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Protein

Cyclin-dependent kinase 2-associated protein 1

Gene

CDK2AP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 polymerase binding Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. DNA-dependent DNA replication Source: UniProtKB
  3. positive regulation of protein phosphorylation Source: UniProtKB
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. nucleus Source: UniProtKB
  2. perinuclear region of cytoplasm Source: UniProtKB
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 – 105InterchainSequence Analysis

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

BgeeiO14519.
CleanExiHS_CDK2AP1.
ExpressionAtlasiO14519. baseline and differential.
GenevestigatoriO14519.

Organism-specific databases

HPAiCAB019377.

Interactioni

Subunit structurei

Homodimer. Interacts with monomeric unphosphorylated CDK2.1 Publication

Protein-protein interaction databases

BioGridi113770. 24 interactions.
IntActiO14519. 16 interactions.
MINTiMINT-88804.
STRINGi9606.ENSP00000261692.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KW6NMR-A/B61-115[»]
ProteinModelPortaliO14519.
SMRiO14519. Positions 62-115.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14519.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the CDK2AP family.Curated

Phylogenomic databases

eggNOGiNOG235568.
GeneTreeiENSGT00390000006964.
HOGENOMiHOG000035115.
HOVERGENiHBG002074.
InParanoidiO14519.
OMAiVHQHIPG.
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

        10         20         30         40         50
MSYKPNLAAH MPAAALNAAG SVHSPSTSMA TSSQYRQLLS DYGPPSLGYT
60 70 80 90 100
QGTGNSQVPQ SKYAELLAII EELGKEIRPT YAGSKSAMER LKRGIIHARG
110
LVRECLAETE RNARS
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. 1 PublicationVSP_046436Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
ENST00000618072; ENSP00000479982; 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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KW6NMR-A/B61-115[»]
ProteinModelPortaliO14519.
SMRiO14519. Positions 62-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113770. 24 interactions.
IntActiO14519. 16 interactions.
MINTiMINT-88804.
STRINGi9606.ENSP00000261692.

Chemistry

BindingDBiO14519.
ChEMBLiCHEMBL5578.

PTM databases

PhosphoSiteiO14519.

Proteomic databases

MaxQBiO14519.
PaxDbiO14519.
PRIDEiO14519.

Protocols and materials databases

DNASUi8099.
Structural Biology KnowledgebaseSearch...

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]
ENST00000618072; ENSP00000479982; ENSG00000111328. [O14519-2]
GeneIDi8099.
KEGGihsa:8099.
UCSCiuc001ueq.4. human. [O14519-1]

Organism-specific databases

CTDi8099.
GeneCardsiGC12M123745.
HGNCiHGNC:14002. CDK2AP1.
HPAiCAB019377.
MIMi602198. gene.
neXtProtiNX_O14519.
PharmGKBiPA26308.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG235568.
GeneTreeiENSGT00390000006964.
HOGENOMiHOG000035115.
HOVERGENiHBG002074.
InParanoidiO14519.
OMAiVHQHIPG.
OrthoDBiEOG71RXN6.
PhylomeDBiO14519.
TreeFamiTF101037.

Miscellaneous databases

ChiTaRSiCDK2AP1. human.
EvolutionaryTraceiO14519.
GeneWikiiCDK2AP1.
GenomeRNAii8099.
NextBioi30740.
PROiO14519.
SOURCEiSearch...

Gene expression databases

BgeeiO14519.
CleanExiHS_CDK2AP1.
ExpressionAtlasiO14519. baseline and differential.
GenevestigatoriO14519.

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.
ProtoNetiSearch...

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: February 4, 2015
This is version 118 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.