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Q9P1W9

- PIM2_HUMAN

UniProt

Q9P1W9 - PIM2_HUMAN

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Protein

Serine/threonine-protein kinase pim-2

Gene
PIM2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression, the regulation of cap-dependent protein translation and through survival signaling by phosphorylation of a pro-apoptotic protein, BAD. Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase transcriptional activity. The stabilization of MYC exerted by PIM2 might explain partly the strong synergism between these 2 oncogenes in tumorigenesis. Regulates cap-dependent protein translation in a mammalian target of rapamycin complex 1 (mTORC1)-independent manner and in parallel to the PI3K-Akt pathway. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Promotes cell survival in response to a variety of proliferative signals via positive regulation of the I-kappa-B kinase/NF-kappa-B cascade; this process requires phosphorylation of MAP3K8/COT. Isoform 1 is less active in this respect. Promotes growth factor-independent proliferation by phosphorylation of cell cycle factors such as CDKN1A and CDKN1B. Involved in the positive regulation of chondrocyte survival and autophagy in the epiphyseal growth plate.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei61 – 611ATP By similarity
Active sitei163 – 1631Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi38 – 469ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. apoptotic mitochondrial changes Source: Ensembl
  2. cell proliferation Source: ProtInc
  3. G1/S transition of mitotic cell cycle Source: UniProtKB
  4. male meiosis Source: ProtInc
  5. negative regulation of apoptotic process Source: UniProtKB
  6. negative regulation of cell proliferation Source: UniProtKB
  7. positive regulation of autophagy Source: UniProtKB
  8. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  9. positive regulation of transcription, DNA-templated Source: UniProtKB
  10. protein phosphorylation Source: UniProtKB
  11. protein stabilization Source: UniProtKB
  12. response to virus Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ9P1W9.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase pim-2 (EC:2.7.11.1)
Alternative name(s):
Pim-2h
Gene namesi
Name:PIM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:8987. PIM2.

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA33319.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 311311Serine/threonine-protein kinase pim-2PRO_0000086532Add
BLAST

Post-translational modificationi

Autophosphorylated By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9P1W9.
PaxDbiQ9P1W9.
PRIDEiQ9P1W9.

PTM databases

PhosphoSiteiQ9P1W9.

Expressioni

Tissue specificityi

Highly expressed in hematopoietic tissues, in leukemic and lymphoma cell lines, testis, small intestine, colon and colorectal adenocarcinoma cells. Weakly expressed in normal liver, but highly expressed in hepatocellular carcinoma tissues.1 Publication

Inductioni

Down-regulated in response to enterovirus 71 (EV71) infection.1 Publication

Gene expression databases

ArrayExpressiQ9P1W9.
BgeeiQ9P1W9.
CleanExiHS_PIM2.
GenevestigatoriQ9P1W9.

Organism-specific databases

HPAiHPA000285.

Interactioni

Subunit structurei

Interacts with MYC By similarity.

Protein-protein interaction databases

BioGridi116228. 9 interactions.
IntActiQ9P1W9. 9 interactions.
MINTiMINT-1432143.
STRINGi9606.ENSP00000365692.

Structurei

Secondary structure

1
311
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 419
Beta strandi44 – 507
Turni52 – 543
Beta strandi57 – 626
Turni66 – 683
Helixi82 – 9110
Beta strandi97 – 993
Beta strandi102 – 1054
Beta strandi113 – 1175
Beta strandi120 – 1245
Helixi125 – 1328
Helixi137 – 15721
Helixi166 – 1683
Beta strandi169 – 1724
Turni173 – 1764
Beta strandi177 – 1804
Turni201 – 2033
Helixi206 – 2116
Helixi216 – 23318
Helixi241 – 2466
Helixi257 – 26610
Turni271 – 2733
Helixi277 – 2826
Turni284 – 2863

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IWIX-ray2.80A/B1-311[»]
ProteinModelPortaliQ9P1W9.
SMRiQ9P1W9. Positions 32-288.

Miscellaneous databases

EvolutionaryTraceiQ9P1W9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 286255Protein kinaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000231357.
HOVERGENiHBG106681.
InParanoidiQ9P1W9.
KOiK08806.
OMAiASTPCGL.
PhylomeDBiQ9P1W9.
TreeFamiTF320810.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
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.

Q9P1W9-1 [UniParc]FASTAAdd to Basket

« Hide

MLTKPLQGPP APPGTPTPPP GGKDREAFEA EYRLGPLLGK GGFGTVFAGH    50
RLTDRLQVAI KVIPRNRVLG WSPLSDSVTC PLEVALLWKV GAGGGHPGVI 100
RLLDWFETQE GFMLVLERPL PAQDLFDYIT EKGPLGEGPS RCFFGQVVAA 150
IQHCHSRGVV HRDIKDENIL IDLRRGCAKL IDFGSGALLH DEPYTDFDGT 200
RVYSPPEWIS RHQYHALPAT VWSLGILLYD MVCGDIPFER DQEILEAELH 250
FPAHVSPDCC ALIRRCLAPK PSSRPSLEEI LLDPWMQTPA EDVPLNPSKG 300
GPAPLAWSLL P 311
Length:311
Mass (Da):34,190
Last modified:October 1, 2000 - v1
Checksum:i160E56C368C67A69
GO

Sequence cautioni

The sequence AAC78506.1 differs from that shown. Reason: Frameshift at position 293.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti138 – 1381G → D.1 Publication
Corresponds to variant rs35044770 [ dbSNP | Ensembl ].
VAR_041008
Natural varianti280 – 2801I → V.1 Publication
Corresponds to variant rs35208542 [ dbSNP | Ensembl ].
VAR_041009

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661N → Y in BAF83620. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U77735 mRNA. Translation: AAC78506.1. Frameshift.
AK290931 mRNA. Translation: BAF83620.1.
AB042425 Genomic DNA. Translation: BAA95613.1.
AF207550 Genomic DNA. No translation available.
BC018111 mRNA. Translation: AAH18111.1.
CCDSiCCDS14312.1.
RefSeqiNP_006866.2. NM_006875.3.
UniGeneiHs.727148.

Genome annotation databases

EnsembliENST00000376509; ENSP00000365692; ENSG00000102096.
ENST00000601083; ENSP00000469116; ENSG00000267878.
GeneIDi11040.
KEGGihsa:11040.
UCSCiuc004dls.3. human.

Polymorphism databases

DMDMi20139243.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U77735 mRNA. Translation: AAC78506.1 . Frameshift.
AK290931 mRNA. Translation: BAF83620.1 .
AB042425 Genomic DNA. Translation: BAA95613.1 .
AF207550 Genomic DNA. No translation available.
BC018111 mRNA. Translation: AAH18111.1 .
CCDSi CCDS14312.1.
RefSeqi NP_006866.2. NM_006875.3.
UniGenei Hs.727148.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2IWI X-ray 2.80 A/B 1-311 [» ]
ProteinModelPortali Q9P1W9.
SMRi Q9P1W9. Positions 32-288.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116228. 9 interactions.
IntActi Q9P1W9. 9 interactions.
MINTi MINT-1432143.
STRINGi 9606.ENSP00000365692.

Chemistry

BindingDBi Q9P1W9.
ChEMBLi CHEMBL4523.
GuidetoPHARMACOLOGYi 2159.

PTM databases

PhosphoSitei Q9P1W9.

Polymorphism databases

DMDMi 20139243.

Proteomic databases

MaxQBi Q9P1W9.
PaxDbi Q9P1W9.
PRIDEi Q9P1W9.

Protocols and materials databases

DNASUi 11040.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000376509 ; ENSP00000365692 ; ENSG00000102096 .
ENST00000601083 ; ENSP00000469116 ; ENSG00000267878 .
GeneIDi 11040.
KEGGi hsa:11040.
UCSCi uc004dls.3. human.

Organism-specific databases

CTDi 11040.
GeneCardsi GC0XM048770.
HGNCi HGNC:8987. PIM2.
HPAi HPA000285.
MIMi 300295. gene.
neXtProti NX_Q9P1W9.
PharmGKBi PA33319.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000231357.
HOVERGENi HBG106681.
InParanoidi Q9P1W9.
KOi K08806.
OMAi ASTPCGL.
PhylomeDBi Q9P1W9.
TreeFami TF320810.

Enzyme and pathway databases

SignaLinki Q9P1W9.

Miscellaneous databases

ChiTaRSi PIM2. human.
EvolutionaryTracei Q9P1W9.
GeneWikii PIM2_(gene).
GenomeRNAii 11040.
NextBioi 41955.
PROi Q9P1W9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9P1W9.
Bgeei Q9P1W9.
CleanExi HS_PIM2.
Genevestigatori Q9P1W9.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The human Pim-2 proto-oncogene and its testicular expression."
    Baytel D., Shalom S., Madgar I., Weissenberg R., Don J.
    Biochim. Biophys. Acta 1442:274-285(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  2. "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].
  3. "Genomic organization of the human UDP-galactose transporter gene."
    Ishida N., Miura N., Yamauchi M., Kawakita M.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [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].
    Tissue: Uterus.
  6. "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
    Leong W.F., Chow V.T.
    Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Pim kinases promote cell cycle progression by phosphorylating and down-regulating p27Kip1 at the transcriptional and posttranscriptional levels."
    Morishita D., Katayama R., Sekimizu K., Tsuruo T., Fujita N.
    Cancer Res. 68:5076-5085(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CDKN1B.
  8. "Serine/threonine kinase Pim-2 promotes liver tumorigenesis induction through mediating survival and preventing apoptosis of liver cell."
    Gong J., Wang J., Ren K., Liu C., Li B., Shi Y.
    J. Surg. Res. 153:17-22(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  9. "Pim-2 phosphorylation of p21(Cip1/WAF1) enhances its stability and inhibits cell proliferation in HCT116 cells."
    Wang Z., Zhang Y., Gu J.J., Davitt C., Reeves R., Magnuson N.S.
    Int. J. Biochem. Cell Biol. 42:1030-1038(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CDKN1A.
  10. "Crystal structure of the PIM2 kinase in complex with an organoruthenium inhibitor."
    Bullock A.N., Russo S., Amos A., Pagano N., Bregman H., Debreczeni J.E., Lee W.H., von Delft F., Meggers E., Knapp S.
    PLoS ONE 4:E7112-E7112(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH RUTHENIUM-PYRIDOCARBAZOLE-1.
  11. "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] ASP-138 AND VAL-280.

Entry informationi

Entry nameiPIM2_HUMAN
AccessioniPrimary (citable) accession number: Q9P1W9
Secondary accession number(s): A8K4G6, Q99739
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 123 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 X
    Human chromosome X: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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