Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P30085 (KCY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
UMP-CMP kinase

EC=2.7.4.14
Alternative name(s):
Deoxycytidylate kinase
Short name=CK
Short name=dCMP kinase
Nucleoside-diphosphate kinase
EC=2.7.4.6
Uridine monophosphate/cytidine monophosphate kinase
Short name=UMP/CMP kinase
Short name=UMP/CMPK
Gene names
Name:CMPK1
Synonyms:CMK, CMPK, UCK, UMK, UMPK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Also displays broad nucleoside diphosphate kinase activity. Ref.1 Ref.3 Ref.16

Catalytic activity

ATP + (d)CMP = ADP + (d)CDP. Ref.1 Ref.16

ATP + UMP = ADP + UDP. Ref.1 Ref.16

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. Ref.1 Ref.16

Cofactor

Binds 1 magnesium ion per monomer.

Subunit structure

Monomer By similarity. HAMAP-Rule MF_03172

Subcellular location

Nucleus. Cytoplasm. Note: Predominantly nuclear. Ref.1 Ref.3

Tissue specificity

Ubiquitously expressed. Ref.2

Domain

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. HAMAP-Rule MF_03172

Sequence similarities

Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.

Sequence caution

The sequence AAF17709.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAH14961.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAD96734.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAG60709.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAI13471.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI14972.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCDP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

UDP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

UMP biosynthetic process

Traceable author statement Ref.1. Source: GOC

dCDP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

dUDP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing small molecule interconversion

Traceable author statement. Source: Reactome

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

nucleoside diphosphate phosphorylation

Inferred from direct assay Ref.16. Source: UniProtKB

nucleoside triphosphate biosynthetic process

Inferred from direct assay Ref.16. Source: UniProtKB

ovulation cycle process

Inferred from electronic annotation. Source: Ensembl

phthalate metabolic process

Inferred from electronic annotation. Source: Ensembl

pyrimidine ribonucleotide biosynthetic process

Traceable author statement Ref.1. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Traceable author statement Ref.1. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

UMP kinase activity

Inferred from electronic annotation. Source: Ensembl

cytidylate kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

nucleoside diphosphate kinase activity

Inferred from direct assay Ref.16. Source: UniProtKB

uridine kinase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P30085-1)

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: P30085-2)

The sequence of this isoform differs from the canonical sequence as follows:
     26-74: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 196196UMP-CMP kinase HAMAP-Rule MF_03172
PRO_0000158949

Regions

Nucleotide binding13 – 186ATP By similarity
Nucleotide binding61 – 633NMP By similarity
Nucleotide binding93 – 964NMP By similarity
Region33 – 6331NMPbind HAMAP-Rule MF_03172
Region133 – 14311LID HAMAP-Rule MF_03172

Sites

Binding site391NMP By similarity
Binding site1001CMP By similarity
Binding site1341ATP By similarity
Binding site1401NMP By similarity
Binding site1511NMP By similarity
Binding site1791ATP; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue431N6-acetyllysine By similarity
Modified residue551N6-acetyllysine Ref.14
Modified residue1061N6-succinyllysine By similarity

Natural variations

Alternative sequence26 – 7449Missing in isoform 2.
VSP_046683

Experimental info

Sequence conflict271Y → I AA sequence Ref.11

Secondary structure

........................... 196
Helix Strand Turn

Details...

Sequences

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

Last modified December 1, 2000. Version 3.
Checksum: 6837B1E6D7543768

FASTA19622,222
        10         20         30         40         50         60 
MKPLVVFVLG GPGAGKGTQC ARIVEKYGYT HLSAGELLRD ERKNPDSQYG ELIEKYIKEG 

        70         80         90        100        110        120 
KIVPVEITIS LLKREMDQTM AANAQKNKFL IDGFPRNQDN LQGWNKTMDG KADVSFVLFF 

       130        140        150        160        170        180 
DCNNEICIER CLERGKSSGR SDDNRESLEK RIQTYLQSTK PIIDLYEEMG KVKKIDASKS 

       190 
VDEVFDEVVQ IFDKEG 

« Hide

Isoform 2 [UniParc].

Checksum: 535CD9D8F1B4A0F2
Show »

FASTA14716,548

References

« Hide 'large scale' references
[1]"Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the human enzyme."
Van Rompay A.R., Johansson M., Karlsson A.
Mol. Pharmacol. 56:562-569(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, FUNCTION.
[2]"Characterization of human UMP-CMP kinase enzymatic activity and 5' untranslated region."
Pearman A.T., Castro-Faria-Neto H.C., McIntyre T.M., Prescott S.M., Stafforini D.M.
Life Sci. 69:2361-2370(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CHROMOSOMAL LOCATION, IDENTIFICATION OF START CODON.
Tissue: Macrophage.
[3]"Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue monophosphates."
Liou J.-Y., Dutschman G.E., Lam W., Jiang Z., Cheng Y.-C.
Cancer Res. 62:1624-1631(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
[4]"Human UMP-CMP kinase gene."
Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., Luo M., Chen J., Hu R.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Pituitary.
[5]"Cloning and characterization of a new human cDNA homologous to pig UMP-CMP kinase mRNA."
Fan Y.X., Yu L., Dai F.Y., Zhou Y., Huang J., Zhao S.Y.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Hypothalamus.
[7]"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. expand/collapse author list , 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] (ISOFORM 2).
[8]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Small intestine.
[9]"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. expand/collapse author list , 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].
[10]"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] (ISOFORM 1).
Tissue: Muscle.
[11]"Human liver protein map: update 1993."
Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C., Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.
Electrophoresis 14:1216-1222(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-29.
Tissue: Liver.
[12]"Human liver protein map: a reference database established by microsequencing and gel comparison."
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10.
Tissue: Liver.
[13]Bienvenut W.V., Bilsland A.E., Keith W.N.
Submitted (JAN-2010) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-16; 62-73; 89-106; 152-171 AND 180-196, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma.
[14]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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].
[16]"The human adenylate kinase 9 is a nucleoside mono- and diphosphate kinase."
Amiri M., Conserva F., Panayiotou C., Karlsson A., Solaroli N.
Int. J. Biochem. Cell Biol. 45:925-931(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[17]"Substrate-induced conformational changes in human UMP/CMP kinase."
Segura-Pena D., Sekulic N., Ort S., Konrad M., Lavie A.
J. Biol. Chem. 279:33882-33889(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF070416 mRNA. Translation: AAF17709.1. Different initiation.
AF259961 mRNA. Translation: AAG22609.1.
AF110643 mRNA. Translation: AAD48583.1.
AF087865 mRNA. Translation: AAP97174.1.
AF112216 mRNA. Translation: AAF17204.1.
AK223014 mRNA. Translation: BAD96734.1. Different initiation.
AK298502 mRNA. Translation: BAG60709.1. Different initiation.
AL513322, AL607122 Genomic DNA. Translation: CAI13471.1. Sequence problems.
AL607122, AL513322 Genomic DNA. Translation: CAI14972.1. Sequence problems.
BC014961 mRNA. Translation: AAH14961.1. Different initiation.
PIRB45482.
RefSeqNP_001129612.1. NM_001136140.1.
NP_057392.1. NM_016308.2.
UniGeneHs.731647.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TEVX-ray2.10A1-196[»]
ProteinModelPortalP30085.
SMRP30085. Positions 3-196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119700. 2 interactions.
IntActP30085. 1 interaction.
MINTMINT-5000978.
STRING9606.ENSP00000360939.

Chemistry

ChEMBLCHEMBL5681.
DrugBankDB00441. Gemcitabine.

PTM databases

PhosphoSiteP30085.

Polymorphism databases

DMDM12644008.

2D gel databases

OGPP30085.
SWISS-2DPAGEP30085.

Proteomic databases

MaxQBP30085.
PaxDbP30085.
PRIDEP30085.

Protocols and materials databases

DNASU51727.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371873; ENSP00000360939; ENSG00000162368.
ENST00000450808; ENSP00000398192; ENSG00000162368.
GeneID51727.
KEGGhsa:51727.

Organism-specific databases

CTD51727.
GeneCardsGC01P047799.
HGNCHGNC:18170. CMPK1.
HPAHPA053730.
HPA058604.
MIM191710. gene.
neXtProtNX_P30085.
PharmGKBPA162382539.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0563.
HOVERGENHBG108060.
InParanoidP30085.
KOK13800.
OrthoDBEOG7X0VJ0.
PhylomeDBP30085.
TreeFamTF354283.

Enzyme and pathway databases

BioCycMetaCyc:HS08663-MONOMER.
BRENDA2.7.4.14. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP30085.

Gene expression databases

ArrayExpressP30085.
BgeeP30085.
CleanExHS_CMPK1.
GenevestigatorP30085.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00235. Adenylate_kinase_Adk.
MF_03172. Adenylate_kinase_UMP_CMP_kin.
InterProIPR000850. Adenylat/UMP-CMP_kin.
IPR027417. P-loop_NTPase.
IPR006266. UMP_CMP_kinase.
[Graphical view]
PANTHERPTHR23359. PTHR23359. 1 hit.
PRINTSPR00094. ADENYLTKNASE.
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01359. UMP_CMP_kin_fam. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP30085.
GeneWikiCMPK.
GenomeRNAi51727.
NextBio35473968.
PROP30085.
SOURCESearch...

Entry information

Entry nameKCY_HUMAN
AccessionPrimary (citable) accession number: P30085
Secondary accession number(s): B4DPU7 expand/collapse secondary AC list , E9PGI8, Q53GB7, Q5SVZ0, Q96C07, Q9UBQ8, Q9UIA2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 150 of the entry and version 3 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 chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM