Q9P286 (PAK7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	719 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Apoptosis
Cellular component	Cytoplasm Mitochondrion Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic 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 apoptotic process Inferred from electronic annotation. Source: Compara signal transduction Traceable author statement PubMed 20070256. Source: UniProtKB
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 719

719

Serine/threonine-protein kinase PAK 7

PRO_0000086477

Regions

Domain

11 – 24

14

CRIB

Domain

449 – 700

252

Protein kinase

Nucleotide binding

455 – 463

9

ATP By similarity

Region

25 – 448

424

Linker

Compositional bias

4 – 8

5

Poly-Lys

Compositional bias

223 – 226

4

Poly-Ser

Compositional bias

367 – 370

4

Poly-Ser

Sites

Active site

568

1

Proton acceptor By similarity

Binding site

478

1

ATP By similarity

Amino acid modifications

Modified residue

104

1

Phosphoserine By similarity

Modified residue

107

1

Phosphothreonine By similarity

Natural variations

Natural variant

118

1

G → D. Ref.14
Corresponds to variant rs55923311 [ dbSNP | Ensembl ].

VAR_040978

Natural variant

187

1

P → A. Ref.14
Corresponds to variant rs34280805 [ dbSNP | Ensembl ].

VAR_040979

Natural variant

312

1

S → P in a colorectal adenocarcinoma sample; somatic mutation. Ref.14

VAR_040980

Natural variant

335

1

R → P. Ref.14
Corresponds to variant rs11700112 [ dbSNP | Ensembl ].

VAR_040981

Natural variant

511

1

S → N. Ref.3 Ref.14
Corresponds to variant rs2297345 [ dbSNP | Ensembl ].

VAR_021865

Natural variant

538

1

T → N in a lung adenocarcinoma sample; somatic mutation. Ref.14

VAR_040982

Natural variant

555

1

A → S. Ref.14
Corresponds to variant rs34102290 [ dbSNP | Ensembl ].

VAR_040983

Natural variant

604

1

V → I in a metastatic melanoma sample; somatic mutation. Ref.14

VAR_040984

Natural variant

704

1

G → S in a metastatic melanoma sample; somatic mutation. Ref.14

VAR_040985

Experimental info

Mutagenesis

19 – 22

4

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

Secondary structure

1

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719

Helix Strand Turn

Details...

Helix

429 – 437

9

Helix

445 – 447

3

Beta strand

449 – 457

9

Beta strand

459 – 468

10

Turn

469 – 471

3

Beta strand

474 – 481

8

Helix

482 – 484

3

Helix

488 – 500

13

Beta strand

509 – 515

7

Beta strand

518 – 524

7

Helix

531 – 535

5

Helix

542 – 561

20

Helix

571 – 573

3

Beta strand

574 – 576

3

Beta strand

582 – 584

3

Beta strand

595 – 597

3

Helix

607 – 609

3

Helix

612 – 615

4

Helix

623 – 638

16

Turn

642 – 645

4

Helix

648 – 657

10

Helix

666 – 668

3

Helix

671 – 680

10

Helix

685 – 687

3

Helix

691 – 695

5

Helix

698 – 702

5

Helix

706 – 708

3

Helix

710 – 712

3

Sequences

	Sequence		Length	Mass (Da)
	Q9P286 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 07A12B1EEC4E2A02	FASTA	719	80,745
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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.

IPI

IPI00001814.

RefSeq

NP_065074.1. NM_020341.3.
NP_817127.1. NM_177990.2.

UniGene

Hs.32539.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2F57	X-ray	1.80	A/B	425-719	[»]

ProteinModelPortal

Q9P286.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9P286. 2 interactions.

MINT

MINT-1443173.

STRING

9606.ENSP00000322957.

PTM databases

PhosphoSite

Q9P286.

Polymorphism databases

DMDM

12585290.

Proteomic databases

PaxDb

Q9P286.

PRIDE

Q9P286.

Protocols and materials databases

DNASU

57144.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000353224; ENSP00000322957; ENSG00000101349.
ENST00000378423; ENSP00000367679; ENSG00000101349.
ENST00000378429; ENSP00000367686; ENSG00000101349.

GeneID

57144.

KEGG

hsa:57144.

UCSC

uc002wnj.2. human.

Organism-specific databases

CTD

57144.

GeneCards

GC20M009518.

HGNC

HGNC:15916. PAK7.

HPA

HPA020444.

MIM

608038. gene.

neXtProt

NX_Q9P286.

PharmGKB

PA32922.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000234205.

HOVERGEN

HBG108518.

InParanoid

Q9P286.

KO

K05736.

OMA

ESLAYSE.

OrthoDB

EOG4RNB7X.

PhylomeDB

Q9P286.

Enzyme and pathway databases

BRENDA

2.7.11.1. 2681.

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

ArrayExpress

Q9P286.

Bgee

Q9P286.

CleanEx

HS_PAK7.

Genevestigator

Q9P286.

GermOnline

ENSG00000101349. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000095. PAK_box_Rho-bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]

Pfam

PF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS50108. CRIB. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9P286.

ChEMBL

CHEMBL4524.

EvolutionaryTrace

Q9P286.

GenomeRNAi

57144.

NextBio

63091.

SOURCE

Search...

Entry information

Entry name

PAK7_HUMAN

Accession

Primary (citable) accession number: Q9P286
Secondary accession number(s): A8K5T6 , D3DW14, Q5W115, Q9BX09, Q9ULF6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 132 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.