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Q9Y4F1 (FARP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
FERM, RhoGEF and pleckstrin domain-containing protein 1
Alternative name(s):
Chondrocyte-derived ezrin-like protein
Pleckstrin homology domain-containing family C member 2
Short name=PH domain-containing family C member 2
Gene names
Name:FARP1
Synonyms:CDEP, PLEKHC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1045 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as guanine nucleotide exchange factor for RAC1. May play a role in semaphorin signaling. Plays a role in the assembly and disassembly of dendritic filopodia, the formation of dendritic spines, regulation of dendrite length and ultimately the formation of synapses By similarity.

Subunit structure

Interacts with CADM1. Interacts with RAC1 By similarity.

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junctionsynapse. Cell junctionsynapsesynaptosome By similarity. Cytoplasmcytosol By similarity. Cell projectionfilopodium By similarity. Cell projectiondendrite By similarity. Cell projectiondendritic spine By similarity. Note: Recruited to the cell membrane via interaction with CADM1 By similarity.

Tissue specificity

Detected in cAMP-treated chondrocytes, but not in untreated chondrocytes. Detected in fetal brain, heart and spleen, and in adult testis, kidney and lung. Ref.1

Induction

Up-regulated in response to cAMP in cultured embryonic chondrocytes. Ref.1

Domain

Intramolecular interaction between the DH domain and the PH domains can stabilize the protein in an autoinhibited conformation. Ref.13

Sequence similarities

Contains 1 DH (DBL-homology) domain.

Contains 1 FERM domain.

Contains 2 PH domains.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Membrane
Synapse
Synaptosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   Molecular functionDevelopmental protein
Guanine-nucleotide releasing factor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdendrite morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of phosphatase activity

Inferred from direct assay PubMed 19389623. Source: UniProtKB

regulation of Rac GTPase activity

Inferred from sequence or structural similarity. Source: GOC

regulation of Rho GTPase activity

Traceable author statement Ref.1. Source: GOC

synapse assembly

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay. Source: HPA

cytoskeleton

Traceable author statement Ref.1. Source: ProtInc

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine

Inferred from electronic annotation. Source: UniProtKB-SubCell

extrinsic component of cytoplasmic side of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

filopodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

synapse

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRac guanyl-nucleotide exchange factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Rho guanyl-nucleotide exchange factor activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y4F1-1)

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: Q9Y4F1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     758-758: R → RPGSFSLMRTPHLGQARRIPCAPERRPLLLVK
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9Y4F1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     58-129: QRAPGKVLLD...FPPDHTQLQE → MVSSSSFLKA...TVTEELLNLF
     130-1045: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10451045FERM, RhoGEF and pleckstrin domain-containing protein 1
PRO_0000232753

Regions

Domain40 – 320281FERM
Domain540 – 730191DH
Domain759 – 85698PH 1
Domain932 – 102998PH 2
Compositional bias449 – 4535Poly-Glu

Amino acid modifications

Modified residue241Phosphothreonine Ref.7 Ref.10
Modified residue3401Phosphoserine Ref.7
Modified residue3731Phosphoserine By similarity
Modified residue4271Phosphoserine Ref.5 Ref.6 Ref.10
Modified residue5101Phosphoserine Ref.10
Modified residue5141Phosphoserine Ref.10
Modified residue8721Phosphoserine Ref.12
Modified residue8891Phosphoserine Ref.8 Ref.12

Natural variations

Alternative sequence58 – 12972QRAPG…TQLQE → MVSSSSFLKATGSSWTGWVL RCSMKPKHHSHLIEKFGEDR ILTHLTGSISYTNWAGSRSL AVTVTEELLNLF in isoform 3.
VSP_040989
Alternative sequence130 – 1045916Missing in isoform 3.
VSP_040990
Alternative sequence7581R → RPGSFSLMRTPHLGQARRIP CAPERRPLLLVK in isoform 2.
VSP_017976
Natural variant81P → L.
Corresponds to variant rs9300466 [ dbSNP | Ensembl ].
VAR_048362
Natural variant7141R → L in a breast cancer sample; somatic mutation. Ref.14
VAR_035851

Experimental info

Sequence conflict6441H → Y in AAH71592. Ref.3

Sequences

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

Last modified November 1, 1999. Version 1.
Checksum: 0E8B2D61C0F58417

FASTA1,045118,633
        10         20         30         40         50         60 
MGEIEQRPTP GSRLGAPENS GISTLERGQK PPPTPSGKLV SIKIQMLDDT QEAFEVPQRA 

        70         80         90        100        110        120 
PGKVLLDAVC NHLNLVEGDY FGLEFPDHKK ITVWLDLLKP IVKQIRRPKH VVVKFVVKFF 

       130        140        150        160        170        180 
PPDHTQLQEE LTRYLFALQV KQDLAQGRLT CNDTSAALLI SHIVQSEIGD FDEALDREHL 

       190        200        210        220        230        240 
AKNKYIPQQD ALEDKIVEFH HNHIGQTPAE SDFQLLEIAR RLEMYGIRLH PAKDREGTKI 

       250        260        270        280        290        300 
NLAVANTGIL VFQGFTKINA FNWAKVRKLS FKRKRFLIKL RPDANSAYQD TLEFLMASRD 

       310        320        330        340        350        360 
FCKSFWKICV EHHAFFRLFE EPKPKPKPVL FSRGSSFRFS GRTQKQVLDY VKEGGHKKVQ 

       370        380        390        400        410        420 
FERKHSKIHS IRSLASQPTE LNSEVLEQSQ QSTSLTFGEG AESPGGQSCR RGKEPKVSAG 

       430        440        450        460        470        480 
EPGSHPSPAP RRSPAGNKQA DGAASAPTEE EEEVVKDRTQ QSKPQPPQPS TGSLTGSPHL 

       490        500        510        520        530        540 
SELSVNSQGG VAPANVTLSP NLSPDTKQAS PLISPLLNDQ ACPRTDDEDE GRRKRFPTDK 

       550        560        570        580        590        600 
AYFIAKEVST TERTYLKDLE VITSWFQSTV SKEDAMPEAL KSLIFPNFEP LHKFHTNFLK 

       610        620        630        640        650        660 
EIEQRLALWE GRSNAQIRDY QRIGDVMLKN IQGMKHLAAH LWKHSEALEA LENGIKSSRR 

       670        680        690        700        710        720 
LENFCRDFEL QKVCYLPLNT FLLRPLHRLM HYKQVLERLC KHHPPSHADF RDCRAALAEI 

       730        740        750        760        770        780 
TEMVAQLHGT MIKMENFQKL HELKKDLIGI DNLVVPGREF IRLGSLSKLS GKGLQQRMFF 

       790        800        810        820        830        840 
LFNDVLLYTS RGLTASNQFK VHGQLPLYGM TIEESEDEWG VPHCLTLRGQ RQSIIVAASS 

       850        860        870        880        890        900 
RSEMEKWVED IQMAIDLAEK SSSPAPEFLA SSPPDNKSPD EATAADQESE DDLSASRTSL 

       910        920        930        940        950        960 
ERQAPHRGNT MVHVCWHRNT SVSMVDFSIA VENQLSGNLL RKFKNSNGWQ KLWVVFTNFC 

       970        980        990       1000       1010       1020 
LFFYKSHQDN HPLASLPLLG YSLTIPSESE NIQKDYVFKL HFKSHVYYFR AESEYTFERW 

      1030       1040 
MEVIRSATSS ASRPHVLSHK ESLVY 

« Hide

Isoform 2 [UniParc].

Checksum: 25A71B2C8C60A280
Show »

FASTA1,076122,113
Isoform 3 [UniParc].

Checksum: ED33383FA354AB1E
Show »

FASTA12914,138

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of CDEP, a novel human protein containing the ezrin-like domain of the band 4.1 superfamily and the Dbl homology domain of rho guanine nucleotide exchange factors."
Koyano Y., Kawamoto T., Shen M., Yan W., Noshiro M., Fujii K., Kato Y.
Biochem. Biophys. Res. Commun. 241:369-375(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, TISSUE SPECIFICITY.
Tissue: Cartilage.
[2]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 1; 2 AND 3).
Tissue: Brain, Placenta and Skin.
[4]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-889, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24; SER-427; SER-510 AND SER-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872 AND SER-889, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Structural basis for autoinhibition of the guanine nucleotide exchange factor FARP2."
He X., Kuo Y.C., Rosche T.J., Zhang X.
Structure 21:355-364(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.09 ANGSTROMS) OF 539-1035, DOMAIN.
[14]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-714.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB008430 mRNA. Translation: BAA24267.1.
AL136300, AL445223 Genomic DNA. Translation: CAI10952.1.
AL136300, AL137249, AL161896 Genomic DNA. Translation: CAI10953.1.
AL161896, AL136300, AL137249 Genomic DNA. Translation: CAI12946.1.
AL445223, AL136300 Genomic DNA. Translation: CAI15981.1.
AL137249, AL136300, AL161896 Genomic DNA. Translation: CAI39458.1.
BC041595 mRNA. Translation: AAH41595.1.
BC065020 mRNA. No translation available.
BC071592 mRNA. Translation: AAH71592.1.
PIRJC5795.
RefSeqNP_001001715.2. NM_001001715.3.
NP_001273768.1. NM_001286839.1.
NP_005757.1. NM_005766.3.
UniGeneHs.403917.
Hs.709933.
Hs.729583.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4H6YX-ray4.09A/B539-1035[»]
ProteinModelPortalQ9Y4F1.
SMRQ9Y4F1. Positions 36-366, 539-1029.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115462. 3 interactions.
IntActQ9Y4F1. 1 interaction.
STRING9606.ENSP00000322926.

PTM databases

PhosphoSiteQ9Y4F1.

Polymorphism databases

DMDM74762059.

Proteomic databases

PaxDbQ9Y4F1.
PRIDEQ9Y4F1.

Protocols and materials databases

DNASU10160.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319562; ENSP00000322926; ENSG00000152767. [Q9Y4F1-1]
ENST00000376581; ENSP00000365765; ENSG00000152767. [Q9Y4F1-3]
GeneID10160.
KEGGhsa:10160.
UCSCuc001vni.3. human. [Q9Y4F1-3]
uc001vnj.3. human. [Q9Y4F1-1]

Organism-specific databases

CTD10160.
GeneCardsGC13P098795.
HGNCHGNC:3591. FARP1.
HPAHPA000760.
MIM602654. gene.
neXtProtNX_Q9Y4F1.
PharmGKBPA28004.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG282099.
HOGENOMHOG000007957.
HOVERGENHBG081521.
KOK17477.
OrthoDBEOG7B5WVD.
PhylomeDBQ9Y4F1.
TreeFamTF351276.

Gene expression databases

ArrayExpressQ9Y4F1.
BgeeQ9Y4F1.
CleanExHS_FARP1.
GenevestigatorQ9Y4F1.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 3 hits.
InterProIPR019749. Band_41_domain.
IPR019750. Band_41_fam.
IPR000219. DH-domain.
IPR000798. Ez/rad/moesin_like.
IPR014847. FERM-adjacent.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF08736. FA. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF00169. PH. 2 hits.
PF00621. RhoGEF. 1 hit.
[Graphical view]
PRINTSPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTSM00295. B41. 1 hit.
SM00233. PH. 2 hits.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
SSF48065. SSF48065. 1 hit.
PROSITEPS50010. DH_2. 1 hit.
PS00660. FERM_1. 1 hit.
PS50057. FERM_3. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFARP1. human.
GeneWikiFARP1.
GenomeRNAi10160.
NextBio38464.
PROQ9Y4F1.
SOURCESearch...

Entry information

Entry nameFARP1_HUMAN
AccessionPrimary (citable) accession number: Q9Y4F1
Secondary accession number(s): Q5JVI9, Q6IQ29
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM