Q9NWT1 (PK1IP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
p21-activated protein kinase-interacting protein 1

Alternative name(s):
PAK/PLC-interacting protein 1
Short name=hPIP1
PAK1-interacting protein 1
WD repeat-containing protein 84

Gene names

Name:	PAK1IP1
Synonyms:	PIP1, WDR84

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	392 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Negatively regulates the PAK1 kinase. PAK1 is a member of the PAK kinase family, which have been shown to play a positive role in the regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists as an inactive homodimer, which is activated by binding of small GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also binds to the N-terminus of PAK1, and inhibits the specific activation of PAK1 by CDC42. Ref.1
Subunit structure	Interacts with PAK1. Ref.1
Subcellular location	Nucleus › nucleolus Ref.5.
Tissue specificity	Expressed in brain, colon, heart, kidney, liver, lung, muscle, peripheral blood leukocytes, placenta, small intestine, spleen and thymus. Ref.1
Sequence similarities	Contains 5 WD repeats.

Ontologies

Keywords
Cellular component	Nucleus
Domain	Repeat WD repeat
Molecular function	Signal transduction inhibitor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of signal transduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: HPA
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 392	392	p21-activated protein kinase-interacting protein 1		PRO_0000051125
Regions
	Repeat	40 – 77	38	WD 1
	Repeat	80 – 118	39	WD 2
	Repeat	121 – 160	40	WD 3
	Repeat	202 – 240	39	WD 4
	Repeat	243 – 284	42	WD 5
Amino acid modifications
	Modified residue	320	1	Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9
	Modified residue	323	1	Phosphoserine Ref.9
Experimental info
	Sequence conflict	22	1	E → K in BAA91296. Ref.2
	Sequence conflict	124	1	G → R in AAK57477. Ref.1
	Sequence conflict	201	1	I → V in AAH10907. Ref.4
	Sequence conflict	257	1	P → L in AAK57477. Ref.1
	Sequence conflict	273	1	M → R in AAK57477. Ref.1
	Sequence conflict	277	1	K → E in AAH10907. Ref.4
	Sequence conflict	311	1	Missing in BAA91296. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9NWT1 [UniParc]. Last modified July 19, 2005. Version 2. Checksum: 7600CDDFCB4F363A	FASTA	392	43,964
	10 20 30 40 50 60 MELVAGCYEQ VLFGFAVHPE PEACGDHEQW TLVADFTHHA HTASLSAVAV NSRFVVTGSK 70 80 90 100 110 120 DETIHIYDMK KKIEHGALVH HSGTITCLKF YGNRHLISGA EDGLICIWDA KKWECLKSIK 130 140 150 160 170 180 AHKGQVTFLS IHPSGKLALS VGTDKTLRTW NLVEGRSAFI KNIKQNAHIV EWSPRGEQYV 190 200 210 220 230 240 VIIQNKIDIY QLDTASISGT ITNEKRISSV KFLSESVLAV AGDEEVIRFF DCDSLVCLCE 250 260 270 280 290 300 FKAHENRVKD MFSFEIPEHH VIVSASSDGF IKMWKLKQDK KVPPSLLCEI NTNARLTCLG 310 320 330 340 350 360 VWLDKVADMK ESLPPAAEPS PVSKEQSKIG KKEPGDTVHK EEKRSKPNTK KRGLTGDSKK 370 380 390 ATKESGLIST KKRKMVEMLE KKRKKKKIKT MQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Regulation of the p21-activated kinase (PAK) by a human Gbeta -like WD-repeat protein, hPIP1." Xia C., Ma W., Stafford L.J., Marcus S., Xiong W.-C., Liu M. Proc. Natl. Acad. Sci. U.S.A. 98:6174-6179(2001) [PubMed: 11371639] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PAK1, TISSUE SPECIFICITY.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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]. Tissue: Prostate.
[5]	"Functional proteomic analysis of human nucleolus." Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J. Mol. Biol. Cell 13:4100-4109(2002) [PubMed: 12429849] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[6]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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-320, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320 AND SER-323, MASS SPECTROMETRY. Tissue: Embryonic kidney.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF283303 mRNA. Translation: AAK57477.1. AK000631 mRNA. Translation: BAA91296.1. AL358777 Genomic DNA. Translation: CAI14002.1. BC010907 mRNA. Translation: AAH10907.1.
IPI	IPI00549540.
RefSeq	NP_060376.2. NM_017906.2.
UniGene	Hs.310231.
3D structure databases
ProteinModelPortal	Q9NWT1.
SMR	Q9NWT1. Positions 2-308.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9NWT1.
PTM databases
PhosphoSite	Q9NWT1.
Polymorphism databases
DMDM	71153057.
2D gel databases
SWISS-2DPAGE	Q9NWT1.
Proteomic databases
PeptideAtlas	Q9NWT1.
PRIDE	Q9NWT1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000379568; ENSP00000368887; ENSG00000111845.
GeneID	55003.
KEGG	hsa:55003.
UCSC	uc003mzg.1. human.
Organism-specific databases
CTD	55003.
GeneCards	GC06P010694.
H-InvDB	HIX0005573.
HGNC	HGNC:20882. PAK1IP1.
HPA	HPA030112.
MIM	607811. gene.
neXtProt	NX_Q9NWT1.
PharmGKB	PA134928299.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05387.
GeneTree	ENSGT00390000001263.
HOGENOM	HBG403002.
HOVERGEN	HBG082144.
InParanoid	Q9NWT1.
OMA	YDMKKKV.
OrthoDB	EOG45MN5T.
PhylomeDB	Q9NWT1.
Gene expression databases
ArrayExpress	Q9NWT1.
Bgee	Q9NWT1.
CleanEx	HS_PAK1IP1.
Genevestigator	Q9NWT1.
GermOnline	ENSG00000111845. Homo sapiens.
Family and domain databases
InterPro	IPR020472. G-protein_beta_WD-40_rep. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR011046. WD40_repeat-like_dom. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_dom. [Graphical view]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
KO	K14830.
Pfam	PF00400. WD40. 4 hits. [Graphical view]
PRINTS	PR00320. GPROTEINBRPT.
SMART	SM00320. WD40. 5 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 1 hit.
PROSITE	PS00678. WD_REPEATS_1. 2 hits. PS50082. WD_REPEATS_2. 4 hits. PS50294. WD_REPEATS_REGION. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	58332.
SOURCE	Search...

Entry information

Entry name

PK1IP_HUMAN

Accession

Primary (citable) accession number: Q9NWT1
Secondary accession number(s): Q5T4J2, Q96QJ8, Q96T87

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	January 25, 2012
This is version 83 of the entry and version 2 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.