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Q810P3 (CDKN3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-dependent kinase inhibitor 3
EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
CDK2-associated dual-specificity phosphatase
Kinase-associated phosphatase
Gene names
Name:Cdkn3
Synonyms:Kap
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May play a role in cell cycle regulation. Dual specificity phosphatase active toward substrates containing either phosphotyrosine or phosphoserine residues. Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner By similarity. UniProtKB Q16667

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. UniProtKB Q16667

A phosphoprotein + H2O = a protein + phosphate. UniProtKB Q16667

Subunit structure

Interacts with cyclin-dependent kinases such as CDK1, CDK2 and CDK3. Does not interact with CDK4. Interacts (via C-terminus) with phosphorylated CDK2 (via C-terminal helix). Interacts with MS4A3 (via C-terminus); the interaction enhances CDKN3 enzymatic activity By similarity. UniProtKB Q16667

Subcellular location

Cytoplasm › perinuclear region By similarity UniProtKB Q16667.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family.

Sequence caution

The sequence BAB26929.1 differs from that shown. Reason: Probable cloning artifact.

The sequence BAC28238.1 differs from that shown. Reason: Probable cloning artifact.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCytoplasm
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle arrest

Inferred from electronic annotation. Source: Compara

   Cellular_componentperinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionprotein serine/threonine phosphatase activity

Inferred from electronic annotation. Source: Compara

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211Cyclin-dependent kinase inhibitor 3
PRO_0000396637

Regions

Region1 – 3434Interaction with CDK2 By similarity UniProtKB Q16667

Sites

Active site1401 By similarity UniProtKB Q16667

Sequences

Sequence LengthMass (Da)Tools
Q810P3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: A119D81C61A7F20F

FASTA21123,793
        10         20         30         40         50         60 
MKPPISIQAS EFDSSDEEPV DEEQTPIQIS WLPLSRVNCS QFLGLCALPG CKFKDVRRNI 

        70         80         90        100        110        120 
QKDTEELKSY GIQDVFVFCT RGELSKYRVP NLLDLYQQYG IVTHHHPIPD GGTPDIGSCW 

       130        140        150        160        170        180 
EIMEELATCL KNNRKTLIHC YGGLGRSCLA ACLLLYLSDS ISPQQAIDSL RDVRGSGAIQ 

       190        200        210 
TIKQYNYLHE FRDKLAAYLS SRDSLSRSVS R

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and DBA/2.
Tissue: Embryonic stem cell and Embryonic testis.
[2]"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: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK010426 mRNA. Translation: BAB26929.1. Sequence problems.
AK033341 mRNA. Translation: BAC28238.1. Sequence problems.
AK146312 mRNA. Translation: BAE27067.1.
BC049694 mRNA. Translation: AAH49694.1.
IPIIPI00944059.
RefSeqNP_082498.1. NM_028222.1.
UniGeneMm.272394.

3D structure databases

HSSPHSSP built from PDB template 1FQ1 based on UniProtKB Q9C053.
ProteinModelPortalQ810P3.
SMRQ810P3. Positions 23-199.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000070575.

PTM databases

PhosphoSiteQ810P3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067426; ENSMUSP00000070575; ENSMUSG00000037628.
GeneID72391.
KEGGmmu:72391.
UCSCuc007the.2. mouse.

Organism-specific databases

CTD1033.
MGIMGI:1919641. Cdkn3.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00390000004717.
HOGENOMHOG000060336.
HOVERGENHBG075798.
InParanoidQ810P3.
KOK14167.
OMAQYGIITH.
OrthoDBEOG49W2GK.

Gene expression databases

BgeeQ810P3.
GenevestigatorQ810P3.

Family and domain databases

InterProIPR008425. CDK_inhib_3.
IPR022778. CDKN3.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]
PfamPF05706. CDKN3. 1 hit.
[Graphical view]
PIRSFPIRSF037322. CDKN3. 1 hit.
PROSITEPS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDKN3. mouse.
NextBio336166.
SOURCESearch...

Entry information

Entry nameCDKN3_MOUSE
AccessionPrimary (citable) accession number: Q810P3
Secondary accession number(s): Q9CWS3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: June 1, 2003
Last modified: April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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