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Protein

p21-activated protein kinase-interacting protein 1

Gene

PAK1IP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 CDC42.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Enzyme and pathway databases

SignaLinkiQ9NWT1.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PAK1IP1
Synonyms:PIP1, WDR84
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:20882. PAK1IP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134928299.

Polymorphism and mutation databases

BioMutaiPAK1IP1.
DMDMi71153057.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 392392p21-activated protein kinase-interacting protein 1PRO_0000051125Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei320 – 3201PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NWT1.
MaxQBiQ9NWT1.
PaxDbiQ9NWT1.
PeptideAtlasiQ9NWT1.
PRIDEiQ9NWT1.

2D gel databases

SWISS-2DPAGEQ9NWT1.

PTM databases

iPTMnetiQ9NWT1.
PhosphoSiteiQ9NWT1.

Expressioni

Tissue specificityi

Expressed in brain, colon, heart, kidney, liver, lung, muscle, peripheral blood leukocytes, placenta, small intestine, spleen and thymus.1 Publication

Gene expression databases

BgeeiQ9NWT1.
CleanExiHS_PAK1IP1.
GenevisibleiQ9NWT1. HS.

Organism-specific databases

HPAiHPA030112.

Interactioni

Subunit structurei

Interacts with PAK1.1 Publication

Protein-protein interaction databases

BioGridi120335. 29 interactions.
IntActiQ9NWT1. 5 interactions.
MINTiMINT-3057412.
STRINGi9606.ENSP00000368887.

Structurei

3D structure databases

ProteinModelPortaliQ9NWT1.
SMRiQ9NWT1. Positions 2-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati33 – 7240WD 1Add
BLAST
Repeati73 – 11341WD 2Add
BLAST
Repeati114 – 15542WD 3Add
BLAST
Repeati156 – 19540WD 4Add
BLAST
Repeati196 – 23540WD 5Add
BLAST
Repeati236 – 27540WD 6Add
BLAST

Sequence similaritiesi

Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0294. Eukaryota.
ENOG410XRDQ. LUCA.
GeneTreeiENSGT00390000001263.
HOGENOMiHOG000007618.
HOVERGENiHBG082144.
InParanoidiQ9NWT1.
KOiK14830.
OMAiSEFKAHE.
OrthoDBiEOG7P2XSW.
PhylomeDBiQ9NWT1.
TreeFamiTF326684.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 3 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NWT1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELVAGCYEQ VLFGFAVHPE PEACGDHEQW TLVADFTHHA HTASLSAVAV
60 70 80 90 100
NSRFVVTGSK DETIHIYDMK KKIEHGALVH HSGTITCLKF YGNRHLISGA
110 120 130 140 150
EDGLICIWDA KKWECLKSIK AHKGQVTFLS IHPSGKLALS VGTDKTLRTW
160 170 180 190 200
NLVEGRSAFI KNIKQNAHIV EWSPRGEQYV VIIQNKIDIY QLDTASISGT
210 220 230 240 250
ITNEKRISSV KFLSESVLAV AGDEEVIRFF DCDSLVCLCE FKAHENRVKD
260 270 280 290 300
MFSFEIPEHH VIVSASSDGF IKMWKLKQDK KVPPSLLCEI NTNARLTCLG
310 320 330 340 350
VWLDKVADMK ESLPPAAEPS PVSKEQSKIG KKEPGDTVHK EEKRSKPNTK
360 370 380 390
KRGLTGDSKK ATKESGLIST KKRKMVEMLE KKRKKKKIKT MQ
Length:392
Mass (Da):43,964
Last modified:July 19, 2005 - v2
Checksum:i7600CDDFCB4F363A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221E → K in BAA91296 (PubMed:14702039).Curated
Sequence conflicti124 – 1241G → R in AAK57477 (PubMed:11371639).Curated
Sequence conflicti201 – 2011I → V in AAH10907 (PubMed:15489334).Curated
Sequence conflicti257 – 2571P → L in AAK57477 (PubMed:11371639).Curated
Sequence conflicti273 – 2731M → R in AAK57477 (PubMed:11371639).Curated
Sequence conflicti277 – 2771K → E in AAH10907 (PubMed:15489334).Curated
Sequence conflicti311 – 3111Missing in BAA91296 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF283303 mRNA. Translation: AAK57477.1.
AK000631 mRNA. Translation: BAA91296.1.
AL358777 Genomic DNA. Translation: CAI14002.1.
BC010907 mRNA. Translation: AAH10907.1.
CCDSiCCDS34339.1.
RefSeqiNP_060376.2. NM_017906.2.
UniGeneiHs.310231.

Genome annotation databases

EnsembliENST00000379568; ENSP00000368887; ENSG00000111845.
GeneIDi55003.
KEGGihsa:55003.
UCSCiuc003mzg.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF283303 mRNA. Translation: AAK57477.1.
AK000631 mRNA. Translation: BAA91296.1.
AL358777 Genomic DNA. Translation: CAI14002.1.
BC010907 mRNA. Translation: AAH10907.1.
CCDSiCCDS34339.1.
RefSeqiNP_060376.2. NM_017906.2.
UniGeneiHs.310231.

3D structure databases

ProteinModelPortaliQ9NWT1.
SMRiQ9NWT1. Positions 2-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120335. 29 interactions.
IntActiQ9NWT1. 5 interactions.
MINTiMINT-3057412.
STRINGi9606.ENSP00000368887.

PTM databases

iPTMnetiQ9NWT1.
PhosphoSiteiQ9NWT1.

Polymorphism and mutation databases

BioMutaiPAK1IP1.
DMDMi71153057.

2D gel databases

SWISS-2DPAGEQ9NWT1.

Proteomic databases

EPDiQ9NWT1.
MaxQBiQ9NWT1.
PaxDbiQ9NWT1.
PeptideAtlasiQ9NWT1.
PRIDEiQ9NWT1.

Protocols and materials databases

DNASUi55003.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379568; ENSP00000368887; ENSG00000111845.
GeneIDi55003.
KEGGihsa:55003.
UCSCiuc003mzg.4. human.

Organism-specific databases

CTDi55003.
GeneCardsiPAK1IP1.
H-InvDBHIX0005573.
HGNCiHGNC:20882. PAK1IP1.
HPAiHPA030112.
MIMi607811. gene.
neXtProtiNX_Q9NWT1.
PharmGKBiPA134928299.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0294. Eukaryota.
ENOG410XRDQ. LUCA.
GeneTreeiENSGT00390000001263.
HOGENOMiHOG000007618.
HOVERGENiHBG082144.
InParanoidiQ9NWT1.
KOiK14830.
OMAiSEFKAHE.
OrthoDBiEOG7P2XSW.
PhylomeDBiQ9NWT1.
TreeFamiTF326684.

Enzyme and pathway databases

SignaLinkiQ9NWT1.

Miscellaneous databases

ChiTaRSiPAK1IP1. human.
GeneWikiiPAK1IP1.
GenomeRNAii55003.
PROiQ9NWT1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NWT1.
CleanExiHS_PAK1IP1.
GenevisibleiQ9NWT1. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 3 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.

Entry informationi

Entry nameiPK1IP_HUMAN
AccessioniPrimary (citable) accession number: Q9NWT1
Secondary accession number(s): Q5T4J2, Q96QJ8, Q96T87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: July 6, 2016
This is version 125 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.