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Protein

p21-activated protein kinase-interacting protein 1

Gene

Pak1ip1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

GO - Biological processi

  • cell proliferation Source: MGI
  • negative regulation of signal transduction Source: UniProtKB-KW
  • palate development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Names & Taxonomyi

Protein namesi
Recommended name:
p21-activated protein kinase-interacting protein 1
Alternative name(s):
PAK1-interacting protein 1
Putative PAK inhibitor Skb15
Gene namesi
Name:Pak1ip1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1915333. Pak1ip1.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: MGI
  • nucleoplasm Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382p21-activated protein kinase-interacting protein 1PRO_0000051126Add
BLAST

Proteomic databases

EPDiQ9DCE5.
MaxQBiQ9DCE5.
PaxDbiQ9DCE5.
PRIDEiQ9DCE5.

PTM databases

iPTMnetiQ9DCE5.
PhosphoSiteiQ9DCE5.

Expressioni

Gene expression databases

BgeeiQ9DCE5.
CleanExiMM_PAK1IP1.
GenevisibleiQ9DCE5. MM.

Interactioni

Subunit structurei

Interacts with PAK1.By similarity

Protein-protein interaction databases

BioGridi212647. 1 interaction.
STRINGi10090.ENSMUSP00000040846.

Structurei

3D structure databases

ProteinModelPortaliQ9DCE5.
SMRiQ9DCE5. Positions 15-308.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati37 – 7741WD 1Add
BLAST
Repeati80 – 12041WD 2Add
BLAST
Repeati122 – 16039WD 3Add
BLAST
Repeati202 – 24039WD 4Add
BLAST
Repeati243 – 28442WD 5Add
BLAST

Sequence similaritiesi

Contains 5 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0294. Eukaryota.
ENOG410XRDQ. LUCA.
GeneTreeiENSGT00390000001263.
HOGENOMiHOG000007618.
HOVERGENiHBG082144.
InParanoidiQ9DCE5.
KOiK14830.
OMAiSEFKAHE.
OrthoDBiEOG7P2XSW.
PhylomeDBiQ9DCE5.
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. 4 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. 3 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DCE5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELVAGSYEQ VLFGFTVQRG PAKSGHQETW TPVADFTHHS HTASLSVLAS
60 70 80 90 100
NSRYVVSGSK DETIHIYDMK RKVEHGALVH HAGTVTCLKF HGNQHLISGA
110 120 130 140 150
EDGHICIWDV KRWKCLKTFK AHRGHVTFLS IHPSGKLALS VGTDKTLRTW
160 170 180 190 200
NLIEGRSAFI KNIKENAHIV EWSPSGGKYI VVVQNKVDVY RLGTASVSGT
210 220 230 240 250
ITNGKRISSV TFLSDSVLAV AGDEEVVRIF DCDSLECLCE FRAHENRVKD
260 270 280 290 300
MVSFEVPDHH VLVTASNDGF IKMWTLPQDK KVPPSLLCEA KTGARLTCLT
310 320 330 340 350
VWLDRAANGM ASLPPAAEPC PDQPKTIEKE SGDTVQEETS EPNSEKSDVS
360 370 380
GDSKQPTKGN SPVTAKKRKM ATMSEKKRKK KM
Length:382
Mass (Da):42,116
Last modified:July 19, 2005 - v2
Checksum:i7EA5788A4B7EF2D1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761G → R in AAK51599 (PubMed:11389855).Curated
Sequence conflicti382 – 3821M → MSLTWQIPDFSSLSECPFDG ILHVPVRRKYLLP (Ref. 2) Curated
Sequence conflicti382 – 3821M → MSLTWQIPDFSSLSECPFDG ILHVPVRRKYLLP in BAB22407 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY030406 mRNA. Translation: AAK51599.1.
AF386076 mRNA. Translation: AAL40652.1.
AK002852 mRNA. Translation: BAB22407.1.
AK077941 mRNA. Translation: BAC37076.1.
AK150747 mRNA. Translation: BAE29818.1.
AK150919 mRNA. Translation: BAE29957.1.
BC051498 mRNA. Translation: AAH51498.1.
CCDSiCCDS36638.1.
RefSeqiNP_080826.2. NM_026550.3.
UniGeneiMm.24789.

Genome annotation databases

EnsembliENSMUST00000046951; ENSMUSP00000040846; ENSMUSG00000038683.
GeneIDi68083.
KEGGimmu:68083.
UCSCiuc007qer.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY030406 mRNA. Translation: AAK51599.1.
AF386076 mRNA. Translation: AAL40652.1.
AK002852 mRNA. Translation: BAB22407.1.
AK077941 mRNA. Translation: BAC37076.1.
AK150747 mRNA. Translation: BAE29818.1.
AK150919 mRNA. Translation: BAE29957.1.
BC051498 mRNA. Translation: AAH51498.1.
CCDSiCCDS36638.1.
RefSeqiNP_080826.2. NM_026550.3.
UniGeneiMm.24789.

3D structure databases

ProteinModelPortaliQ9DCE5.
SMRiQ9DCE5. Positions 15-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212647. 1 interaction.
STRINGi10090.ENSMUSP00000040846.

PTM databases

iPTMnetiQ9DCE5.
PhosphoSiteiQ9DCE5.

Proteomic databases

EPDiQ9DCE5.
MaxQBiQ9DCE5.
PaxDbiQ9DCE5.
PRIDEiQ9DCE5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000046951; ENSMUSP00000040846; ENSMUSG00000038683.
GeneIDi68083.
KEGGimmu:68083.
UCSCiuc007qer.2. mouse.

Organism-specific databases

CTDi55003.
MGIiMGI:1915333. Pak1ip1.

Phylogenomic databases

eggNOGiKOG0294. Eukaryota.
ENOG410XRDQ. LUCA.
GeneTreeiENSGT00390000001263.
HOGENOMiHOG000007618.
HOVERGENiHBG082144.
InParanoidiQ9DCE5.
KOiK14830.
OMAiSEFKAHE.
OrthoDBiEOG7P2XSW.
PhylomeDBiQ9DCE5.
TreeFamiTF326684.

Miscellaneous databases

ChiTaRSiPak1ip1. mouse.
NextBioi326384.
PROiQ9DCE5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DCE5.
CleanExiMM_PAK1IP1.
GenevisibleiQ9DCE5. MM.

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. 4 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. 3 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genetic and molecular characterization of Skb15, a highly conserved inhibitor of the fission yeast PAK, Shk1."
    Kim H.W., Yang P., Qyang Y., Lai H., Du H., Henkel J.S., Kumar K., Bao S., Liu M., Marcus S.
    Mol. Cell 7:1095-1101(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Mouse homolog of human p21-activated protein kinase-interacting protein 1 (hPIP1)."
    Liu M., Xia C.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Kidney and Testis.
  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] OF 254-382.
    Strain: C57BL/6J.
    Tissue: Thymus.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.

Entry informationi

Entry nameiPK1IP_MOUSE
AccessioniPrimary (citable) accession number: Q9DCE5
Secondary accession number(s): Q3UBK7
, Q80UT4, Q8C5N6, Q923K2, Q9D3E9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: March 16, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.