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Q9EPK8

- TRPV4_MOUSE

UniProt

Q9EPK8 - TRPV4_MOUSE

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Protein

Transient receptor potential cation channel subfamily V member 4

Gene

Trpv4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Non-selective calcium permeant cation channel probably involved in osmotic sensitivity and mechanosensitivity. Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification. Also activated by low pH, citrate and phorbol esters. Increase of intracellular Ca2+ potentiates currents. Channel activity seems to be regulated by a calmodulin-dependent mechanism with a negative feedback mechanism. Acts as a regulator of intracellular Ca2+ in synoviocytes. Plays an obligatory role as a molecular component in the nonselective cation channel activation induced by 4-alpha-phorbol 12,13-didecanoate and hypotonic stimulation in synoviocytes and also regulates production of IL-8 (By similarity). Promotes cell-cell junction formation in skin keratinocytes and plays an important role in the formation and/or maintenance of functional intercellular barriers.By similarity3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei192 – 1921ATPBy similarity
Binding sitei201 – 2011ATPBy similarity
Binding sitei239 – 2391ATPBy similarity
Binding sitei248 – 2481ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium channel activity Source: UniProtKB
  3. calmodulin binding Source: UniProtKB
  4. cation channel activity Source: UniProtKB
  5. osmosensor activity Source: MGI
  6. protein kinase binding Source: BHF-UCL
  7. SH2 domain binding Source: BHF-UCL

GO - Biological processi

  1. actin cytoskeleton reorganization Source: Ensembl
  2. actin filament organization Source: Ensembl
  3. calcium ion import Source: BHF-UCL
  4. cell-cell junction assembly Source: UniProtKB
  5. cellular calcium ion homeostasis Source: UniProtKB
  6. cellular hypotonic response Source: BHF-UCL
  7. cellular response to heat Source: UniProtKB
  8. cellular response to osmotic stress Source: UniProtKB
  9. cortical microtubule organization Source: Ensembl
  10. hyperosmotic salinity response Source: MGI
  11. microtubule polymerization Source: Ensembl
  12. negative regulation of neuron projection development Source: Ensembl
  13. osmosensory signaling pathway Source: BHF-UCL
  14. positive regulation of cytosolic calcium ion concentration Source: Ensembl
  15. positive regulation of microtubule depolymerization Source: Ensembl
  16. regulation of response to osmotic stress Source: MGI
  17. response to osmotic stress Source: MGI
  18. vasopressin secretion Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Calcium, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_227861. TRP channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Transient receptor potential cation channel subfamily V member 4
Short name:
TrpV4
Alternative name(s):
Osm-9-like TRP channel 4
Short name:
OTRPC4
Transient receptor potential protein 12
Short name:
TRP12
Vanilloid receptor-like channel 2
Vanilloid receptor-like protein 2
Vanilloid receptor-related osmotically-activated channel
Short name:
VR-OAC
Gene namesi
Name:Trpv4
Synonyms:Trp12, Vrl2, Vroac
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1926945. Trpv4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 465465CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei466 – 48621HelicalSequence AnalysisAdd
BLAST
Topological domaini487 – 50822ExtracellularSequence AnalysisAdd
BLAST
Transmembranei509 – 52921HelicalSequence AnalysisAdd
BLAST
Topological domaini530 – 55021CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei551 – 57121HelicalSequence AnalysisAdd
BLAST
Topological domaini572 – 5721ExtracellularSequence Analysis
Transmembranei573 – 59321HelicalSequence AnalysisAdd
BLAST
Topological domaini594 – 61623CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei617 – 63721HelicalSequence AnalysisAdd
BLAST
Intramembranei648 – 67831Pore-formingCuratedAdd
BLAST
Transmembranei691 – 71121HelicalSequence AnalysisAdd
BLAST
Topological domaini712 – 871160CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. adherens junction Source: UniProtKB
  2. cell surface Source: Ensembl
  3. cilium Source: MGI
  4. cortical actin cytoskeleton Source: Ensembl
  5. cytoplasmic microtubule Source: Ensembl
  6. cytoplasmic vesicle Source: Ensembl
  7. filopodium Source: Ensembl
  8. focal adhesion Source: Ensembl
  9. growth cone Source: Ensembl
  10. integral component of membrane Source: UniProtKB-KW
  11. lamellipodium Source: Ensembl
  12. plasma membrane Source: UniProtKB
  13. ruffle membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice display impairment of the intercellular junction-dependent barrier function in the skin.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi142 – 1432PP → AL: Strongly reduced interaction with PACSIN3. 1 Publication
Mutagenesisi253 – 2531Y → F: Abolishes hypotonicity-dependent channel activity. 1 Publication
Mutagenesisi672 – 6721D → A: Greatly reduces Ca(2+) permeation and channel rectification; when associated with A-682. 1 Publication
Mutagenesisi675 – 6751K → A: No effect on channel pore properties. 1 Publication
Mutagenesisi680 – 6801M → A: Impairs Ca(2+) permeation. 1 Publication
Mutagenesisi682 – 6821D → A: Greatly reduces Ca(2+) permeation and channel rectification; when associated with A-672. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 871871Transient receptor potential cation channel subfamily V member 4PRO_0000215348Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei253 – 2531Phosphotyrosine; by LYN1 Publication
Modified residuei824 – 8241Phosphoserine; by PKC and PKABy similarity

Post-translational modificationi

Phosphorylation results in enhancement of its channel function.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9EPK8.
PRIDEiQ9EPK8.

PTM databases

PhosphoSiteiQ9EPK8.

Expressioni

Tissue specificityi

Detected in liver, kidney, heart, brain cortex, cerebellum and brainstem (at protein level). Expressed in heart, lung, spleen, liver, kidney, brain, skeletal muscle and testis. In the central nervous system, expressed in the lamina terminalis (arched vascular organ and neurons of the subfornical organ), median preoptic area, ventral hippocampal commissure, and ependymal cells of the choroid plexus. In the cochlea, expressed in both inner and outer hair cells, and in marginal cells of the cochlear stria vascularis. Expressed in large neurons of the trigeminal ganglion. In the kidney cortex, strongly expressed by epithelial cells of tubules and much weaker in glomeruli.5 Publications

Gene expression databases

BgeeiQ9EPK8.
ExpressionAtlasiQ9EPK8. baseline and differential.
GenevestigatoriQ9EPK8.

Interactioni

Subunit structurei

Interacts with calmodulin (By similarity). Interacts with CTNNB1. The TRPV4 and CTNNB1 complex can interact with CDH1. Part of a complex containing MLC1, AQP4, HEPACAM and ATP1B1 (By similarity). Interacts with MAP7 and Src family Tyr protein kinases LYN, SRC, FYN, HCK, LCK and YES. Interacts with PACSIN1, PACSIN2 and PACSIN3 (via SH3 domain).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
UBCP0CG483EBI-7091763,EBI-3390054From a different organism.

Protein-protein interaction databases

DIPiDIP-44011N.
IntActiQ9EPK8. 2 interactions.
MINTiMINT-4050076.

Structurei

3D structure databases

ProteinModelPortaliQ9EPK8.
SMRiQ9EPK8. Positions 148-755.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati237 – 26630ANK 1Add
BLAST
Repeati284 – 31330ANK 2Add
BLAST
Repeati369 – 39830ANK 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni812 – 83120Interaction with calmodulinBy similarityAdd
BLAST

Sequence similaritiesi

Contains 3 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG278734.
GeneTreeiENSGT00550000074425.
HOGENOMiHOG000234630.
HOVERGENiHBG054085.
InParanoidiQ9EPK8.
KOiK04973.
OMAiEDQTNCT.
OrthoDBiEOG70S74P.
PhylomeDBiQ9EPK8.
TreeFamiTF314711.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR008348. TRPV4_channel.
[Graphical view]
PANTHERiPTHR10582:SF4. PTHR10582:SF4. 1 hit.
PfamiPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01768. TRPVRECEPTOR.
PR01769. VRL2RECEPTOR.
SMARTiSM00248. ANK. 3 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9EPK8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MADPGDGPRA APGEVAEPPG DESGTSGGEA FPLSSLANLF EGEEGSSSLS
60 70 80 90 100
PVDASRPAGP GDGRPNLRMK FQGAFRKGVP NPIDLLESTL YESSVVPGPK
110 120 130 140 150
KAPMDSLFDY GTYRHHPSDN KRWRRKVVEK QPQSPKAPAP QPPPILKVFN
160 170 180 190 200
RPILFDIVSR GSTADLDGLL SFLLTHKKRL TDEEFREPST GKTCLPKALL
210 220 230 240 250
NLSNGRNDTI PVLLDIAERT GNMREFINSP FRDIYYRGQT SLHIAIERRC
260 270 280 290 300
KHYVELLVAQ GADVHAQARG RFFQPKDEGG YFYFGELPLS LAACTNQPHI
310 320 330 340 350
VNYLTENPHK KADMRRQDSR GNTVLHALVA IADNTRENTK FVTKMYDLLL
360 370 380 390 400
LKCSRLFPDS NLETVLNNDG LSPLMMAAKT GKIGVFQHII RREVTDEDTR
410 420 430 440 450
HLSRKFKDWA YGPVYSSLYD LSSLDTCGEE VSVLEILVYN SKIENRHEML
460 470 480 490 500
AVEPINELLR DKWRKFGAVS FYINVVSYLC AMVIFTLTAY YQPLEGTPPY
510 520 530 540 550
PYRTTVDYLR LAGEVITLFT GVLFFFTSIK DLFTKKCPGV NSLFVDGSFQ
560 570 580 590 600
LLYFIYSVLV VVSAALYLAG IEAYLAVMVF ALVLGWMNAL YFTRGLKLTG
610 620 630 640 650
TYSIMIQKIL FKDLFRFLLV YLLFMIGYAS ALVTLLNPCT NMKVCDEDQS
660 670 680 690 700
NCTVPTYPAC RDSETFSAFL LDLFKLTIGM GDLEMLSSAK YPVVFILLLV
710 720 730 740 750
TYIILTFVLL LNMLIALMGE TVGQVSKESK HIWKLQWATT ILDIERSFPV
760 770 780 790 800
FLRKAFRSGE MVTVGKSSDG TPDRRWCFRV DEVNWSHWNQ NLGIINEDPG
810 820 830 840 850
KSEIYQYYGF SHTVGRLRRD RWSSVVPRVV ELNKNSSADE VVVPLDNLGN
860 870
PNCDGHQQGY APKWRTDDAP L
Length:871
Mass (Da):98,027
Last modified:March 1, 2001 - v1
Checksum:i5BAC6E33F89CEA05
GO

Sequence cautioni

The sequence AAG28028.1 differs from that shown. Reason: Frameshift at positions 47, 50, 53, 72 and 73. Curated
The sequence AAK69486.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451G → S in AAG28028. (PubMed:11081638)Curated
Sequence conflicti90 – 901L → R in AAG17543. (PubMed:11025659)Curated
Sequence conflicti90 – 901L → R in AAK69486. 1 PublicationCurated
Sequence conflicti137 – 1371A → T in BAA83731. (PubMed:12692122)Curated
Sequence conflicti210 – 2112IP → LQ in BAA83731. (PubMed:12692122)Curated
Sequence conflicti477 – 4771S → P in AAG28028. (PubMed:11081638)Curated
Sequence conflicti784 – 7841N → S in BAA83731. (PubMed:12692122)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF263522 mRNA. Translation: AAG28028.1. Frameshift.
AJ296078 mRNA. Translation: CAC20703.1.
AF208026 mRNA. Translation: AAG17543.1.
AB021875 mRNA. Translation: BAA83731.2.
AF279672 mRNA. Translation: AAK69486.1. Different initiation.
BC127052 mRNA. Translation: AAI27053.1.
CCDSiCCDS19568.1.
RefSeqiNP_071300.2. NM_022017.3.
UniGeneiMm.266450.

Genome annotation databases

EnsembliENSMUST00000071968; ENSMUSP00000071859; ENSMUSG00000014158.
ENSMUST00000112225; ENSMUSP00000107844; ENSMUSG00000014158.
GeneIDi63873.
KEGGimmu:63873.
UCSCiuc008yzu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF263522 mRNA. Translation: AAG28028.1 . Frameshift.
AJ296078 mRNA. Translation: CAC20703.1 .
AF208026 mRNA. Translation: AAG17543.1 .
AB021875 mRNA. Translation: BAA83731.2 .
AF279672 mRNA. Translation: AAK69486.1 . Different initiation.
BC127052 mRNA. Translation: AAI27053.1 .
CCDSi CCDS19568.1.
RefSeqi NP_071300.2. NM_022017.3.
UniGenei Mm.266450.

3D structure databases

ProteinModelPortali Q9EPK8.
SMRi Q9EPK8. Positions 148-755.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-44011N.
IntActi Q9EPK8. 2 interactions.
MINTi MINT-4050076.

Chemistry

BindingDBi Q9EPK8.
ChEMBLi CHEMBL6126.
GuidetoPHARMACOLOGYi 510.

PTM databases

PhosphoSitei Q9EPK8.

Proteomic databases

PaxDbi Q9EPK8.
PRIDEi Q9EPK8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000071968 ; ENSMUSP00000071859 ; ENSMUSG00000014158 .
ENSMUST00000112225 ; ENSMUSP00000107844 ; ENSMUSG00000014158 .
GeneIDi 63873.
KEGGi mmu:63873.
UCSCi uc008yzu.1. mouse.

Organism-specific databases

CTDi 59341.
MGIi MGI:1926945. Trpv4.

Phylogenomic databases

eggNOGi NOG278734.
GeneTreei ENSGT00550000074425.
HOGENOMi HOG000234630.
HOVERGENi HBG054085.
InParanoidi Q9EPK8.
KOi K04973.
OMAi EDQTNCT.
OrthoDBi EOG70S74P.
PhylomeDBi Q9EPK8.
TreeFami TF314711.

Enzyme and pathway databases

Reactomei REACT_227861. TRP channels.

Miscellaneous databases

NextBioi 319803.
PROi Q9EPK8.
SOURCEi Search...

Gene expression databases

Bgeei Q9EPK8.
ExpressionAtlasi Q9EPK8. baseline and differential.
Genevestigatori Q9EPK8.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR008348. TRPV4_channel.
[Graphical view ]
PANTHERi PTHR10582:SF4. PTHR10582:SF4. 1 hit.
Pfami PF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view ]
PRINTSi PR01768. TRPVRECEPTOR.
PR01769. VRL2RECEPTOR.
SMARTi SM00248. ANK. 3 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
TIGRFAMsi TIGR00870. trp. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Vanilloid receptor-related osmotically activated channel (VR-OAC), a candidate vertebrate osmoreceptor."
    Liedtke W.B., Choe Y., Marti-Renom M.A., Bell A.M., Denis C.S., Sali A., Hudspeth A.J., Friedman J.M., Heller S.
    Cell 103:525-535(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Hypothalamus.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Kidney.
  3. "OTRPC4, a nonselective cation channel that confers sensitivity to extracellular osmolarity."
    Strotmann R., Harteneck C., Nunnenmacher K., Schultz G., Plant T.D.
    Nat. Cell Biol. 2:695-702(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: 129/SvEv.
  4. "Impaired pressure sensation in mice lacking TRPV4."
    Suzuki M., Mizuno A., Kodaira K., Imai M.
    J. Biol. Chem. 278:22664-22668(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Kidney.
  5. "Cloning of mouse and human vanilloid receptor-like protein 2 (VRL-2)."
    Derst C., Schafer M.K.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. Cited for: CHARACTERIZATION OF CHANNEL PORE, MUTAGENESIS OF ASP-672; LYS-675; MET-680 AND ASP-682.
  8. "Microtubule-associated protein 7 increases the membrane expression of transient receptor potential vanilloid 4 (TRPV4)."
    Suzuki M., Hirao A., Mizuno A.
    J. Biol. Chem. 278:51448-51453(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP7.
  9. "Regulation of a transient receptor potential (TRP) channel by tyrosine phosphorylation. SRC family kinase-dependent tyrosine phosphorylation of TRPV4 on TYR-253 mediates its response to hypotonic stress."
    Xu H., Zhao H., Tian W., Yoshida K., Roullet J.B., Cohen D.M.
    J. Biol. Chem. 278:11520-11527(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LYN; SRC; FYN; HCK; LCK AND YES, PHOSPHORYLATION AT TYR-253, MUTAGENESIS OF TYR-253.
  10. "PACSINs bind to the TRPV4 cation channel. PACSIN 3 modulates the subcellular localization of TRPV4."
    Cuajungco M.P., Grimm C., Oshima K., D'hoedt D., Nilius B., Mensenkamp A.R., Bindels R.J., Plomann M., Heller S.
    J. Biol. Chem. 281:18753-18762(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PACSIN1; PACSIN2 AND PACSIN3, MUTAGENESIS OF 142-PRO-PRO-143, TISSUE SPECIFICITY.
  11. "Stimulus-specific modulation of the cation channel TRPV4 by PACSIN 3."
    D'hoedt D., Owsianik G., Prenen J., Cuajungco M.P., Grimm C., Heller S., Voets T., Nilius B.
    J. Biol. Chem. 283:6272-6280(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PACSIN3.
  12. "The TRPV4 channel contributes to intercellular junction formation in keratinocytes."
    Sokabe T., Fukumi-Tominaga T., Yonemura S., Mizuno A., Tominaga M.
    J. Biol. Chem. 285:18749-18758(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH CTNBB1 AND CDH1.

Entry informationi

Entry nameiTRPV4_MOUSE
AccessioniPrimary (citable) accession number: Q9EPK8
Secondary accession number(s): A0JNY0
, Q91XR5, Q9EQZ4, Q9ERZ7, Q9ES76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3