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Protein

Lymphokine-activated killer T-cell-originated protein kinase

Gene

PBK

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

Functioni

Phosphorylates MAP kinase p38. Seems to be active only in mitosis. May also play a role in the activation of lymphoid cells. When phosphorylated, forms a complex with TP53, leading to TP53 destabilization and attenuation of G2/M checkpoint during doxorubicin-induced DNA damage.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by phosphorylation.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei64 – 641ATPPROSITE-ProRule annotation
Active sitei167 – 1671Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi38 – 469ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ96KB5.

Names & Taxonomyi

Protein namesi
Recommended name:
Lymphokine-activated killer T-cell-originated protein kinase (EC:2.7.12.2)
Alternative name(s):
Cancer/testis antigen 84
Short name:
CT84
MAPKK-like protein kinase
Nori-3
PDZ-binding kinase
Spermatogenesis-related protein kinase
Short name:
SPK
T-LAK cell-originated protein kinase
Gene namesi
Name:PBK
Synonyms:TOPK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:18282. PBK.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: CACAO
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91T → E: TP53-binding. 1 Publication
Mutagenesisi64 – 652KK → AA: Loss of activity. 1 Publication
Mutagenesisi320 – 3201T → A: Decrease in the binding to DLG1. 1 Publication
Mutagenesisi322 – 3221V → A: Decrease in the binding to DLG1. 1 Publication

Organism-specific databases

PharmGKBiPA134925802.

Polymorphism and mutation databases

BioMutaiPBK.
DMDMi83305809.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 322322Lymphokine-activated killer T-cell-originated protein kinasePRO_0000086763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei9 – 91Phosphothreonine1 Publication
Modified residuei24 – 241Phosphothreonine1 Publication
Modified residuei32 – 321Phosphoserine2 Publications
Modified residuei59 – 591Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated; in a cell-cycle dependent manner at mitosis.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ96KB5.
PeptideAtlasiQ96KB5.
PRIDEiQ96KB5.

PTM databases

PhosphoSiteiQ96KB5.

Expressioni

Tissue specificityi

Expressed in the testis and placenta. In the testis, restrictedly expressed in outer cell layer of seminiferous tubules.2 Publications

Gene expression databases

BgeeiQ96KB5.
CleanExiHS_PBK.
ExpressionAtlasiQ96KB5. baseline and differential.
GenevisibleiQ96KB5. HS.

Organism-specific databases

HPAiHPA005753.

Interactioni

Subunit structurei

Interacts with DLG1 and TP53.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARAFP103983EBI-536853,EBI-365961
TP53P046377EBI-536853,EBI-366083

Protein-protein interaction databases

BioGridi120971. 25 interactions.
IntActiQ96KB5. 9 interactions.
MINTiMINT-130347.
STRINGi9606.ENSP00000301905.

Structurei

3D structure databases

ProteinModelPortaliQ96KB5.
SMRiQ96KB5. Positions 79-316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 322291Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni320 – 3223PDZ-interaction

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00720000108839.
HOGENOMiHOG000294208.
HOVERGENiHBG056011.
InParanoidiQ96KB5.
KOiK08865.
OMAiELFYLCT.
OrthoDBiEOG7S4X6F.
PhylomeDBiQ96KB5.
TreeFamiTF329763.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96KB5-1) [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
MEGISNFKTP SKLSEKKKSV LCSTPTINIP ASPFMQKLGF GTGVNVYLMK
60 70 80 90 100
RSPRGLSHSP WAVKKINPIC NDHYRSVYQK RLMDEAKILK SLHHPNIVGY
110 120 130 140 150
RAFTEANDGS LCLAMEYGGE KSLNDLIEER YKASQDPFPA AIILKVALNM
160 170 180 190 200
ARGLKYLHQE KKLLHGDIKS SNVVIKGDFE TIKICDVGVS LPLDENMTVT
210 220 230 240 250
DPEACYIGTE PWKPKEAVEE NGVITDKADI FAFGLTLWEM MTLSIPHINL
260 270 280 290 300
SNDDDDEDKT FDESDFDDEA YYAALGTRPP INMEELDESY QKVIELFSVC
310 320
TNEDPKDRPS AAHIVEALET DV
Length:322
Mass (Da):36,085
Last modified:December 6, 2005 - v3
Checksum:i6BF55789BC204ABE
GO
Isoform 2 (identifier: Q96KB5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     198-198: T → TAPAFITILLVS

Note: No experimental confirmation available.
Show »
Length:333
Mass (Da):37,211
Checksum:i05A472E8DD4D9928
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341F → I in AAF71521 (PubMed:11378444).Curated
Sequence conflicti169 – 1691K → E in BAB55019 (PubMed:14702039).Curated
Sequence conflicti254 – 2541D → N in BAB55019 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071N → S.4 Publications
Corresponds to variant rs3779620 [ dbSNP | Ensembl ].
VAR_021162
Natural varianti220 – 2201E → D.
Corresponds to variant rs17057901 [ dbSNP | Ensembl ].
VAR_051676
Natural varianti241 – 2411M → L.1 Publication
Corresponds to variant rs36086402 [ dbSNP | Ensembl ].
VAR_041234

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei198 – 1981T → TAPAFITILLVS in isoform 2. 1 PublicationVSP_055269

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027249 mRNA. Translation: BAA99576.1.
AB027250 mRNA. Translation: BAA99577.1.
AF189722 mRNA. Translation: AAF69107.1.
AF237709 mRNA. Translation: AAF71521.1.
AK027291 mRNA. Translation: BAB55019.1.
AK301836 mRNA. Translation: BAG63280.1.
AC104997 Genomic DNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63536.1.
CH471080 Genomic DNA. Translation: EAW63537.1.
BC015191 mRNA. Translation: AAH15191.1.
CCDSiCCDS6063.1. [Q96KB5-1]
CCDS64858.1. [Q96KB5-2]
RefSeqiNP_001265874.1. NM_001278945.1. [Q96KB5-2]
NP_060962.2. NM_018492.3. [Q96KB5-1]
XP_006716431.1. XM_006716368.2. [Q96KB5-1]
UniGeneiHs.104741.

Genome annotation databases

EnsembliENST00000301905; ENSP00000301905; ENSG00000168078.
ENST00000522944; ENSP00000428489; ENSG00000168078. [Q96KB5-2]
GeneIDi55872.
KEGGihsa:55872.
UCSCiuc003xgi.3. human. [Q96KB5-1]
uc011lap.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027249 mRNA. Translation: BAA99576.1.
AB027250 mRNA. Translation: BAA99577.1.
AF189722 mRNA. Translation: AAF69107.1.
AF237709 mRNA. Translation: AAF71521.1.
AK027291 mRNA. Translation: BAB55019.1.
AK301836 mRNA. Translation: BAG63280.1.
AC104997 Genomic DNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63536.1.
CH471080 Genomic DNA. Translation: EAW63537.1.
BC015191 mRNA. Translation: AAH15191.1.
CCDSiCCDS6063.1. [Q96KB5-1]
CCDS64858.1. [Q96KB5-2]
RefSeqiNP_001265874.1. NM_001278945.1. [Q96KB5-2]
NP_060962.2. NM_018492.3. [Q96KB5-1]
XP_006716431.1. XM_006716368.2. [Q96KB5-1]
UniGeneiHs.104741.

3D structure databases

ProteinModelPortaliQ96KB5.
SMRiQ96KB5. Positions 79-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120971. 25 interactions.
IntActiQ96KB5. 9 interactions.
MINTiMINT-130347.
STRINGi9606.ENSP00000301905.

Chemistry

ChEMBLiCHEMBL4896.
GuidetoPHARMACOLOGYi2140.

PTM databases

PhosphoSiteiQ96KB5.

Polymorphism and mutation databases

BioMutaiPBK.
DMDMi83305809.

Proteomic databases

PaxDbiQ96KB5.
PeptideAtlasiQ96KB5.
PRIDEiQ96KB5.

Protocols and materials databases

DNASUi55872.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301905; ENSP00000301905; ENSG00000168078.
ENST00000522944; ENSP00000428489; ENSG00000168078. [Q96KB5-2]
GeneIDi55872.
KEGGihsa:55872.
UCSCiuc003xgi.3. human. [Q96KB5-1]
uc011lap.2. human.

Organism-specific databases

CTDi55872.
GeneCardsiGC08M027724.
HGNCiHGNC:18282. PBK.
HPAiHPA005753.
MIMi611210. gene.
neXtProtiNX_Q96KB5.
PharmGKBiPA134925802.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00720000108839.
HOGENOMiHOG000294208.
HOVERGENiHBG056011.
InParanoidiQ96KB5.
KOiK08865.
OMAiELFYLCT.
OrthoDBiEOG7S4X6F.
PhylomeDBiQ96KB5.
TreeFamiTF329763.

Enzyme and pathway databases

SignaLinkiQ96KB5.

Miscellaneous databases

ChiTaRSiPBK. human.
GeneWikiiPBK_(gene).
GenomeRNAii55872.
NextBioi35475910.
PROiQ96KB5.
SOURCEiSearch...

Gene expression databases

BgeeiQ96KB5.
CleanExiHS_PBK.
ExpressionAtlasiQ96KB5. baseline and differential.
GenevisibleiQ96KB5. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a novel MAPKK-like protein kinase, lymphokine-activated killer T-cell-originated protein kinase, specifically expressed in the testis and activated lymphoid cells."
    Abe Y., Matsumoto S., Kito K., Ueda N.
    J. Biol. Chem. 275:21525-21531(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION, TISSUE SPECIFICITY.
    Tissue: Lymphoid tissue.
  2. "Characterization of PDZ-binding kinase, a mitotic kinase."
    Gaudet S., Branton D., Lue R.A.
    Proc. Natl. Acad. Sci. U.S.A. 97:5167-5172(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION, MUTAGENESIS OF 64-LEU-LEU-65; THR-320 AND VAL-322, INTERACTION WITH DLG1, VARIANT SER-107.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT SER-107.
    Tissue: Fetal brain.
  4. "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.
    , 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] (ISOFORMS 1 AND 2), VARIANT SER-107.
    Tissue: Embryo and Testis.
  5. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Brain.
  8. "Attenuation of DNA damage checkpoint by PBK, a novel mitotic kinase, involves protein-protein interaction with tumor suppressor p53."
    Nandi A.K., Ford T., Fleksher D., Neuman B., Rapoport A.P.
    Biochem. Biophys. Res. Commun. 358:181-188(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TP53, MUTAGENESIS OF THR-9.
  9. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24; SER-32 AND SER-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9; SER-32 AND SER-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-107 AND LEU-241.

Entry informationi

Entry nameiTOPK_HUMAN
AccessioniPrimary (citable) accession number: Q96KB5
Secondary accession number(s): B4DX68
, D3DST2, Q9NPD9, Q9NYL7, Q9NZK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: December 6, 2005
Last modified: July 22, 2015
This is version 126 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. 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.