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P63001 (RAC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related C3 botulinum toxin substrate 1
Alternative name(s):
p21-Rac1
Gene names
Name:Rac1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In glioma cells, promotes cell migration and invasion. Required for atypical chemokine receptor ACKR2-induced LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In podocytes, promotes nuclear shuttling of NR3C2; this modulation is required for a proper kidney functioning. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3. Ref.11

Enzyme regulation

Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP, GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity, and GDP dissociation inhibitors which inhibit the dissociation of the nucleotide from the GTPase. GTP hydrolysis is stimulated by ARHGAP30 By similarity. Ref.12

Subunit structure

Interacts with the GEF proteins PREX1, FARP1, FARP2, DOCK1, DOCK2 and DOCK7, which promote the exchange between GDP and GTP, and therefore activate it. Part of a quaternary complex containing PARD3, some PARD6 protein (PARD6A, PARD6B or PARD6G) and some atypical PKC protein (PRKCI or PRKCZ), which plays a central role in epithelial cell polarization. Found in a trimeric complex composed of DOCK1 and ELMO1, which plays a central role in phagocytosis of apoptotic cells. Interacts with RALBP1 via its effector domain. Interacts with BAIAP2, BAIAP2L1, PLXNB1, CYFIP1/SRA-1 and DEF6. Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1. Interacts with DSCAM; the interaction requires PAK1. Interacts with TBC1D2. Interacts with UNKL. Interacts with USP6. Interacts with SPATA13. Interacts with ITGB4. Interacts with the GTP-bound form of RAB7A. Interacts with ARHGEF2. Interacts with ARHGEF16; mediates activation of RAC1 by EPHA2. Interacts with NOXA1. Interacts with S100A8 and calprotectin (S100A8/9). Interacts with ARHGDIA; the interaction is induced by SEMA5A, mediated through PLXNB3 and inactivates and stabilizes RAC1. Interacts with PACSIN2. Interacts with ITGB1BP1 By similarity. Interacts with the GEF protein RASGRF2, which promotes the exchange between GDP and GTP, and therefore activates it. Interacts with PARD6A, PARD6B and PARD6G in a GTP-dependent manner. Part of a complex with MAP2K3, MAP3K3 and CCM2. Interacts with NISCH. Interacts with PIP5K1A. Interacts (GTP-bound form preferentially) with PKN2 (via the REM repeats); the interaction stimulates autophosphorylation and phosphorylation of PKN2. Interacts with SRGAP2. Interacts with PLXNB3. Interacts (when active) with PPP5C (via TPR repeats); activates PPP5C phosphatase activity and translocates PPP5C to the cell membrane. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Melanosome By similarity. Cytoplasm By similarity. Note: Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine. Found in the ruffled border (a late endosomal-like compartment in the plasma membrane) of bone-resorbing osteoclasts By similarity.

Tissue specificity

Widely expressed. Ref.1

Domain

The effector region mediates interaction with DEF6 By similarity.

Post-translational modification

GTP-bound active form is ubiquitinated by HACE1, leading to its degradation by the proteasome By similarity.

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMIsopeptide bond
Lipoprotein
Methylation
Prenylation
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from genetic interaction PubMed 21178006. Source: MGI

Wnt signaling pathway, planar cell polarity pathway

Inferred from genetic interaction PubMed 18953410. Source: MGI

actin filament organization

Inferred from electronic annotation. Source: Ensembl

anatomical structure arrangement

Inferred from mutant phenotype PubMed 20016102. Source: MGI

auditory receptor cell morphogenesis

Inferred from mutant phenotype PubMed 20016102. Source: MGI

axon guidance

Inferred from mutant phenotype PubMed 17409253. Source: MGI

bone resorption

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from direct assay PubMed 14657280. Source: MGI

cell migration

Inferred from direct assay PubMed 15728191. Source: MGI

cell motility

Inferred from sequence or structural similarity. Source: UniProtKB

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cell-cell junction organization

Inferred from mutant phenotype PubMed 20016102. Source: MGI

cerebral cortex radially oriented cell migration

Inferred from mutant phenotype PubMed 17409253. Source: MGI

cochlea morphogenesis

Inferred from mutant phenotype PubMed 20016102. Source: MGI

cytoskeleton organization

Inferred from direct assay PubMed 14657280. Source: MGI

dendrite development

Inferred from direct assay PubMed 12213441. Source: MGI

dendrite morphogenesis

Inferred from genetic interaction PubMed 20335472. Source: MGI

dopaminergic neuron differentiation

Inferred from genetic interaction PubMed 18953410. Source: MGI

embryonic olfactory bulb interneuron precursor migration

Inferred from mutant phenotype PubMed 17409253. Source: MGI

endocytosis

Inferred from direct assay PubMed 12446704. Source: MGI

engulfment of apoptotic cell

Inferred from direct assay PubMed 20691665. Source: BHF-UCL

epithelial cell morphogenesis

Inferred from mutant phenotype PubMed 20016102. Source: MGI

hyperosmotic response

Inferred from direct assay PubMed 12783890. Source: MGI

lamellipodium assembly

Inferred from direct assay PubMed 15728191. Source: MGI

localization within membrane

Inferred from electronic annotation. Source: Ensembl

mast cell chemotaxis

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-23 production

Inferred from electronic annotation. Source: Ensembl

phagocytosis, engulfment

Inferred from mutant phenotype PubMed 10934045. Source: UniProtKB

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

positive regulation of actin filament polymerization

Inferred from direct assay PubMed 12853475. Source: MGI

positive regulation of lamellipodium assembly

Inferred from sequence orthology PubMed 15467718. Source: MGI

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from mutant phenotype PubMed 15728722. Source: MGI

positive regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization to plasma membrane

Inferred from direct assay PubMed 23184663. Source: MGI

regulation of cell migration

Inferred from mutant phenotype PubMed 17409253. Source: MGI

regulation of respiratory burst

Inferred from electronic annotation. Source: Ensembl

ruffle assembly

Inferred from mutant phenotype PubMed 10934045. Source: UniProtKB

ruffle organization

Inferred from sequence orthology PubMed 15467718. Source: MGI

semaphorin-plexin signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from direct assay PubMed 12525493. Source: MGI

substrate adhesion-dependent cell spreading

Inferred from direct assay PubMed 18156211. Source: MGI

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: Ensembl

cell projection

Inferred from direct assay PubMed 15728722. Source: MGI

cytoplasm

Inferred from direct assay PubMed 12213441. Source: MGI

cytoplasmic membrane-bounded vesicle

Inferred from direct assay PubMed 12783890PubMed 14516655. Source: MGI

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

extrinsic component of plasma membrane

Inferred from direct assay PubMed 14516655. Source: MGI

lamellipodium

Inferred from direct assay PubMed 12783890PubMed 14657280. Source: MGI

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from direct assay PubMed 14657280. Source: MGI

phagocytic cup

Inferred from direct assay PubMed 10934045. Source: UniProtKB

ruffle membrane

Inferred from direct assay PubMed 10934045. Source: UniProtKB

trans-Golgi network

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGTP binding

Inferred from direct assay PubMed 12783890PubMed 14580336PubMed 15728191PubMed 23528453. Source: MGI

GTP-dependent protein binding

Inferred from physical interaction PubMed 10954424. Source: UniProtKB

GTPase activity

Inferred from direct assay PubMed 10699171PubMed 12525493PubMed 15249579. Source: MGI

Rho GDP-dissociation inhibitor binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.14. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Dlg4Q621082EBI-413646,EBI-300895
PAK1Q131533EBI-413646,EBI-1307From a different organism.
Sod1P082284EBI-413646,EBI-1635090

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 189189Ras-related C3 botulinum toxin substrate 1
PRO_0000042038
Propeptide190 – 1923Removed in mature form By similarity
PRO_0000042039

Regions

Nucleotide binding10 – 178GTP By similarity
Nucleotide binding57 – 615GTP By similarity
Nucleotide binding115 – 1184GTP By similarity
Motif32 – 409Effector region Potential

Amino acid modifications

Modified residue1891Cysteine methyl ester By similarity
Lipidation1891S-geranylgeranyl cysteine By similarity
Cross-link147Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Mutagenesis121G → V: Constitutively active. Interacts with PARD6 proteins. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P63001 [UniParc].

Last modified August 31, 2004. Version 1.
Checksum: ACEDF83A45E5EA67

FASTA19221,450
        10         20         30         40         50         60 
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG 

        70         80         90        100        110        120 
QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPNTPI ILVGTKLDLR 

       130        140        150        160        170        180 
DDKDTIEKLK EKKLTPITYP QGLAMAKEIG AVKYLECSAL TQRGLKTVFD EAIRAVLCPP 

       190 
PVKKRKRKCL LL 

« Hide

References

« Hide 'large scale' references
[1]"The murine rac1 gene: cDNA cloning, tissue distribution and regulated expression of rac1 mRNA by disassembly of actin microfilaments."
Moll J., Sansig G., Fattori E., van der Putten H.
Oncogene 6:863-866(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Thymus.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Head, Liver, Thymus and Tongue.
[3]"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].
Strain: Czech II and FVB/N.
Tissue: Mammary tumor.
[4]"The exchange factor Ras-GRF2 activates Ras-dependent and Rac-dependent mitogen-activated protein kinase pathways."
Fan W.-T., Koch C.A., de Hoog C.L., Fam N.P., Moran M.F.
Curr. Biol. 8:935-938(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RASGRF2.
[5]"The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42."
Joberty G., Petersen C., Gao L., Macara I.G.
Nat. Cell Biol. 2:531-539(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARD6A, MUTAGENESIS OF GLY-12.
[6]"A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity."
Lin D., Edwards A.S., Fawcett J.P., Mbamalu G., Scott J.D., Pawson T.
Nat. Cell Biol. 2:540-547(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARD6B.
[7]"Type Ialpha phosphatidylinositol-4-phosphate 5-kinase mediates Rac-dependent actin assembly."
Tolias K.F., Hartwig J.H., Ishihara H., Shibasaki Y., Cantley L.C., Carpenter C.L.
Curr. Biol. 10:153-156(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIP5K1A.
[8]"Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock."
Uhlik M.T., Abell A.N., Johnson N.L., Sun W., Cuevas B.D., Lobel-Rice K.E., Horne E.A., Dell'Acqua M.L., Johnson G.L.
Nat. Cell Biol. 5:1104-1110(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP3K3; MAP2K3 AND CCM2.
[9]"Regulation of p21-activated kinase-independent Rac1 signal transduction by Nischarin."
Reddig P.J., Xu D., Juliano R.L.
J. Biol. Chem. 280:30994-31002(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NISCH.
[10]"Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKN gamma kinase activation leading to cytoskeleton function and cell migration in astrocytes."
Bourguignon L.Y., Gilad E., Peyrollier K., Brightman A., Swanson R.A.
J. Neurochem. 101:1002-1017(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PKN2.
[11]"Modification of mineralocorticoid receptor function by Rac1 GTPase: implication in proteinuric kidney disease."
Shibata S., Nagase M., Yoshida S., Kawarazaki W., Kurihara H., Tanaka H., Miyoshi J., Takai Y., Fujita T.
Nat. Med. 14:1370-1376(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"The F-BAR domain of srGAP2 induces membrane protrusions required for neuronal migration and morphogenesis."
Guerrier S., Coutinho-Budd J., Sassa T., Gresset A., Jordan N.V., Chen K., Jin W.L., Frost A., Polleux F.
Cell 138:990-1004(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRGAP2, ENZYME REGULATION.
[13]"Semaphorin 5A and plexin-B3 inhibit human glioma cell motility through RhoGDIalpha-mediated inactivation of Rac1 GTPase."
Li X., Lee A.Y.
J. Biol. Chem. 285:32436-32445(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLXNB3.
[14]"The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells."
Wallace S.W., Magalhaes A., Hall A.
Mol. Cell. Biol. 31:81-91(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PKN2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57277 mRNA. Translation: CAA40545.1.
AK009017 mRNA. Translation: BAB26027.1.
AK011072 mRNA. Translation: BAB69451.1.
AK034601 mRNA. Translation: BAC28767.1.
AK047969 mRNA. Translation: BAC33203.1.
AK088825 mRNA. Translation: BAC40596.1.
BC003828 mRNA. Translation: AAH03828.1.
BC051053 mRNA. Translation: AAH51053.1.
CCDSCCDS19843.1.
PIRA60347.
RefSeqNP_033033.1. NM_009007.2.
UniGeneMm.292510.
Mm.469963.
Mm.475073.

3D structure databases

ProteinModelPortalP63001.
SMRP63001. Positions 1-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202556. 20 interactions.
IntActP63001. 28 interactions.
MINTMINT-1602774.

Chemistry

BindingDBP63001.
ChEMBLCHEMBL5628.

PTM databases

PhosphoSiteP63001.

Proteomic databases

MaxQBP63001.
PaxDbP63001.
PRIDEP63001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000080537; ENSMUSP00000079380; ENSMUSG00000001847.
GeneID19353.
KEGGmmu:19353.
UCSCuc009akk.1. mouse.

Organism-specific databases

CTD5879.
MGIMGI:97845. Rac1.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00640000091266.
HOGENOMHOG000233974.
HOVERGENHBG009351.
KOK04392.
OrthoDBEOG764747.
PhylomeDBP63001.
TreeFamTF101109.

Enzyme and pathway databases

ReactomeREACT_188576. Developmental Biology.

Gene expression databases

ArrayExpressP63001.
BgeeP63001.
CleanExMM_RAC1.
GenevestigatorP63001.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAC1. mouse.
NextBio296387.
PROP63001.
SOURCESearch...

Entry information

Entry nameRAC1_MOUSE
AccessionPrimary (citable) accession number: P63001
Secondary accession number(s): O95501, P15154, Q9BTB4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot