ID PK1IP_HUMAN Reviewed; 392 AA.
AC Q9NWT1; Q5T4J2; Q96QJ8; Q96T87;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 27-MAR-2024, entry version 177.
DE RecName: Full=p21-activated protein kinase-interacting protein 1;
DE AltName: Full=PAK/PLC-interacting protein 1;
DE Short=hPIP1;
DE AltName: Full=PAK1-interacting protein 1;
DE AltName: Full=WD repeat-containing protein 84;
GN Name=PAK1IP1; Synonyms=PIP1, WDR84;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PAK1, AND TISSUE
RP SPECIFICITY.
RX PubMed=11371639; DOI=10.1073/pnas.101137298;
RA Xia C., Ma W., Stafford L.J., Marcus S., Xiong W.-C., Liu M.;
RT "Regulation of the p21-activated kinase (PAK) by a human Gbeta -like WD-
RT repeat protein, hPIP1.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6174-6179(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP FUNCTION.
RX PubMed=24120868; DOI=10.1016/j.celrep.2013.08.049;
RA Sloan K.E., Bohnsack M.T., Watkins N.J.;
RT "The 5S RNP couples p53 homeostasis to ribosome biogenesis and nucleolar
RT stress.";
RL Cell Rep. 5:237-247(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Negatively regulates the PAK1 kinase. PAK1 is a member of the
CC PAK kinase family, which has been shown to play a positive role in the
CC regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists
CC as an inactive homodimer, which is activated by binding of small
CC GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also
CC binds to the N-terminus of PAK1, and inhibits the specific activation
CC of PAK1 by CDC42. May be involved in ribosomal large subunit assembly
CC (PubMed:24120868). {ECO:0000269|PubMed:11371639,
CC ECO:0000269|PubMed:24120868}.
CC -!- SUBUNIT: Interacts with PAK1. {ECO:0000269|PubMed:11371639}.
CC -!- INTERACTION:
CC Q9NWT1; Q6FHY5: MEOX2; NbExp=6; IntAct=EBI-7641942, EBI-16439278;
CC Q9NWT1; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-7641942, EBI-742388;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, colon, heart, kidney, liver,
CC lung, muscle, peripheral blood leukocytes, placenta, small intestine,
CC spleen and thymus. {ECO:0000269|PubMed:11371639}.
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DR EMBL; AF283303; AAK57477.1; -; mRNA.
DR EMBL; AK000631; BAA91296.1; -; mRNA.
DR EMBL; AL358777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010907; AAH10907.1; -; mRNA.
DR CCDS; CCDS34339.1; -.
DR RefSeq; NP_060376.2; NM_017906.2.
DR AlphaFoldDB; Q9NWT1; -.
DR SMR; Q9NWT1; -.
DR BioGRID; 120335; 149.
DR IntAct; Q9NWT1; 32.
DR MINT; Q9NWT1; -.
DR STRING; 9606.ENSP00000368887; -.
DR GlyGen; Q9NWT1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NWT1; -.
DR PhosphoSitePlus; Q9NWT1; -.
DR SwissPalm; Q9NWT1; -.
DR BioMuta; PAK1IP1; -.
DR DMDM; 71153057; -.
DR SWISS-2DPAGE; Q9NWT1; -.
DR EPD; Q9NWT1; -.
DR jPOST; Q9NWT1; -.
DR MassIVE; Q9NWT1; -.
DR MaxQB; Q9NWT1; -.
DR PaxDb; 9606-ENSP00000368887; -.
DR PeptideAtlas; Q9NWT1; -.
DR ProteomicsDB; 82977; -.
DR Pumba; Q9NWT1; -.
DR Antibodypedia; 24813; 100 antibodies from 23 providers.
DR DNASU; 55003; -.
DR Ensembl; ENST00000379568.4; ENSP00000368887.3; ENSG00000111845.5.
DR Ensembl; ENST00000644756.2; ENSP00000496482.1; ENSG00000285226.2.
DR GeneID; 55003; -.
DR KEGG; hsa:55003; -.
DR MANE-Select; ENST00000379568.4; ENSP00000368887.3; NM_017906.3; NP_060376.2.
DR UCSC; uc003mzg.4; human.
DR AGR; HGNC:20882; -.
DR CTD; 55003; -.
DR DisGeNET; 55003; -.
DR GeneCards; PAK1IP1; -.
DR HGNC; HGNC:20882; PAK1IP1.
DR HPA; ENSG00000111845; Low tissue specificity.
DR MIM; 607811; gene.
DR neXtProt; NX_Q9NWT1; -.
DR OpenTargets; ENSG00000111845; -.
DR PharmGKB; PA134928299; -.
DR VEuPathDB; HostDB:ENSG00000111845; -.
DR eggNOG; KOG0294; Eukaryota.
DR GeneTree; ENSGT00390000001263; -.
DR HOGENOM; CLU_031466_2_0_1; -.
DR InParanoid; Q9NWT1; -.
DR OMA; FGYRVKT; -.
DR OrthoDB; 198243at2759; -.
DR PhylomeDB; Q9NWT1; -.
DR TreeFam; TF326684; -.
DR PathwayCommons; Q9NWT1; -.
DR SignaLink; Q9NWT1; -.
DR BioGRID-ORCS; 55003; 787 hits in 1134 CRISPR screens.
DR ChiTaRS; PAK1IP1; human.
DR GeneWiki; PAK1IP1; -.
DR GenomeRNAi; 55003; -.
DR Pharos; Q9NWT1; Tbio.
DR PRO; PR:Q9NWT1; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NWT1; Protein.
DR Bgee; ENSG00000111845; Expressed in prostate gland and 97 other cell types or tissues.
DR ExpressionAtlas; Q9NWT1; baseline and differential.
DR Genevisible; Q9NWT1; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:UniProtKB.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR44675:SF1; P21-ACTIVATED PROTEIN KINASE-INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR44675; PAK1 INTERACTING PROTEIN 1; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribosome biogenesis;
KW Signal transduction inhibitor; WD repeat.
FT CHAIN 1..392
FT /note="p21-activated protein kinase-interacting protein 1"
FT /id="PRO_0000051125"
FT REPEAT 33..72
FT /note="WD 1"
FT REPEAT 73..113
FT /note="WD 2"
FT REPEAT 114..155
FT /note="WD 3"
FT REPEAT 156..195
FT /note="WD 4"
FT REPEAT 196..235
FT /note="WD 5"
FT REPEAT 236..275
FT /note="WD 6"
FT REGION 312..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..392
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CONFLICT 22
FT /note="E -> K (in Ref. 2; BAA91296)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="G -> R (in Ref. 1; AAK57477)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="I -> V (in Ref. 4; AAH10907)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="P -> L (in Ref. 1; AAK57477)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="M -> R (in Ref. 1; AAK57477)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="K -> E (in Ref. 4; AAH10907)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="Missing (in Ref. 2; BAA91296)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 43964 MW; 7600CDDFCB4F363A CRC64;
MELVAGCYEQ VLFGFAVHPE PEACGDHEQW TLVADFTHHA HTASLSAVAV NSRFVVTGSK
DETIHIYDMK KKIEHGALVH HSGTITCLKF YGNRHLISGA EDGLICIWDA KKWECLKSIK
AHKGQVTFLS IHPSGKLALS VGTDKTLRTW NLVEGRSAFI KNIKQNAHIV EWSPRGEQYV
VIIQNKIDIY QLDTASISGT ITNEKRISSV KFLSESVLAV AGDEEVIRFF DCDSLVCLCE
FKAHENRVKD MFSFEIPEHH VIVSASSDGF IKMWKLKQDK KVPPSLLCEI NTNARLTCLG
VWLDKVADMK ESLPPAAEPS PVSKEQSKIG KKEPGDTVHK EEKRSKPNTK KRGLTGDSKK
ATKESGLIST KKRKMVEMLE KKRKKKKIKT MQ
//
