P3IP1_HUMAN
ID P3IP1_HUMAN Reviewed; 263 AA.
AC Q96FE7; B4DRR9; D1MEI0; O00318; Q49A94; Q86YW2; Q8NCJ9;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Phosphoinositide-3-kinase-interacting protein 1;
DE Short=PI3K-interacting protein 1;
DE AltName: Full=Kringle domain-containing protein HGFL;
DE Flags: Precursor;
GN Name=PIK3IP1; Synonyms=HGFL;
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] (ISOFORMS 1 AND 2), AND VARIANT SER-251.
RA Chiang H., Chang M.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND SUBCELLULAR LOCATION.
RX PubMed=19088825;
RA Gao P., Zeng W.T., Deng W.W., Li N., Shi T.P., Ma D.;
RT "Both PIK3IP1 and its novel found splicing isoform, PIK3IP1-v1, are located
RT on cell membrane and induce cell apoptosis.";
RL Beijing Da Xue Xue Bao 40:572-577(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-251.
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Mammary gland, and Tongue;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP SER-251.
RC TISSUE=Brain;
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 [8]
RP PROTEIN SEQUENCE OF 22-36.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [9]
RP GLYCOSYLATION AT SER-39 AND ASN-66, STRUCTURE OF CARBOHYDRATES, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
CC -!- FUNCTION: Negative regulator of hepatic phosphatidylinositol 3-kinase
CC (PI3K) activity. {ECO:0000250|UniProtKB:Q7TMJ8}.
CC -!- INTERACTION:
CC Q96FE7; P43364: MAGEA11; NbExp=3; IntAct=EBI-10285708, EBI-739552;
CC Q96FE7; O43934: MFSD11; NbExp=3; IntAct=EBI-10285708, EBI-17633886;
CC Q96FE7; P78382: SLC35A1; NbExp=3; IntAct=EBI-10285708, EBI-12870360;
CC Q96FE7; A2RU14: TMEM218; NbExp=3; IntAct=EBI-10285708, EBI-10173151;
CC Q96FE7; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-10285708, EBI-741480;
CC Q96FE7; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-10285708, EBI-10173939;
CC Q96FE7; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-10285708, EBI-947187;
CC Q96FE7; O75841: UPK1B; NbExp=3; IntAct=EBI-10285708, EBI-12237619;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19088825};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=HGFL(L);
CC IsoId=Q96FE7-1; Sequence=Displayed;
CC Name=2; Synonyms=HGFL(S);
CC IsoId=Q96FE7-2; Sequence=VSP_023639, VSP_023640;
CC Name=3;
CC IsoId=Q96FE7-3; Sequence=VSP_023638;
CC Name=4;
CC IsoId=Q96FE7-4; Sequence=VSP_043368;
CC Name=5; Synonyms=PIK3IP1-v1;
CC IsoId=Q96FE7-5; Sequence=VSP_053370;
CC -!- PTM: N- and O-glycosylated. O-glycosylated with core 1 or possibly core
CC 8 glycans. N-glycan heterogeneity at Asn-66: dHex1Hex5HexNAc4 (major)
CC and dHex1Hex6HexNAc5 (minor). {ECO:0000269|PubMed:22171320}.
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DR EMBL; AF528079; AAO33762.1; -; mRNA.
DR EMBL; AF528080; AAO33763.1; -; mRNA.
DR EMBL; GU135609; ACZ26468.1; -; mRNA.
DR EMBL; CR456340; CAG30226.1; -; mRNA.
DR EMBL; AK074688; BAC11140.1; -; mRNA.
DR EMBL; AK299397; BAG61381.1; -; mRNA.
DR EMBL; AC002073; AAB54054.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW59962.1; -; Genomic_DNA.
DR EMBL; BC011049; AAH11049.1; -; mRNA.
DR EMBL; BC041903; AAH41903.1; -; mRNA.
DR CCDS; CCDS13893.1; -. [Q96FE7-1]
DR CCDS; CCDS46690.1; -. [Q96FE7-4]
DR RefSeq; NP_001129383.1; NM_001135911.1. [Q96FE7-4]
DR RefSeq; NP_443112.2; NM_052880.4. [Q96FE7-1]
DR AlphaFoldDB; Q96FE7; -.
DR SMR; Q96FE7; -.
DR BioGRID; 125260; 21.
DR IntAct; Q96FE7; 7.
DR STRING; 9606.ENSP00000215912; -.
DR GlyConnect; 686; 11 N-Linked glycans (1 site), 5 O-Linked glycans (3 sites).
DR GlyGen; Q96FE7; 6 sites, 12 N-linked glycans (1 site), 6 O-linked glycans (4 sites).
DR iPTMnet; Q96FE7; -.
DR PhosphoSitePlus; Q96FE7; -.
DR BioMuta; PIK3IP1; -.
DR DMDM; 134034149; -.
DR jPOST; Q96FE7; -.
DR MassIVE; Q96FE7; -.
DR PaxDb; Q96FE7; -.
DR PeptideAtlas; Q96FE7; -.
DR PRIDE; Q96FE7; -.
DR ProteomicsDB; 12726; -.
DR ProteomicsDB; 76518; -. [Q96FE7-1]
DR ProteomicsDB; 76519; -. [Q96FE7-2]
DR ProteomicsDB; 76520; -. [Q96FE7-3]
DR ProteomicsDB; 76521; -. [Q96FE7-4]
DR Antibodypedia; 1229; 136 antibodies from 22 providers.
DR DNASU; 113791; -.
DR Ensembl; ENST00000215912.10; ENSP00000215912.4; ENSG00000100100.13. [Q96FE7-1]
DR Ensembl; ENST00000402249.7; ENSP00000385204.3; ENSG00000100100.13. [Q96FE7-2]
DR Ensembl; ENST00000441972.5; ENSP00000415608.1; ENSG00000100100.13. [Q96FE7-4]
DR GeneID; 113791; -.
DR KEGG; hsa:113791; -.
DR MANE-Select; ENST00000215912.10; ENSP00000215912.4; NM_052880.5; NP_443112.2.
DR UCSC; uc003akm.4; human. [Q96FE7-1]
DR CTD; 113791; -.
DR DisGeNET; 113791; -.
DR GeneCards; PIK3IP1; -.
DR HGNC; HGNC:24942; PIK3IP1.
DR HPA; ENSG00000100100; Low tissue specificity.
DR MIM; 619158; gene.
DR neXtProt; NX_Q96FE7; -.
DR OpenTargets; ENSG00000100100; -.
DR PharmGKB; PA162399553; -.
DR VEuPathDB; HostDB:ENSG00000100100; -.
DR eggNOG; ENOG502QTWD; Eukaryota.
DR GeneTree; ENSGT00390000017774; -.
DR HOGENOM; CLU_092099_0_0_1; -.
DR InParanoid; Q96FE7; -.
DR OMA; DQKVCER; -.
DR PhylomeDB; Q96FE7; -.
DR TreeFam; TF331319; -.
DR PathwayCommons; Q96FE7; -.
DR SignaLink; Q96FE7; -.
DR SIGNOR; Q96FE7; -.
DR BioGRID-ORCS; 113791; 16 hits in 1076 CRISPR screens.
DR ChiTaRS; PIK3IP1; human.
DR GeneWiki; PIK3IP1; -.
DR GenomeRNAi; 113791; -.
DR Pharos; Q96FE7; Tbio.
DR PRO; PR:Q96FE7; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q96FE7; protein.
DR Bgee; ENSG00000100100; Expressed in lymph node and 194 other tissues.
DR ExpressionAtlas; Q96FE7; baseline and differential.
DR Genevisible; Q96FE7; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0036313; F:phosphatidylinositol 3-kinase catalytic subunit binding; IPI:UniProtKB.
DR GO; GO:0043553; P:negative regulation of phosphatidylinositol 3-kinase activity; IDA:UniProtKB.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR CDD; cd00108; KR; 1.
DR Gene3D; 2.40.20.10; -; 1.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR Pfam; PF00051; Kringle; 1.
DR SMART; SM00130; KR; 1.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Kringle; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 22..263
FT /note="Phosphoinositide-3-kinase-interacting protein 1"
FT /id="PRO_0000280347"
FT TOPO_DOM 22..168
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..101
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT REGION 242..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 39
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:22171320"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:22171320"
FT DISULFID 25..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DISULFID 46..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DISULFID 70..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT VAR_SEQ 1..157
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023638"
FT VAR_SEQ 24..102
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:19088825"
FT /id="VSP_053370"
FT VAR_SEQ 171..263
FT /note="YVLGITMMVIIIAIGAGIILGYSYKRGKDLKEQHDQKVCEREMQRITLPLSA
FT FTNPTCEIVDEKTVVVHTSQTPVDPQEGTTPLMGQAGTPGA -> GRI (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043368"
FT VAR_SEQ 197..234
FT /note="GKDLKEQHDQKVCEREMQRITLPLSAFTNPTCEIVDEK -> SVASLLGPLR
FT RRGGRYTKSNFVAFLPKRKQDVENQLKM (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_023639"
FT VAR_SEQ 235..263
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_023640"
FT VARIANT 251
FT /note="T -> S (in dbSNP:rs2040533)"
FT /evidence="ECO:0000269|PubMed:15461802,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT /id="VAR_031121"
FT CONFLICT 98
FT /note="D -> G (in Ref. 4; BAC11140)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="E -> G (in Ref. 4; BAC11140)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 28248 MW; 197C3EEE8E54A242 CRC64;
MLLAWVQAFL VSNMLLAEAY GSGGCFWDNG HLYREDQTSP APGLRCLNWL DAQSGLASAP
VSGAGNHSYC RNPDEDPRGP WCYVSGEAGV PEKRPCEDLR CPETTSQALP AFTTEIQEAS
EGPGADEVQV FAPANALPAR SEAAAVQPVI GISQRVRMNS KEKKDLGTLG YVLGITMMVI
IIAIGAGIIL GYSYKRGKDL KEQHDQKVCE REMQRITLPL SAFTNPTCEI VDEKTVVVHT
SQTPVDPQEG TTPLMGQAGT PGA
