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Q00944 (FAK1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 137. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Focal adhesion kinase 1

Short name=FADK 1
EC=2.7.10.2
Alternative name(s):
Focal adhesion kinase-related nonkinase
Short name=FRNK
Short name=p41/p43FRNK
Protein-tyrosine kinase 2
p125FAK
pp125FAK
Gene names
Name:PTK2
Synonyms:FAK, FAK1
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length1053 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development, embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), ephrin receptors, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Regulates P53/TP53 activity and stability. Phosphorylates SRC; this increases SRC kinase activity. Isoform 2 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Enzyme regulation

Subject to autoinhibition, mediated by interactions between the FERM domain and the kinase domain. Activated by autophosphorylation at Tyr-397. This promotes interaction with SRC and phosphorylation at Tyr-576 and Tyr-577 in the kinase activation loop. Phosphorylation at Tyr-576 and Tyr-577 is required for maximal kinase activity. Inhibited by TAE226. Ref.19

Subunit structure

Interacts with ARHGAP26, GRB7, DCC, PIK3R1, PXN and SRC. Interacts with the ARP2/3 complex. Ref.4 Ref.5 Ref.6 Ref.8 Ref.9 Ref.11 Ref.16

Subcellular location

Cell junctionfocal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmperinuclear region. Cytoplasmcytoskeleton By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Nucleus. Note: Constituent of focal adhesions. Detected at microtubules By similarity. Ref.3

Domain

The carboxy-terminal region is the site of focal adhesion targeting (FAT) sequence which mediates the localization of FAK1 to focal adhesions.

Post-translational modification

Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. Isoform 2 is phosphorylated on serine or threonine residues, but apparently not on tyrosine residues. Ref.3 Ref.7 Ref.14 Ref.19

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily.

Contains 1 FERM domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processAngiogenesis
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityAlternative promoter usage
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

signal complex assembly

Inferred from electronic annotation. Source: InterPro

   Cellular_componentfocal adhesion

Inferred from electronic annotation. Source: UniProtKB-SubCell

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

identical protein binding

Inferred from physical interaction Ref.11PubMed 20802513. Source: IntAct

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction PubMed 10512882Ref.11PubMed 18171471PubMed 20802513PubMed 8922390PubMed 9425168. Source: IntAct

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-2896409,EBI-2896409
ACTR3P611575EBI-2896409,EBI-351419From a different organism.
METP085815EBI-2896409,EBI-1039152From a different organism.
PXNP490242EBI-2896409,EBI-2896280
SRCP005233EBI-2896409,EBI-848039

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]
Isoform 1 (identifier: Q00944-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q00944-2)

Also known as: FRNK;

The sequence of this isoform differs from the canonical sequence as follows:
     1-692: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10531053Focal adhesion kinase 1
PRO_0000088076

Regions

Domain35 – 355321FERM
Domain422 – 680259Protein kinase
Nucleotide binding428 – 4347ATP Probable
Nucleotide binding500 – 5023ATP Probable
Compositional bias712 – 73322Pro-rich
Compositional bias865 – 91450Pro-rich

Sites

Active site5461Proton acceptor By similarity
Binding site4541ATP Probable

Amino acid modifications

Modified residue3971Phosphotyrosine; by autocatalysis Ref.7
Modified residue4071Phosphotyrosine By similarity
Modified residue5761Phosphotyrosine; by SRC Ref.7 Ref.19
Modified residue5771Phosphotyrosine; by SRC By similarity
Modified residue8631Phosphotyrosine Ref.7
Modified residue9111Phosphoserine Ref.14
Modified residue9261Phosphotyrosine By similarity

Natural variations

Alternative sequence1 – 692692Missing in isoform 2.
VSP_042173

Experimental info

Mutagenesis3951D → A: Abolishes interaction with PIK3R1. Ref.5

Secondary structure

................................................................................................................................... 1053
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: 8051154219B953B9

FASTA1,053119,207
        10         20         30         40         50         60 
MAAAYLDPNL NHTPSSSAKT HLGTGMERSP GAMERVLKVF HYFENSSEPT TWASIIRHGD 

        70         80         90        100        110        120 
ATDVRGIIQK IVDCHKVKNV ACYGLRLSHL QSEEVHWLHL DMGVSNVREK FELAHPPEEW 

       130        140        150        160        170        180 
KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKNDYMLEIA DQVDQEIALK LGCLEIRRSY 

       190        200        210        220        230        240 
GEMRGNALEK KSNYEVLEKD VGLRRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI 

       250        260        270        280        290        300 
LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGANP THLADFNQVQ 

       310        320        330        340        350        360 
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGATQSFII 

       370        380        390        400        410        420 
RPQKEGERAL PSIPKLANNE KQGVRSHTVS VSETDDYAEI IDEEDTYTMP STRDYEIQRE 

       430        440        450        460        470        480 
RIELGRCIGE GQFGDVHQGI YMSPENPAMA VAIKTCKNCT SDSVREKFLQ EALTMRQFDH 

       490        500        510        520        530        540 
PHIVKLIGVI TENPVWIIME LCTLGELRSF LQVRKFSLDL ASLILYAYQL STALAYLESK 

       550        560        570        580        590        600 
RFVHRDIAAR NVLVSATDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT 

       610        620        630        640        650        660 
SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT LYSLMTKCWA 

       670        680        690        700        710        720 
YDPSRRPRFT ELKAQLSTIL EEEKLQQEER MRMESRRQVT VSWDSGGSDE APPKPSRPGY 

       730        740        750        760        770        780 
PSPRSSEGFY PSPQHMVQPN HYQVSGYSGS HGIPAMAGSI YPGQASLLDQ TDSWNHRPQE 

       790        800        810        820        830        840 
VSAWQPNMED SGTLDVRGMG QVLPTHLMEE RLIRQQQEME EDQRWLEKEE RFLVMKPDVR 

       850        860        870        880        890        900 
LSRGSIERED GGLQGPAGNQ HIYQPVGKPD HAAPPKKPPR PGAPHLGSLA SLNSPVDSYN 

       910        920        930        940        950        960 
EGVKIKPQEI SPPPTANLDR SNDKVYENVT GLVKAVIEMS SKIQPAPPEE YVPMVKEVGL 

       970        980        990       1000       1010       1020 
ALRTLLATVD ESLPVLPAST HREIEMAQKL LNSDLAELIN KMKLAQQYVM TSLQQEYKKQ 

      1030       1040       1050 
MLTAAHALAV DAKNLLDVID QARLKMISQS RPH 

« Hide

Isoform 2 (FRNK) [UniParc].

Checksum: 61E6AD4B50CCCC49
Show »

FASTA36140,032

References

[1]"pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions."
Schaller M.D., Borgman C.A., Cobb B.S., Vines R.R., Reynolds A.B., Parsons J.T.
Proc. Natl. Acad. Sci. U.S.A. 89:5192-5196(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-1053 (ISOFORM 1).
Tissue: Embryo.
[2]"Chicken and mouse focal adhesion kinases are similar in structure at their amino termini."
Devor B.B., Zhang X., Patel S.K., Polte T.R., Hanks S.K.
Biochem. Biophys. Res. Commun. 190:1084-1089(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-63 (ISOFORM 1).
Tissue: Embryo.
[3]"Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK."
Schaller M.D., Borgman C.A., Parsons J.T.
Mol. Cell. Biol. 13:785-791(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE PROMOTER USAGE, IDENTIFICATION OF ISOFORM 2, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[4]"An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase."
Hildebrand J.D., Taylor J.M., Parsons J.T.
Mol. Cell. Biol. 16:3169-3178(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGAP26.
[5]"Requirement of phosphatidylinositol 3-kinase in focal adhesion kinase-promoted cell migration."
Reiske H.R., Kao S.C., Cary L.A., Guan J.L., Lai J.F., Chen H.C.
J. Biol. Chem. 274:12361-12366(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIK3R1 AND SRC, MUTAGENESIS OF ASP-395.
[6]"Association of Grb7 with phosphoinositides and its role in the regulation of cell migration."
Shen T.L., Han D.C., Guan J.L.
J. Biol. Chem. 277:29069-29077(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRB7.
[7]"Tyr-863 phosphorylation enhances focal adhesion kinase autophosphorylation at Tyr-397."
Leu T.H., Maa M.C.
Oncogene 21:6992-7000(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-397; TYR-576 AND TYR-863.
[8]"Focal adhesion kinase in netrin-1 signaling."
Ren X.R., Ming G.L., Xie Y., Hong Y., Sun D.M., Zhao Z.Q., Feng Z., Wang Q., Shim S., Chen Z.F., Song H.J., Mei L., Xiong W.C.
Nat. Neurosci. 7:1204-1212(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DCC.
[9]"Activation of FAK and Src are receptor-proximal events required for netrin signaling."
Li W., Lee J., Vikis H.G., Lee S.H., Liu G., Aurandt J., Shen T.L., Fearon E.R., Guan J.L., Han M., Rao Y., Hong K., Guan K.L.
Nat. Neurosci. 7:1213-1221(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DCC.
[10]"Netrin requires focal adhesion kinase and Src family kinases for axon outgrowth and attraction."
Liu G., Beggs H., Jurgensen C., Park H.T., Tang H., Gorski J., Jones K.R., Reichardt L.F., Wu J., Rao Y.
Nat. Neurosci. 7:1222-1232(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex."
Serrels B., Serrels A., Brunton V.G., Holt M., McLean G.W., Gray C.H., Jones G.E., Frame M.C.
Nat. Cell Biol. 9:1046-1056(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THE ARP2/3 COMPLEX.
[12]"FRNK inhibition of focal adhesion kinase-dependent signaling and migration in vascular smooth muscle cells."
Koshman Y.E., Kim T., Chu M., Engman S.J., Iyengar R., Robia S.L., Samarel A.M.
Arterioscler. Thromb. Vasc. Biol. 30:2226-2233(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Focal adhesion kinase-related nonkinase inhibits vascular smooth muscle cell invasion by focal adhesion targeting, tyrosine 168 phosphorylation, and competition for p130Cas Binding."
Koshman Y.E., Chu M., Engman S.J., Kim T., Iyengar R., Robia S.L., Samarel A.M.
Arterioscler. Thromb. Vasc. Biol. 31:2432-2440(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Serine-910 phosphorylation of focal adhesion kinase is critical for sarcomere reorganization in cardiomyocyte hypertrophy."
Chu M., Iyengar R., Koshman Y.E., Kim T., Russell B., Martin J.L., Heroux A.L., Robia S.L., Samarel A.M.
Cardiovasc. Res. 92:409-419(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-911, FUNCTION.
[15]"Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase."
Liu G., Guibao C.D., Zheng J.
Mol. Cell. Biol. 22:2751-2760(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 916-1053.
[16]"NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model."
Gao G., Prutzman K.C., King M.L., Scheswohl D.M., DeRose E.F., London R.E., Schaller M.D., Campbell S.L.
J. Biol. Chem. 279:8441-8451(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 920-1053 IN COMPLEX WITH PXN, INTERACTION WITH PXN.
[17]"The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation."
Prutzman K.C., Gao G., King M.L., Iyer V.V., Mueller G.A., Schaller M.D., Campbell S.L.
Structure 12:881-891(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 920-1053.
[18]"Crystal structure of the FERM domain of focal adhesion kinase."
Ceccarelli D.F., Song H.K., Poy F., Schaller M.D., Eck M.J.
J. Biol. Chem. 281:252-259(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 31-405.
[19]"Structural basis for the autoinhibition of focal adhesion kinase."
Lietha D., Cai X., Ceccarelli D.F., Li Y., Schaller M.D., Eck M.J.
Cell 129:1177-1187(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 411-686 IN COMPLEXES WITH STAUROSPORINE AND ATP ANALOG, ENZYME REGULATION, PHOSPHORYLATION AT TYR-576 AND TYR-577.
[20]"Crystal structures of the FAK kinase in complex with TAE226 and related bis-anilino pyrimidine inhibitors reveal a helical DFG conformation."
Lietha D., Eck M.J.
PLoS ONE 3:E3800-E3800(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 411-686 IN COMPLEX WITH TAE226.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86656 mRNA. Translation: AAA48765.1.
L08402 mRNA. Translation: AAA48766.1.
PIRA45388.
PC1239.
RefSeqNP_990766.1. NM_205435.1. [Q00944-1]
UniGeneGga.15614.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KTMNMR-A916-1053[»]
1PV3NMR-A920-1053[»]
1QVXNMR-A920-1053[»]
2AEHX-ray2.53A/B31-399[»]
2AL6X-ray2.35A/B31-405[»]
2J0JX-ray2.80A31-686[»]
2J0KX-ray3.00A/B31-686[»]
2J0LX-ray2.30A411-686[»]
2J0MX-ray2.80A31-399[»]
B411-686[»]
2JKKX-ray2.00A411-686[»]
2JKMX-ray2.31A411-686[»]
2JKOX-ray1.65A411-686[»]
2JKQX-ray2.60A411-686[»]
2L6FNMR-A916-1053[»]
2L6GNMR-A916-1053[»]
2L6HNMR-A916-1053[»]
3ZDTX-ray3.15A/B31-405[»]
4BRXX-ray2.05A411-686[»]
4C7TX-ray2.05A411-686[»]
4CYEX-ray3.20A/B31-405[»]
ProteinModelPortalQ00944.
SMRQ00944. Positions 33-686, 916-1053.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid676665. 2 interactions.
IntActQ00944. 11 interactions.
MINTMINT-1517788.

Proteomic databases

PaxDbQ00944.
PRIDEQ00944.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000026060; ENSGALP00000026013; ENSGALG00000016171. [Q00944-1]
GeneID396416.
KEGGgga:396416.

Organism-specific databases

CTD5747.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000115459.
HOGENOMHOG000069938.
HOVERGENHBG004018.
KOK05725.
PhylomeDBQ00944.

Enzyme and pathway databases

BRENDA2.7.10.2. 1306.

Family and domain databases

InterProIPR019749. Band_41_domain.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR005189. Focal_adhesion_kin_target_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamPF00373. FERM_M. 1 hit.
PF03623. Focal_AT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
ProDomPD006413. Focal_adhesion_target_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00295. B41. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF68993. SSF68993. 1 hit.
PROSITEPS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ00944.
NextBio20816457.
PROQ00944.

Entry information

Entry nameFAK1_CHICK
AccessionPrimary (citable) accession number: Q00944
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1994
Last modified: June 11, 2014
This is version 137 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references