PK1IP_MOUSE
ID PK1IP_MOUSE Reviewed; 382 AA.
AC Q9DCE5; Q3UBK7; Q80UT4; Q8C5N6; Q923K2; Q9D3E9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=p21-activated protein kinase-interacting protein 1;
DE AltName: Full=PAK1-interacting protein 1;
DE AltName: Full=Putative PAK inhibitor Skb15;
GN Name=Pak1ip1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11389855; DOI=10.1016/s1097-2765(01)00248-9;
RA Kim H.W., Yang P., Qyang Y., Lai H., Du H., Henkel J.S., Kumar K., Bao S.,
RA Liu M., Marcus S.;
RT "Genetic and molecular characterization of Skb15, a highly conserved
RT inhibitor of the fission yeast PAK, Shk1.";
RL Mol. Cell 7:1095-1101(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu M., Xia C.;
RT "Mouse homolog of human p21-activated protein kinase-interacting protein 1
RT (hPIP1).";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Kidney, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-382.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 {ECO:0000250|UniProtKB:Q9NWT1}.
CC -!- SUBUNIT: Interacts with PAK1. {ECO:0000250|UniProtKB:Q9NWT1}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9NWT1}.
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DR EMBL; AY030406; AAK51599.1; -; mRNA.
DR EMBL; AF386076; AAL40652.1; -; mRNA.
DR EMBL; AK002852; BAB22407.1; -; mRNA.
DR EMBL; AK077941; BAC37076.1; -; mRNA.
DR EMBL; AK150747; BAE29818.1; -; mRNA.
DR EMBL; AK150919; BAE29957.1; -; mRNA.
DR EMBL; BC051498; AAH51498.1; -; mRNA.
DR CCDS; CCDS36638.1; -.
DR RefSeq; NP_080826.2; NM_026550.3.
DR AlphaFoldDB; Q9DCE5; -.
DR SMR; Q9DCE5; -.
DR BioGRID; 212647; 7.
DR STRING; 10090.ENSMUSP00000040846; -.
DR iPTMnet; Q9DCE5; -.
DR PhosphoSitePlus; Q9DCE5; -.
DR EPD; Q9DCE5; -.
DR jPOST; Q9DCE5; -.
DR MaxQB; Q9DCE5; -.
DR PaxDb; Q9DCE5; -.
DR PRIDE; Q9DCE5; -.
DR ProteomicsDB; 289588; -.
DR Antibodypedia; 24813; 89 antibodies from 23 providers.
DR DNASU; 68083; -.
DR Ensembl; ENSMUST00000046951; ENSMUSP00000040846; ENSMUSG00000038683.
DR GeneID; 68083; -.
DR KEGG; mmu:68083; -.
DR UCSC; uc007qer.2; mouse.
DR CTD; 55003; -.
DR MGI; MGI:1915333; Pak1ip1.
DR VEuPathDB; HostDB:ENSMUSG00000038683; -.
DR eggNOG; KOG0294; Eukaryota.
DR GeneTree; ENSGT00390000001263; -.
DR HOGENOM; CLU_031466_2_0_1; -.
DR InParanoid; Q9DCE5; -.
DR OMA; FGYRVKT; -.
DR OrthoDB; 824688at2759; -.
DR PhylomeDB; Q9DCE5; -.
DR TreeFam; TF326684; -.
DR BioGRID-ORCS; 68083; 30 hits in 80 CRISPR screens.
DR ChiTaRS; Pak1ip1; mouse.
DR PRO; PR:Q9DCE5; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9DCE5; protein.
DR Bgee; ENSMUSG00000038683; Expressed in placenta labyrinth and 259 other tissues.
DR Genevisible; Q9DCE5; MM.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0008283; P:cell population proliferation; IPI:MGI.
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; ISS:UniProtKB.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISS:UniProtKB.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Repeat; Ribosome biogenesis;
KW Signal transduction inhibitor; WD repeat.
FT CHAIN 1..382
FT /note="p21-activated protein kinase-interacting protein 1"
FT /id="PRO_0000051126"
FT REPEAT 37..77
FT /note="WD 1"
FT REPEAT 80..120
FT /note="WD 2"
FT REPEAT 122..160
FT /note="WD 3"
FT REPEAT 202..240
FT /note="WD 4"
FT REPEAT 243..284
FT /note="WD 5"
FT REGION 313..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 176
FT /note="G -> R (in Ref. 1; AAK51599)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="M -> MSLTWQIPDFSSLSECPFDGILHVPVRRKYLLP (in Ref. 2
FT and 3; BAB22407)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 42116 MW; 7EA5788A4B7EF2D1 CRC64;
MELVAGSYEQ VLFGFTVQRG PAKSGHQETW TPVADFTHHS HTASLSVLAS NSRYVVSGSK
DETIHIYDMK RKVEHGALVH HAGTVTCLKF HGNQHLISGA EDGHICIWDV KRWKCLKTFK
AHRGHVTFLS IHPSGKLALS VGTDKTLRTW NLIEGRSAFI KNIKENAHIV EWSPSGGKYI
VVVQNKVDVY RLGTASVSGT ITNGKRISSV TFLSDSVLAV AGDEEVVRIF DCDSLECLCE
FRAHENRVKD MVSFEVPDHH VLVTASNDGF IKMWTLPQDK KVPPSLLCEA KTGARLTCLT
VWLDRAANGM ASLPPAAEPC PDQPKTIEKE SGDTVQEETS EPNSEKSDVS GDSKQPTKGN
SPVTAKKRKM ATMSEKKRKK KM
