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Protein
Submitted name:

CDC2L5 protein

Gene

CDK13

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinaseUniRule annotation, Transferase

Keywords - Ligandi

ATP-bindingUniRule annotation, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Submitted name:
CDC2L5 proteinImported
Submitted name:
Cyclin-dependent kinase 13Imported
Gene namesi
Name:CDK13Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:1733. CDK13.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26264.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000181839.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini91 – 324234Protein kinaseInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG0600. Eukaryota.
ENOG410XPIR. LUCA.
GeneTreeiENSGT00830000128304.
HOGENOMiHOG000152150.
KOiK08819.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BVE2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPEDKEADS LRGNISVKAV KKEVEKKLRC LLADLPLPPE LPGGDDLSKS
60 70 80 90 100
PEEKKTATQL HSKRRPKICG PRYGETKEKD IDWGKRCVDK FDIIGIIGEG
110 120 130 140 150
TYGQVYKARD KDTGEMVALK KVRLDNEKEG FPITAIREIK ILRQLTHQSI
160 170 180 190 200
INMKEIVTDK EDALDFKKDK GAFYLVFEYM DHDLMGLLES GLVHFNENHI
210 220 230 240 250
KSFMRQLMEG LDYCHKKNFL HRDIKCSNIL LNNRGQIKLA DFGLARLYSS
260 270 280 290 300
EESRPYTNKV ITLWYRPPEL LLGEERYTPA IDVWSCGCIL GELFTKKPIF
310 320
QANQELAQLE LIRHEENEVS DKQI
Length:324
Mass (Da):37,339
Last modified:June 1, 2001 - v1
Checksum:i5433011D95D0F2CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC006023 Genomic DNA. No translation available.
AC072061 Genomic DNA. No translation available.
BC001274 mRNA. Translation: AAH01274.1.
RefSeqiNP_003709.3. NM_003718.4.
NP_112557.2. NM_031267.3.
UniGeneiHs.233552.

Genome annotation databases

EnsembliENST00000613626; ENSP00000480835; ENSG00000065883.
GeneIDi8621.
KEGGihsa:8621.
UCSCiuc064dab.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC006023 Genomic DNA. No translation available.
AC072061 Genomic DNA. No translation available.
BC001274 mRNA. Translation: AAH01274.1.
RefSeqiNP_003709.3. NM_003718.4.
NP_112557.2. NM_031267.3.
UniGeneiHs.233552.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000181839.

Protocols and materials databases

DNASUi8621.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000613626; ENSP00000480835; ENSG00000065883.
GeneIDi8621.
KEGGihsa:8621.
UCSCiuc064dab.1. human.

Organism-specific databases

CTDi8621.
HGNCiHGNC:1733. CDK13.
PharmGKBiPA26264.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0600. Eukaryota.
ENOG410XPIR. LUCA.
GeneTreeiENSGT00830000128304.
HOGENOMiHOG000152150.
KOiK08819.

Miscellaneous databases

GenomeRNAii8621.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: PlacentaImported.
  3. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Ensembl
    Submitted (SEP-2014) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiQ9BVE2_HUMAN
AccessioniPrimary (citable) accession number: Q9BVE2
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2001
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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 one 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.