IASRRGNVIM VRLLLDRGAQ IETRTKDELT PLHCAARNGH VRISEILLDH GAPIQAKTKN
310 320 330 340 350 360
GLSPIHMAAQ GDHLDCVRLL LQYNAEIDDI TLDHLTPLHV AAHCGHHRVA KVLLDKGAKP
370 380 390 400 410 420
NSRALNGFTP LHIACKKNHI RVMELLLKTG ASIDAVTESG LTPLHVASFM GHLPIVKNLL
430 440 450 460 470 480
QRGASPNVSN VKVETPLHMA ARAGHTEVAK YLLQNKAKAN AKAKDDQTPL HCAARIGHTG
490 500 510 520 530 540
MVKLLLENGA SPNLATTAGH TPLHTAAREG HVDTALALLE KEASQACMTK KGFTPLHVAA
550 560 570 580 590 600
KYGKVRLAEL LLEHDAHPNA AGKNGLTPLH VAVHHNNLDI VKLLLPRGGS PHSPAWNGYT
610 620 630 640 650 660
PLHIAAKQNQ IEVARSLLQY GGSANAESVQ GVTPLHLAAQ EGHTEMVALL LSKQANGNLG
670 680 690 700 710 720
NKSGLTPLHL VSQEGHVPVA DVLIKHGVTV DATTRMGYTP LHVASHYGNI KLVKFLLQHQ
730 740 750 760 770 780
ADVNAKTKLG YSPLHQAAQQ GHTDIVTLLL KNGASPNEVS SNGTTPLAIA KRLGYISVTD
790 800 810 820 830 840
VLKVVTDETS VVLVSDKHRM SYPETVDEIL DVSEDEGDEL VGSKAERRDS RDVGEEKELL
850 860 870 880 890 900
DFVPKLDQVV ESPAIPRIPC VTPETVVIRS EDQEQASKEY DEDSLIPSSP ATETSDNISP
910 920 930 940 950 960
VASPVHTGFL VSFMVDARGG SMRGSRHNGL RVVIPPRTCA APTRITCRLV KPQKLNTPPP
970 980 990 1000 1010 1020
LAEEEGLASR IIALGPTGAQ FLSPVIVEIP HFASHGRGDR ELVVLRSENG SVWKEHKSRY
1030 1040 1050 1060 1070 1080
GESYLDQILN GMDEELGSLE ELEKKRVCRI ITTDFPLYFV IMSRLCQDYD TIGPEGGSLR
1090 1100 1110 1120 1130 1140
SKLVPLVQAT FPENAVTKKV KLALQAQPVP DELVTKLLGN QATFSPIVTV EPRRRKFHRP
1150 1160 1170 1180 1190 1200
IGLRIPLPPS WTDNPRDSGE GDTTSLRLLC SVIGGTDQAQ WEDITGTTKL IYANECANFT
1210 1220 1230 1240 1250 1260
TNVSARFWLS DCPRTAEAVH FATLLYKELT AVPYMAKFVI FAKMNDAREG RLRCYCMTDD
1270 1280 1290 1300 1310 1320
KVDKTLEQHE NFVEVARSRD IEVLEGMPLF AELSGNLVPV KKAAQQRSFH FQSFRENRLA
1330 1340 1350 1360 1370 1380
IPVKVRDSSR EPGGFLSFLR KTMKYEDTQH ILCHLNITMP PCTKGSGAED RRRTLTPLTL
1390 1400 1410 1420 1430 1440
RYSILSESRL GFTSDTDRVE MRMAVIREHL GLSWAELARE LQFSVEDINR IRVENPNSLL
1450 1460 1470 1480 1490 1500
DQSTALLTLW VDREGENAKM ENLYTALRNI DRSEIVNMLE GSGRQSRNLK PERRHGDREY
1510 1520 1530 1540 1550 1560
SLSPSQVNGY SSLQDELLSP ASLQYALPSP LCADQYWNEV TVIDAIPLAA TEHDTMLEMS
1570 1580 1590 1600 1610 1620
DMQVWSAGLT PSLVTAEDSS LECSKAEDSD AIPEWKLEGA HSEDTQGPEL GSQDLVEDDT
1630 1640 1650 1660 1670 1680
VDSDATNGLA DLLGQEEGQR SEKKRQEVSG TEQDTETEVS LVSGQQRVHA RITDSPSVRQ
1690 1700 1710 1720 1730 1740
VLDRSQARTL DWDKQGSTAV HPQEATQSSW QEEVTQGPHS FQRRITTIQG PEPGALQEYE
1750 1760 1770 1780 1790 1800
QVLVSTREHV QRGPPETGSP KAGKEPSLWA PESAFSQEVQ GDELQNIPGE QVTEEQFTDE
1810 1820 1830 1840 1850 1860
QGNIVTKKII RKVVRQVDSS GAIDTQQHEE VELRGSGLQP DLIEGRKGAQ IVKRASLKRG
KQ