Reviewed, UniProtKB/Swiss-Prot O96013 (PAK4_HUMAN)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase PAK 4
    EC=2.7.11.1
Alternative name(s):
    p21-activated kinase 4
      Short name=PAK-4

Gene names

Name:	PAK4
Synonyms:	KIAA1142

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	591 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Activates the JNK pathway. Plays a role in the reorganization of the actin cytoskeleton and in the formation of filopodia. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates ARHGEF2. Ref.7
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with FGFR2 and GRB2 By similarity. Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and weakly with RAC1. Interacts with its substrate ARHGEF2.
Tissue specificity	Highest expression in prostate, testis and colon.
Post-translational modification	Autophosphorylated on serine residues when activated by CDC42/p21. Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Phosphorylated on tyrosine residues upon stimulation of FGFR2 By similarity.
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.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell motion Ref.1 Traceable author statement. Source: ProtInc protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro signal transduction Ref.1 Traceable author statement. Source: ProtInc
Cellular component	Golgi apparatus Ref.1 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC42	P60953	1	EBI-713738,EBI-81752
LRRK1	Q38SD2	1	EBI-713738,EBI-1050422
YWHAG	P61981	1	EBI-713738,EBI-359832
YWHAQ	P27348	1	EBI-713738,EBI-359854
YWHAZ	P63104	1	EBI-713738,EBI-347088

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O96013-1)

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.

Isoform 2 (identifier: O96013-2)

The sequence of this isoform differs from the canonical sequence as follows:
     120-120: E → K
     121-285: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: O96013-3)

The sequence of this isoform differs from the canonical sequence as follows:
     69-221: Missing.

Isoform 4 (identifier: O96013-4)

The sequence of this isoform differs from the canonical sequence as follows:
     132-221: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 591

591

Serine/threonine-protein kinase PAK 4

PRO_0000086474

Regions

Domain

11 – 24

14

CRIB

Domain

321 – 572

252

Protein kinase

Nucleotide binding

327 – 335

9

ATP By similarity

Region

25 – 320

296

Linker

Region

298 – 323

26

GEF-interaction domain (GID)

Sites

Active site

440

1

Proton acceptor By similarity

Binding site

350

1

ATP By similarity

Amino acid modifications

Modified residue

41

1

Phosphoserine Ref.11

Modified residue

99

1

Phosphoserine Ref.10

Modified residue

104

1

Phosphoserine Ref.10 Ref.11

Modified residue

148

1

Phosphoserine Ref.10 Ref.11

Modified residue

167

1

Phosphoserine Ref.10 Ref.11

Modified residue

181

1

Phosphoserine Ref.10 Ref.11 Ref.12

Modified residue

187

1

Phosphothreonine Ref.11

Modified residue

207

1

Phosphothreonine Ref.10 Ref.11

Modified residue

258

1

Phosphoserine Ref.11

Modified residue

267

1

Phosphoserine Ref.10 Ref.11

Modified residue

277

1

Phosphothreonine Ref.11

Modified residue

291

1

Phosphoserine Ref.10 Ref.11

Modified residue

474

1

Phosphoserine; by autocatalysis Ref.9 Ref.10 Ref.11 Ref.12 Ref.14

Natural variations

Alternative sequence

69 – 221

153

Missing in isoform 3.

VSP_017572

Alternative sequence

120

1

E → K in isoform 2.

VSP_004892

Alternative sequence

121 – 285

165

Missing in isoform 2.

VSP_004893

Alternative sequence

132 – 221

90

Missing in isoform 4.

VSP_017573

Natural variant

135

1

R → Q Ref.15

VAR_040970

Natural variant

139

1

A → T Ref.15

VAR_040971

Secondary structure

1

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591

Helix Strand Turn

Details...

Beta strand

15 – 26

12

Turn

27 – 30

4

Beta strand

31 – 34

4

Helix

37 – 39

3

Turn

40 – 42

3

Helix

306 – 309

4

Turn

318 – 320

3

Helix

364 – 371

8

Beta strand

381 – 389

9

Beta strand

391 – 395

5

Helix

404 – 407

4

Helix

414 – 433

20

Helix

443 – 445

3

Beta strand

446 – 448

3

Beta strand

454 – 456

3

Helix

479 – 481

3

Helix

484 – 487

4

Helix

495 – 509

15

Turn

514 – 517

4

Helix

520 – 528

9

Helix

543 – 552

10

Helix

557 – 559

3

Helix

563 – 566

4

Helix

570 – 574

5

Helix

578 – 585

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 04C2A5C0B06427D5	FASTA	591	64,072
	10 20 30 40 50 60 MFGKRKKRVE ISAPSNFEHR VHTGFDQHEQ KFTGLPRQWQ SLIEESARRP KPLVDPACIT 70 80 90 100 110 120 SIQPGAPKTI VRGSKGAKDG ALTLLLDEFE NMSVTRSNSL RRDSPPPPAR ARQENGMPEE 130 140 150 160 170 180 PATTARGGPG KAGSRGRFAG HSEAGGGSGD RRRAGPEKRP KSSREGSGGP QESSRDKRPL 190 200 210 220 230 240 SGPDVGTPQP AGLASGAKLA AGRPFNTYPR ADTDHPSRGA QGEPHDVAPN GPSAGGLAIP 250 260 270 280 290 300 QSSSSSSRPP TRARGAPSPG VLGPHASEPQ LAPPACTPAA PAVPGPPGPR SPQREPQRVS 310 320 330 340 350 360 HEQFRAALQL VVDPGDPRSY LDNFIKIGEG STGIVCIATV RSSGKLVAVK KMDLRKQQRR 370 380 390 400 410 420 ELLFNEVVIM RDYQHENVVE MYNSYLVGDE LWVVMEFLEG GALTDIVTHT RMNEEQIAAV 430 440 450 460 470 480 CLAVLQALSV LHAQGVIHRD IKSDSILLTH DGRVKLSDFG FCAQVSKEVP RRKSLVGTPY 490 500 510 520 530 540 WMAPELISRL PYGPEVDIWS LGIMVIEMVD GEPPYFNEPP LKAMKMIRDN LPPRLKNLHK 550 560 570 580 590 VSPSLKGFLD RLLVRDPAQR ATAAELLKHP FLAKAGPPAS IVPLMRQNRT R
	Isoform 2. Checksum: 505879690593E93A	FASTA	426	47,924
	10 20 30 40 50 60 MFGKRKKRVE ISAPSNFEHR VHTGFDQHEQ KFTGLPRQWQ SLIEESARRP KPLVDPACIT 70 80 90 100 110 120 SIQPGAPKTI VRGSKGAKDG ALTLLLDEFE NMSVTRSNSL RRDSPPPPAR ARQENGMPEK 130 140 150 160 170 180 PPGPRSPQRE PQRVSHEQFR AALQLVVDPG DPRSYLDNFI KIGEGSTGIV CIATVRSSGK 190 200 210 220 230 240 LVAVKKMDLR KQQRRELLFN EVVIMRDYQH ENVVEMYNSY LVGDELWVVM EFLEGGALTD 250 260 270 280 290 300 IVTHTRMNEE QIAAVCLAVL QALSVLHAQG VIHRDIKSDS ILLTHDGRVK LSDFGFCAQV 310 320 330 340 350 360 SKEVPRRKSL VGTPYWMAPE LISRLPYGPE VDIWSLGIMV IEMVDGEPPY FNEPPLKAMK 370 380 390 400 410 420 MIRDNLPPRL KNLHKVSPSL KGFLDRLLVR DPAQRATAAE LLKHPFLAKA GPPASIVPLM RQNRTR
	Isoform 3. Checksum: 4A596EBBCECE9883	FASTA	438	48,268
	10 20 30 40 50 60 MFGKRKKRVE ISAPSNFEHR VHTGFDQHEQ KFTGLPRQWQ SLIEESARRP KPLVDPACIT 70 80 90 100 110 120 SIQPGAPKGE PHDVAPNGPS AGGLAIPQSS SSSSRPPTRA RGAPSPGVLG PHASEPQLAP 130 140 150 160 170 180 PACTPAAPAV PGPPGPRSPQ REPQRVSHEQ FRAALQLVVD PGDPRSYLDN FIKIGEGSTG 190 200 210 220 230 240 IVCIATVRSS GKLVAVKKMD LRKQQRRELL FNEVVIMRDY QHENVVEMYN SYLVGDELWV 250 260 270 280 290 300 VMEFLEGGAL TDIVTHTRMN EEQIAAVCLA VLQALSVLHA QGVIHRDIKS DSILLTHDGR 310 320 330 340 350 360 VKLSDFGFCA QVSKEVPRRK SLVGTPYWMA PELISRLPYG PEVDIWSLGI MVIEMVDGEP 370 380 390 400 410 420 PYFNEPPLKA MKMIRDNLPP RLKNLHKVSP SLKGFLDRLL VRDPAQRATA AELLKHPFLA 430 KAGPPASIVP LMRQNRTR
	Isoform 4. Checksum: 6EE6240ECE65E79D	FASTA	501	54,940
	10 20 30 40 50 60 MFGKRKKRVE ISAPSNFEHR VHTGFDQHEQ KFTGLPRQWQ SLIEESARRP KPLVDPACIT 70 80 90 100 110 120 SIQPGAPKTI VRGSKGAKDG ALTLLLDEFE NMSVTRSNSL RRDSPPPPAR ARQENGMPEE 130 140 150 160 170 180 PATTARGGPG KGEPHDVAPN GPSAGGLAIP QSSSSSSRPP TRARGAPSPG VLGPHASEPQ 190 200 210 220 230 240 LAPPACTPAA PAVPGPPGPR SPQREPQRVS HEQFRAALQL VVDPGDPRSY LDNFIKIGEG 250 260 270 280 290 300 STGIVCIATV RSSGKLVAVK KMDLRKQQRR ELLFNEVVIM RDYQHENVVE MYNSYLVGDE 310 320 330 340 350 360 LWVVMEFLEG GALTDIVTHT RMNEEQIAAV CLAVLQALSV LHAQGVIHRD IKSDSILLTH 370 380 390 400 410 420 DGRVKLSDFG FCAQVSKEVP RRKSLVGTPY WMAPELISRL PYGPEVDIWS LGIMVIEMVD 430 440 450 460 470 480 GEPPYFNEPP LKAMKMIRDN LPPRLKNLHK VSPSLKGFLD RLLVRDPAQR ATAAELLKHP 490 500 FLAKAGPPAS IVPLMRQNRT R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia." Abo A., Qu J., Cammarano M.S., Dan C., Fritsch A., Baud V., Belisle B., Minden A. EMBO J. 17:6527-6540(1998) [PubMed: 9822598] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Lymphoma.
[2]	Melnick M.B. Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Neuroblastoma.
[3]	"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain." Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O. DNA Res. 6:329-336(1999) [PubMed: 10574461] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Brain.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Brain.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4). Tissue: Eye, Pancreas and Placenta.
[6]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 264-591 (ISOFORM 1). Tissue: Teratocarcinoma.
[7]	"Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin." Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B., Sampath R., Bamburg J.R., Bernard O. EMBO J. 24:473-486(2005) [PubMed: 15660133] [Abstract] Cited for: FUNCTION.
[8]	"PAK4 mediates morphological changes through the regulation of GEF-H1." Callow M.G., Zozulya S., Gishizky M.L., Jallal B., Smeal T. J. Cell Sci. 118:1861-1872(2005) [PubMed: 15827085] [Abstract] Cited for: INTERACTION WITH ARHGEF2.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-104; SER-148; SER-167; SER-181; THR-207; SER-267; SER-291 AND SER-474, MASS SPECTROMETRY.
[11]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-104; SER-148; SER-167; SER-181; THR-187; THR-207; SER-258; SER-267; THR-277; SER-291 AND SER-474, MASS SPECTROMETRY.
[12]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-474, MASS SPECTROMETRY.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"Crystal structure of the human p21-activated kinase 4." Eswaran J., Debreczeni J.E., Bunkoczi G., Filippakopoulos P., Das S., Fedorov O., Sundstrom M., Arrowsmith C., Edwards A., von Delft F., Knapp S. Submitted (JUL-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 300-591, PHOSPHORYLATION AT SER-474.
[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: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-135 AND THR-139.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AJ011855 mRNA. Translation: CAA09820.1.
AF005046 mRNA. Translation: AAD01210.1.
AB032968 mRNA. Translation: BAA86456.1. Different initiation.
AL834236 mRNA. Translation: CAD38914.2.
BC002921 mRNA. Translation: AAH02921.1.
BC011368 mRNA. Translation: AAH11368.1.
BC025282 mRNA. Translation: AAH25282.1.
BC034511 mRNA. Translation: AAH34511.1.
AK074728 mRNA. Translation: BAC11166.1. Different initiation.

IPI

IPI00014068.
IPI00178714.
IPI00384231.
IPI00556065.

RefSeq

NP_001014831.1.
NP_001014832.1.
NP_001014834.1.
NP_001014835.1.
NP_005875.1.

UniGene

Hs.20447

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BVA	X-ray	2.30	A/B	300-591	[»]
2CDZ	X-ray	2.30	A	291-591	[»]
2J0I	X-ray	1.60	A	291-591	[»]
2OV2	X-ray	2.10	I/J/K/L/M/N/O/P	10-44	[»]
2Q0N	X-ray	1.75	A	291-591	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O96013. 13 interactions.

PTM databases

PhosphoSite

O96013.

Proteomic databases

PRIDE

O96013.

Genome annotation databases

Ensembl

ENSG00000130669. Homo sapiens. [Contig view]

GeneID

10298.

KEGG

hsa:10298.

UCSC

uc002okj.1. human.
uc002okm.1. human.
uc002okp.1. human.

Organism-specific databases

GeneCards

GC19P044274.

H-InvDB

HIX0015110.

HGNC

HGNC:16059. PAK4.

MIM

605451. gene.

PharmGKB

PA32920.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O96013.

HOVERGEN

O96013.

OMA

O96013. ARQENGM.

Enzyme and pathway databases

BRENDA

2.7.11.1. 247.

Pathway_Interaction_DB

fgf_pathway. FGF signaling pathway.

Gene expression databases

ArrayExpress

O96013.

Bgee

O96013.

CleanEx

HS_PAK4.

GermOnline

ENSG00000130669. Homo sapiens.

Family and domain databases

InterPro

IPR000095. PAK_box_Rho_bd.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR015750. Ser/Thr_Kinase_Pak-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]

PANTHER

PTHR22986:SF84. Pak_like. 1 hit.

Pfam

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

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

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

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 Resources

NextBio

39028.

SOURCE

Search...

Entry information

Entry name

PAK4_HUMAN

Accession

Primary (citable) accession number: O96013
Secondary accession number(s): Q8N4E1 , Q8NCH5, Q8NDE3, Q9BU33, Q9ULS8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	May 1, 1999
Last modified:	July 7, 2009
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)