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Q9P286 (PAK7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase PAK 7

EC=2.7.11.1
Alternative name(s):
p21-activated kinase 5
Short name=PAK-5
p21-activated kinase 7
Short name=PAK-7
Gene names
Name:PAK7
Synonyms:KIAA1264, PAK5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length719 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF1 and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions. Ref.7 Ref.8 Ref.10 Ref.11 Ref.12

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and RAC1. Interacts with MARK2, leading to inhibit MARK2 independently of kinase activity. Interacts with RHOD and RHOH. Ref.8 Ref.9

Subcellular location

Mitochondrion. Cytoplasm. Nucleus. Note: Shuttles between the nucleus and the mitochondria, and mitochondrial localization is essential for the role in cell survival. Ref.7 Ref.10

Tissue specificity

Predominantly expressed in brain.

Domain

An autoinhibitory domain is present in the N-terminal region of the protein. Ref.6

Post-translational modification

Autophosphorylated when activated by CDC42/p21.

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.

Contains 1 CRIB domain.

Contains 1 protein kinase domain.

Sequence caution

The sequence BAA86578.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
Mitochondrion
Nucleus
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Traceable author statement PubMed 20070256. Source: UniProtKB

cell growth

Traceable author statement PubMed 20070256. Source: UniProtKB

cell migration

Traceable author statement PubMed 20070256. Source: UniProtKB

cell proliferation

Traceable author statement PubMed 20070256. Source: UniProtKB

cytoskeleton organization

Traceable author statement PubMed 20070256. Source: UniProtKB

negative regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement PubMed 20070256. Source: UniProtKB

signal transduction by phosphorylation

Inferred from Biological aspect of Ancestor. Source: GOC

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

receptor signaling protein serine/threonine kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 719719Serine/threonine-protein kinase PAK 7
PRO_0000086477

Regions

Domain11 – 2414CRIB
Domain449 – 700252Protein kinase
Nucleotide binding455 – 4639ATP By similarity
Region25 – 448424Linker
Compositional bias4 – 85Poly-Lys
Compositional bias223 – 2264Poly-Ser
Compositional bias367 – 3704Poly-Ser

Sites

Active site5681Proton acceptor By similarity
Binding site4781ATP By similarity

Amino acid modifications

Modified residue1041Phosphoserine By similarity
Modified residue1071Phosphothreonine By similarity

Natural variations

Natural variant1181G → D. Ref.14
Corresponds to variant rs55923311 [ dbSNP | Ensembl ].
VAR_040978
Natural variant1871P → A. Ref.14
Corresponds to variant rs34280805 [ dbSNP | Ensembl ].
VAR_040979
Natural variant3121S → P in a colorectal adenocarcinoma sample; somatic mutation. Ref.14
VAR_040980
Natural variant3351R → P. Ref.14
Corresponds to variant rs11700112 [ dbSNP | Ensembl ].
VAR_040981
Natural variant5111S → N. Ref.3 Ref.14
Corresponds to variant rs2297345 [ dbSNP | Ensembl ].
VAR_021865
Natural variant5381T → N in a lung adenocarcinoma sample; somatic mutation. Ref.14
VAR_040982
Natural variant5551A → S. Ref.14
Corresponds to variant rs34102290 [ dbSNP | Ensembl ].
VAR_040983
Natural variant6041V → I in a metastatic melanoma sample; somatic mutation. Ref.14
VAR_040984
Natural variant7041G → S in a metastatic melanoma sample; somatic mutation. Ref.14
VAR_040985

Experimental info

Mutagenesis19 – 224HRVH → LRVL: Complete loss of CDC42 binding and CDC42-mediated autophosphorylation. Ref.6

Secondary structure

...................................................... 719
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9P286 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 07A12B1EEC4E2A02

FASTA71980,745
        10         20         30         40         50         60 
MFGKKKKKIE ISGPSNFEHR VHTGFDPQEQ KFTGLPQQWH SLLADTANRP KPMVDPSCIT 

        70         80         90        100        110        120 
PIQLAPMKTI VRGNKPCKET SINGLLEDFD NISVTRSNSL RKESPPTPDQ GASSHGPGHA 

       130        140        150        160        170        180 
EENGFITFSQ YSSESDTTAD YTTEKYREKS LYGDDLDPYY RGSHAAKQNG HVMKMKHGEA 

       190        200        210        220        230        240 
YYSEVKPLKS DFARFSADYH SHLDSLSKPS EYSDLKWEYQ RASSSSPLDY SFQFTPSRTA 

       250        260        270        280        290        300 
GTSGCSKESL AYSESEWGPS LDDYDRRPKS SYLNQTSPQP TMRQRSRSGS GLQEPMMPFG 

       310        320        330        340        350        360 
ASAFKTHPQG HSYNSYTYPR LSEPTMCIPK VDYDRAQMVL SPPLSGSDTY PRGPAKLPQS 

       370        380        390        400        410        420 
QSKSGYSSSS HQYPSGYHKA TLYHHPSLQS SSQYISTASY LSSLSLSSST YPPPSWGSSS 

       430        440        450        460        470        480 
DQQPSRVSHE QFRAALQLVV SPGDPREYLA NFIKIGEGST GIVCIATEKH TGKQVAVKKM 

       490        500        510        520        530        540 
DLRKQQRREL LFNEVVIMRD YHHDNVVDMY SSYLVGDELW VVMEFLEGGA LTDIVTHTRM 

       550        560        570        580        590        600 
NEEQIATVCL SVLRALSYLH NQGVIHRDIK SDSILLTSDG RIKLSDFGFC AQVSKEVPKR 

       610        620        630        640        650        660 
KSLVGTPYWM APEVISRLPY GTEVDIWSLG IMVIEMIDGE PPYFNEPPLQ AMRRIRDSLP 

       670        680        690        700        710 
PRVKDLHKVS SVLRGFLDLM LVREPSQRAT AQELLGHPFL KLAGPPSCIV PLMRQYRHH 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of PAK5, a novel member of mammalian p21-activated kinase-II subfamily that is predominantly expressed in brain."
Pandey A., Dan I., Kristiansen T.Z., Watanabe N.M., Voldby J., Kajikawa E., Khosravi-Far R., Blagoev B., Mann M.
Oncogene 21:3939-3948(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"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. expand/collapse author list , 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], VARIANT ASN-511.
Tissue: Brain.
[4]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Identification of an autoinhibitory domain of p21-activated protein kinase 5."
Ching Y.P., Leong V.Y., Wong C.M., Kung H.F.
J. Biol. Chem. 278:33621-33624(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN, MUTAGENESIS OF 19-HIS--HIS-22.
[7]"p21-Activated kinase 5 (Pak5) localizes to mitochondria and inhibits apoptosis by phosphorylating BAD."
Cotteret S., Jaffer Z.M., Beeser A., Chernoff J.
Mol. Cell. Biol. 23:5526-5539(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"PAK5 kinase is an inhibitor of MARK/Par-1, which leads to stable microtubules and dynamic actin."
Matenia D., Griesshaber B., Li X.Y., Thiessen A., Johne C., Jiao J., Mandelkow E., Mandelkow E.M.
Mol. Biol. Cell 16:4410-4422(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MARK2.
[9]"Multiple Rho proteins regulate the subcellular targeting of PAK5."
Wu X., Frost J.A.
Biochem. Biophys. Res. Commun. 351:328-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RHOD AND RHOH.
[10]"Nucleocytoplasmic shuttling of Pak5 regulates its antiapoptotic properties."
Cotteret S., Chernoff J.
Mol. Cell. Biol. 26:3215-3230(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"p21 activated kinase 5 activates Raf-1 and targets it to mitochondria."
Wu X., Carr H.S., Dan I., Ruvolo P.P., Frost J.A.
J. Cell. Biochem. 105:167-175(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF RAF1.
[12]"p120-catenin is a binding partner and substrate for Group B Pak kinases."
Wong L.E., Reynolds A.B., Dissanayaka N.T., Minden A.
J. Cell. Biochem. 110:1244-1254(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF CTNND1.
[13]"Crystal Structures of the p21-activated kinases PAK4, PAK5, and PAK6 reveal catalytic domain plasticity of active group II PAKs."
Eswaran J., Lee W.H., Debreczeni J.E., Filippakopoulos P., Turnbull A., Fedorov O., Deacon S.W., Peterson J.R., Knapp S.
Structure 15:201-213(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 425-719.
[14]"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. expand/collapse author list , 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-118; ALA-187; PRO-312; PRO-335; ASN-511; ASN-538; SER-555; ILE-604 AND SER-704.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB040812 mRNA. Translation: BAA94194.1.
AB033090 mRNA. Translation: BAA86578.1. Different initiation.
AK291401 mRNA. Translation: BAF84090.1.
AL031652, AL135935, AL353612 Genomic DNA. Translation: CAI42211.1.
AL135935, AL031652, AL353612 Genomic DNA. Translation: CAH71126.1.
AL353612, AL031652, AL135935 Genomic DNA. Translation: CAI23529.1.
CH471133 Genomic DNA. Translation: EAX10358.1.
CH471133 Genomic DNA. Translation: EAX10359.1.
CH471133 Genomic DNA. Translation: EAX10360.1.
CCDSCCDS13107.1.
RefSeqNP_065074.1. NM_020341.3.
NP_817127.1. NM_177990.2.
XP_005260823.1. XM_005260766.2.
XP_006723660.1. XM_006723597.1.
UniGeneHs.32539.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2F57X-ray1.80A/B425-719[»]
ProteinModelPortalQ9P286.
SMRQ9P286. Positions 10-42, 422-718.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121402. 13 interactions.
IntActQ9P286. 2 interactions.
MINTMINT-1443173.
STRING9606.ENSP00000322957.

Chemistry

BindingDBQ9P286.
ChEMBLCHEMBL4524.
GuidetoPHARMACOLOGY2138.

PTM databases

PhosphoSiteQ9P286.

Polymorphism databases

DMDM12585290.

Proteomic databases

PaxDbQ9P286.
PRIDEQ9P286.

Protocols and materials databases

DNASU57144.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000353224; ENSP00000322957; ENSG00000101349.
ENST00000378423; ENSP00000367679; ENSG00000101349.
ENST00000378429; ENSP00000367686; ENSG00000101349.
GeneID57144.
KEGGhsa:57144.
UCSCuc002wnj.2. human.

Organism-specific databases

CTD57144.
GeneCardsGC20M009518.
HGNCHGNC:15916. PAK7.
HPAHPA020444.
MIM608038. gene.
neXtProtNX_Q9P286.
PharmGKBPA32922.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000234205.
HOVERGENHBG108518.
InParanoidQ9P286.
KOK05736.
OMASHAAKQN.
OrthoDBEOG73804D.
PhylomeDBQ9P286.
TreeFamTF105352.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
ReactomeREACT_111045. Developmental Biology.
SignaLinkQ9P286.

Gene expression databases

ArrayExpressQ9P286.
BgeeQ9P286.
CleanExHS_PAK7.
GenevestigatorQ9P286.

Family and domain databases

Gene3D3.90.810.10. 1 hit.
InterProIPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR028754. PAK7.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]
PANTHERPTHR24361:SF183. PTHR24361:SF183. 1 hit.
PfamPF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50108. CRIB. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9P286.
GeneWikiPAK7.
GenomeRNAi57144.
NextBio63091.
PROQ9P286.
SOURCESearch...

Entry information

Entry namePAK7_HUMAN
AccessionPrimary (citable) accession number: Q9P286
Secondary accession number(s): A8K5T6 expand/collapse secondary AC list , D3DW14, Q5W115, Q9BX09, Q9ULF6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM