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P08134

- RHOC_HUMAN

UniProt

P08134 - RHOC_HUMAN

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Protein

Rho-related GTP-binding protein RhoC

Gene
RHOC, ARH9, ARHC
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Regulates apical junction formation in bronchial epithelial cells.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 198GTP By similarity
Nucleotide bindingi59 – 635GTP By similarity
Nucleotide bindingi117 – 1204GTP By similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
  3. signal transducer activity Source: UniProtKB

GO - Biological processi

  1. apical junction assembly Source: UniProtKB
  2. axon guidance Source: Reactome
  3. cytokinesis Source: UniProtKB
  4. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  5. regulation of small GTPase mediated signal transduction Source: Reactome
  6. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_18407. G alpha (12/13) signalling events.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
SignaLinkiP08134.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho-related GTP-binding protein RhoC
Alternative name(s):
Rho cDNA clone 9
Short name:
h9
Gene namesi
Name:RHOC
Synonyms:ARH9, ARHC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:669. RHOC.

Subcellular locationi

Cell membrane; Lipid-anchor; Cytoplasmic side Reviewed prediction. Cleavage furrow
Note: Translocates to the equatorial region before furrow formation in a ECT2-dependent manner.1 Publication

GO - Cellular componenti

  1. cleavage furrow Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. nucleus Source: Ensembl
  5. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24951.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 190190Rho-related GTP-binding protein RhoCPRO_0000042022Add
BLAST
Propeptidei191 – 1933Removed in mature form By similarityPRO_0000042023

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411ADP-ribosylasparagine; by botulinum toxin By similarity
Modified residuei190 – 1901Cysteine methyl ester By similarity
Lipidationi190 – 1901S-geranylgeranyl cysteine By similarity

Keywords - PTMi

ADP-ribosylation, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiP08134.
PaxDbiP08134.
PRIDEiP08134.

PTM databases

PhosphoSiteiP08134.

Expressioni

Gene expression databases

ArrayExpressiP08134.
BgeeiP08134.
CleanExiHS_RHOC.
GenevestigatoriP08134.

Organism-specific databases

HPAiCAB010821.

Interactioni

Subunit structurei

Interacts with RTKN By similarity. Interacts with AKAP13, DIAPH1, PKN2, ROCK1 and ROCK2. Interacts with ARHGDIA.4 Publications

Protein-protein interaction databases

BioGridi106882. 11 interactions.
IntActiP08134. 6 interactions.
MINTiMINT-1216716.
STRINGi9606.ENSP00000285735.

Structurei

Secondary structure

1
193
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1310
Helixi18 – 2710
Beta strandi43 – 486
Beta strandi51 – 588
Helixi64 – 663
Turni67 – 693
Helixi70 – 734
Beta strandi78 – 858
Helixi89 – 979
Helixi99 – 1068
Beta strandi112 – 1176
Helixi119 – 1213
Helixi125 – 1328
Turni133 – 1353
Helixi141 – 15010
Beta strandi154 – 1585
Turni161 – 1633
Helixi167 – 17913

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z2CX-ray3.00A/C1-193[»]
2GCNX-ray1.85A1-181[»]
2GCOX-ray1.40A/B1-181[»]
2GCPX-ray2.15A1-181[»]
ProteinModelPortaliP08134.
SMRiP08134. Positions 3-179.

Miscellaneous databases

EvolutionaryTraceiP08134.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi34 – 429Effector region Reviewed prediction

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
KOiK07857.
OrthoDBiEOG73FQPD.
PhylomeDBiP08134.
TreeFamiTF300837.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08134-1 [UniParc]FASTAAdd to Basket

« Hide

MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYIADIEVDG    50
KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT 100
PEVKHFCPNV PIILVGNKKD LRQDEHTRRE LAKMKQEPVR SEEGRDMANR 150
ISAFGYLECS AKTKEGVREV FEMATRAGLQ VRKNKRRRGC PIL 193
Length:193
Mass (Da):22,006
Last modified:August 1, 1988 - v1
Checksum:iA193DA581560F131
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti120 – 1201D → H.
Corresponds to variant rs11538959 [ dbSNP | Ensembl ].
VAR_051974

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06821 mRNA. Translation: CAA29969.1.
L25081 mRNA. Translation: AAC33179.1.
AF498972 mRNA. Translation: AAM21119.1.
CR450360 mRNA. Translation: CAG29356.1.
BT019448 mRNA. Translation: AAV38255.1.
AK094474 mRNA. Translation: BAG52873.1.
AL603832 Genomic DNA. Translation: CAI14058.1.
CH471122 Genomic DNA. Translation: EAW56534.1.
BC007245 mRNA. Translation: AAH07245.1.
BC009177 mRNA. Translation: AAH09177.1.
BC052808 mRNA. Translation: AAH52808.1.
CCDSiCCDS854.1.
PIRiS01029. TVHURC.
RefSeqiNP_001036143.1. NM_001042678.1.
NP_001036144.1. NM_001042679.1.
NP_786886.1. NM_175744.4.
UniGeneiHs.502659.
Hs.658289.

Genome annotation databases

EnsembliENST00000285735; ENSP00000285735; ENSG00000155366.
ENST00000339083; ENSP00000345236; ENSG00000155366.
ENST00000369632; ENSP00000358646; ENSG00000155366.
ENST00000369633; ENSP00000358647; ENSG00000155366.
ENST00000369637; ENSP00000358651; ENSG00000155366.
ENST00000369638; ENSP00000358652; ENSG00000155366.
ENST00000369642; ENSP00000358656; ENSG00000155366.
GeneIDi389.
KEGGihsa:389.
UCSCiuc001ecp.1. human.

Polymorphism databases

DMDMi132543.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06821 mRNA. Translation: CAA29969.1 .
L25081 mRNA. Translation: AAC33179.1 .
AF498972 mRNA. Translation: AAM21119.1 .
CR450360 mRNA. Translation: CAG29356.1 .
BT019448 mRNA. Translation: AAV38255.1 .
AK094474 mRNA. Translation: BAG52873.1 .
AL603832 Genomic DNA. Translation: CAI14058.1 .
CH471122 Genomic DNA. Translation: EAW56534.1 .
BC007245 mRNA. Translation: AAH07245.1 .
BC009177 mRNA. Translation: AAH09177.1 .
BC052808 mRNA. Translation: AAH52808.1 .
CCDSi CCDS854.1.
PIRi S01029. TVHURC.
RefSeqi NP_001036143.1. NM_001042678.1.
NP_001036144.1. NM_001042679.1.
NP_786886.1. NM_175744.4.
UniGenei Hs.502659.
Hs.658289.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Z2C X-ray 3.00 A/C 1-193 [» ]
2GCN X-ray 1.85 A 1-181 [» ]
2GCO X-ray 1.40 A/B 1-181 [» ]
2GCP X-ray 2.15 A 1-181 [» ]
ProteinModelPortali P08134.
SMRi P08134. Positions 3-179.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106882. 11 interactions.
IntActi P08134. 6 interactions.
MINTi MINT-1216716.
STRINGi 9606.ENSP00000285735.

PTM databases

PhosphoSitei P08134.

Polymorphism databases

DMDMi 132543.

Proteomic databases

MaxQBi P08134.
PaxDbi P08134.
PRIDEi P08134.

Protocols and materials databases

DNASUi 389.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000285735 ; ENSP00000285735 ; ENSG00000155366 .
ENST00000339083 ; ENSP00000345236 ; ENSG00000155366 .
ENST00000369632 ; ENSP00000358646 ; ENSG00000155366 .
ENST00000369633 ; ENSP00000358647 ; ENSG00000155366 .
ENST00000369637 ; ENSP00000358651 ; ENSG00000155366 .
ENST00000369638 ; ENSP00000358652 ; ENSG00000155366 .
ENST00000369642 ; ENSP00000358656 ; ENSG00000155366 .
GeneIDi 389.
KEGGi hsa:389.
UCSCi uc001ecp.1. human.

Organism-specific databases

CTDi 389.
GeneCardsi GC01M113243.
HGNCi HGNC:669. RHOC.
HPAi CAB010821.
MIMi 165380. gene.
neXtProti NX_P08134.
PharmGKBi PA24951.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
HOGENOMi HOG000233974.
HOVERGENi HBG009351.
KOi K07857.
OrthoDBi EOG73FQPD.
PhylomeDBi P08134.
TreeFami TF300837.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.
REACT_18407. G alpha (12/13) signalling events.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
SignaLinki P08134.

Miscellaneous databases

EvolutionaryTracei P08134.
GeneWikii RhoC.
GenomeRNAii 389.
NextBioi 1619.
PROi P08134.
SOURCEi Search...

Gene expression databases

ArrayExpressi P08134.
Bgeei P08134.
CleanExi HS_RHOC.
Genevestigatori P08134.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view ]
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00174. RHO. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51420. RHO. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Coding sequence of human rho cDNAs clone 6 and clone 9."
    Chardin P., Madaule P., Tavitian A.
    Nucleic Acids Res. 16:2717-2717(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Fagan K.P., Oliveira L., Pittler S.J.
    Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  3. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum.
  7. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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].
    Tissue: Skin.
  10. "The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton."
    Leung T., Chen X.-Q., Manser E., Lim L.
    Mol. Cell. Biol. 16:5313-5327(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ROCK1 AND ROCK2.
  11. "AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation."
    Diviani D., Soderling J., Scott J.D.
    J. Biol. Chem. 276:44247-44257(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AKAP13.
  12. "Dissecting the role of Rho-mediated signaling in contractile ring formation."
    Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S., Miki T.
    Mol. Biol. Cell 17:43-55(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "Regulation of Rho GTPase crosstalk, degradation and activity by RhoGDI1."
    Boulter E., Garcia-Mata R., Guilluy C., Dubash A., Rossi G., Brennwald P.J., Burridge K.
    Nat. Cell Biol. 12:477-483(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGDIA.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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: FUNCTION, INTERACTION WITH PKN2.
  16. "Structural and mechanistic insights into the interaction between Rho and mammalian Dia."
    Rose R., Weyand M., Lammers M., Ishizaki T., Ahmadian M.R., Wittinghofer A.
    Nature 435:513-518(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH DIAPH1.

Entry informationi

Entry nameiRHOC_HUMAN
AccessioniPrimary (citable) accession number: P08134
Secondary accession number(s): B3KSW1, Q6ICN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: September 3, 2014
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi