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O14519

- CDKA1_HUMAN

UniProt

O14519 - CDKA1_HUMAN

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Protein

Cyclin-dependent kinase 2-associated protein 1

Gene
CDK2AP1, CDKAP1, DOC1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

specific inhibitor of the cell-cycle kinase CDK2 By similarity.

GO - Molecular functioni

  1. DNA binding Source: ProtInc

GO - Biological processi

  1. DNA-dependent DNA replication Source: ProtInc
  2. mitotic S phase Source: ProtInc
  3. protein phosphorylation Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 2-associated protein 1
Short name:
CDK2-associated protein 1
Alternative name(s):
Deleted in oral cancer 1
Short name:
DOC-1
Putative oral cancer suppressor
Gene namesi
Name:CDK2AP1
Synonyms:CDKAP1, DOC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:14002. CDK2AP1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. nucleus Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi105 – 1051C → A: Does not alter homodimerization. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA26308.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 115115Cyclin-dependent kinase 2-associated protein 1PRO_0000089452Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461Phosphoserine; by IKKE1 Publication
Disulfide bondi105 – 105Interchain Reviewed prediction

Post-translational modificationi

Phosphorylated in vitro by IKBKE at Ser-46.1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiO14519.
PaxDbiO14519.
PRIDEiO14519.

PTM databases

PhosphoSiteiO14519.

Expressioni

Gene expression databases

ArrayExpressiO14519.
BgeeiO14519.
CleanExiHS_CDK2AP1.
GenevestigatoriO14519.

Organism-specific databases

HPAiCAB019377.

Interactioni

Subunit structurei

Homodimer. Interacts with monomeric unphosphorylated CDK2.1 Publication

Protein-protein interaction databases

BioGridi113770. 19 interactions.
IntActiO14519. 5 interactions.
MINTiMINT-88804.
STRINGi9606.ENSP00000261692.

Structurei

Secondary structure

1
115
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi62 – 7312
Turni74 – 763
Helixi77 – 815
Helixi85 – 10925
Turni110 – 1145

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KW6NMR-A/B61-115[»]
ProteinModelPortaliO14519.
SMRiO14519. Positions 62-115.

Miscellaneous databases

EvolutionaryTraceiO14519.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 6060intrinsically disorderedAdd
BLAST

Sequence similaritiesi

Belongs to the CDK2AP family.

Phylogenomic databases

eggNOGiNOG235568.
HOGENOMiHOG000035115.
HOVERGENiHBG002074.
InParanoidiO14519.
OMAiCAICTHY.
OrthoDBiEOG71RXN6.
PhylomeDBiO14519.
TreeFamiTF101037.

Family and domain databases

InterProiIPR017266. CDK2-associated_2.
IPR019187. Cyclin-dep_kinase2-assoc_pr.
[Graphical view]
PfamiPF09806. CDK2AP. 1 hit.
[Graphical view]
PIRSFiPIRSF037709. CDK2-associated_p2. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O14519-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSYKPNLAAH MPAAALNAAG SVHSPSTSMA TSSQYRQLLS DYGPPSLGYT    50
QGTGNSQVPQ SKYAELLAII EELGKEIRPT YAGSKSAMER LKRGIIHARG 100
LVRECLAETE RNARS 115
Length:115
Mass (Da):12,365
Last modified:January 1, 1998 - v1
Checksum:iF3149F72467598C2
GO
Isoform 2 (identifier: O14519-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Note: No experimental confirmation available.

Show »
Length:87
Mass (Da):9,601
Checksum:i6B823B0C04D5D88A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828Missing in isoform 2. VSP_046436Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB006077 mRNA. Translation: BAA22937.1.
AF006484 mRNA. Translation: AAC77831.1.
DB465022 mRNA. No translation available.
AC068768 Genomic DNA. No translation available.
BC034717 mRNA. Translation: AAH34717.1.
CCDSiCCDS58289.1. [O14519-2]
CCDS9245.1. [O14519-1]
RefSeqiNP_001257362.1. NM_001270433.1. [O14519-2]
NP_001257363.1. NM_001270434.1. [O14519-2]
NP_004633.1. NM_004642.3. [O14519-1]
UniGeneiHs.433201.

Genome annotation databases

EnsembliENST00000261692; ENSP00000261692; ENSG00000111328. [O14519-1]
ENST00000535979; ENSP00000442565; ENSG00000111328. [O14519-2]
ENST00000538446; ENSP00000442502; ENSG00000111328. [O14519-2]
ENST00000542174; ENSP00000440729; ENSG00000111328. [O14519-2]
ENST00000544658; ENSP00000438561; ENSG00000111328. [O14519-2]
GeneIDi8099.
KEGGihsa:8099.
UCSCiuc001ueq.4. human. [O14519-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB006077 mRNA. Translation: BAA22937.1 .
AF006484 mRNA. Translation: AAC77831.1 .
DB465022 mRNA. No translation available.
AC068768 Genomic DNA. No translation available.
BC034717 mRNA. Translation: AAH34717.1 .
CCDSi CCDS58289.1. [O14519-2 ]
CCDS9245.1. [O14519-1 ]
RefSeqi NP_001257362.1. NM_001270433.1. [O14519-2 ]
NP_001257363.1. NM_001270434.1. [O14519-2 ]
NP_004633.1. NM_004642.3. [O14519-1 ]
UniGenei Hs.433201.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KW6 NMR - A/B 61-115 [» ]
ProteinModelPortali O14519.
SMRi O14519. Positions 62-115.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113770. 19 interactions.
IntActi O14519. 5 interactions.
MINTi MINT-88804.
STRINGi 9606.ENSP00000261692.

Chemistry

BindingDBi O14519.
ChEMBLi CHEMBL5578.

PTM databases

PhosphoSitei O14519.

Proteomic databases

MaxQBi O14519.
PaxDbi O14519.
PRIDEi O14519.

Protocols and materials databases

DNASUi 8099.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261692 ; ENSP00000261692 ; ENSG00000111328 . [O14519-1 ]
ENST00000535979 ; ENSP00000442565 ; ENSG00000111328 . [O14519-2 ]
ENST00000538446 ; ENSP00000442502 ; ENSG00000111328 . [O14519-2 ]
ENST00000542174 ; ENSP00000440729 ; ENSG00000111328 . [O14519-2 ]
ENST00000544658 ; ENSP00000438561 ; ENSG00000111328 . [O14519-2 ]
GeneIDi 8099.
KEGGi hsa:8099.
UCSCi uc001ueq.4. human. [O14519-1 ]

Organism-specific databases

CTDi 8099.
GeneCardsi GC12M123745.
HGNCi HGNC:14002. CDK2AP1.
HPAi CAB019377.
MIMi 602198. gene.
neXtProti NX_O14519.
PharmGKBi PA26308.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG235568.
HOGENOMi HOG000035115.
HOVERGENi HBG002074.
InParanoidi O14519.
OMAi CAICTHY.
OrthoDBi EOG71RXN6.
PhylomeDBi O14519.
TreeFami TF101037.

Miscellaneous databases

EvolutionaryTracei O14519.
GeneWikii CDK2AP1.
GenomeRNAii 8099.
NextBioi 30740.
PROi O14519.
SOURCEi Search...

Gene expression databases

ArrayExpressi O14519.
Bgeei O14519.
CleanExi HS_CDK2AP1.
Genevestigatori O14519.

Family and domain databases

InterProi IPR017266. CDK2-associated_2.
IPR019187. Cyclin-dep_kinase2-assoc_pr.
[Graphical view ]
Pfami PF09806. CDK2AP. 1 hit.
[Graphical view ]
PIRSFi PIRSF037709. CDK2-associated_p2. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation, mapping and mutation analysis of a human cDNA homologous to the doc-1 gene of the Chinese hamster, a candidate tumor suppressor for oral cancer."
    Daigo Y., Suzuki K., Maruyama O., Miyoshi Y., Yasuda T., Kabuto T., Imaoka S., Fujiwara T., Takahashi E., Fujino M.A., Nakamura Y.
    Genes Chromosomes Cancer 20:204-207(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning, mapping, expression, function, and mutation analyses of the human ortholog of the hamster putative tumor suppressor gene Doc-1."
    Tsuji T., Duh F.-M., Latif F., Popescu N.C., Zimonjic D.B., McBride J., Matsuo K., Ohyama H., Todd R., Nagata E., Terakado N., Sasaki A., Matsumura T., Lerman M.I., Wong D.T.
    J. Biol. Chem. 273:6704-6709(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Skin.
  6. "Human cyclin-dependent kinase 2-associated protein 1 (CDK2AP1) is dimeric in its disulfide-reduced state, with natively disordered N-terminal region."
    Ertekin A., Aramini J.M., Rossi P., Leonard P.G., Janjua H., Xiao R., Maglaqui M., Lee H.W., Prestegard J.H., Montelione G.T.
    J. Biol. Chem. 287:16541-16549(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 61-115, SUBUNIT, PHOSPHORYLATION AT SER-46, DISULFIDE BOND, MUTAGENESIS OF CYS-105.

Entry informationi

Entry nameiCDKA1_HUMAN
AccessioniPrimary (citable) accession number: O14519
Secondary accession number(s): F5GYA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 113 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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