S11IP_HUMAN
ID S11IP_HUMAN Reviewed; 1088 AA.
AC Q8N1F8; C9JQV3; Q8NAW9; Q8WXE4; Q96CN3; Q96PY9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 4.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Serine/threonine-protein kinase 11-interacting protein;
DE AltName: Full=LKB1-interacting protein 1;
GN Name=STK11IP; Synonyms=KIAA1898, LIP1, LKB1IP, STK11IP1;
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, IDENTIFICATION IN A TERNARY COMPLEX
RP COMPOSED OF STK11/LKB1 AND SMAD4, INTERACTION WITH STK11/LKB1 AND SMAD4,
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, AND VARIANT PHE-741.
RX PubMed=11741830; DOI=10.1093/hmg/10.25.2869;
RA Smith D.P., Rayter S.I., Niederlander C., Spicer J., Jones C.M.,
RA Ashworth A.;
RT "LIP1, a cytoplasmic protein functionally linked to the Peutz-Jeghers
RT syndrome kinase LKB1.";
RL Hum. Mol. Genet. 10:2869-2877(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-382; GLY-399;
RP ILE-552; PHE-741 AND VAL-1074.
RC TISSUE=Brain, and Carcinoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 76-1088, AND VARIANT PHE-741.
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387; SER-389; SER-392 AND
RP SER-761, AND IDENTIFICATION BY 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP IDENTIFICATION BY 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-387; SER-599; SER-761;
RP SER-773 AND SER-777, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470 AND SER-761, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP VARIANT ILE-552.
RX PubMed=12438709; DOI=10.1159/000066620;
RA Buchet-Poyau K., Mehenni H., Radhakrishna U., Antonarakis S.E.;
RT "Search for the second Peutz-Jeghers syndrome locus: exclusion of the
RT STK13, PRKCG, KLK10, and PSCD2 genes on chromosome 19 and the STK11IP gene
RT on chromosome 2.";
RL Cytogenet. Genome Res. 97:171-178(2002).
CC -!- FUNCTION: May regulate STK11/LKB1 function by controlling its
CC subcellular localization. {ECO:0000269|PubMed:11741830}.
CC -!- SUBUNIT: Found in a ternary complex composed of STK11/LKB1, STK11IP and
CC SMAD4. Interacts with STK11/LKB1 and SMAD4.
CC {ECO:0000269|PubMed:11741830}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11741830}.
CC Note=Some cells show granular or punctuate expression. Colocalizes with
CC STK11/LKB1 and SMAD4 in granular or punctuate structures.
CC -!- SIMILARITY: Belongs to the STK11IP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34051.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL49726.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF450267; AAL49726.1; ALT_INIT; mRNA.
DR EMBL; AC009955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014114; AAH14114.2; -; mRNA.
DR EMBL; BC034051; AAH34051.1; ALT_INIT; mRNA.
DR EMBL; AB067485; BAB67791.1; -; mRNA.
DR CCDS; CCDS46521.2; -.
DR RefSeq; NP_443134.3; NM_052902.3.
DR AlphaFoldDB; Q8N1F8; -.
DR BioGRID; 125352; 84.
DR IntAct; Q8N1F8; 20.
DR MINT; Q8N1F8; -.
DR STRING; 9606.ENSP00000295641; -.
DR GlyGen; Q8N1F8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N1F8; -.
DR PhosphoSitePlus; Q8N1F8; -.
DR BioMuta; STK11IP; -.
DR DMDM; 296452972; -.
DR EPD; Q8N1F8; -.
DR jPOST; Q8N1F8; -.
DR MassIVE; Q8N1F8; -.
DR MaxQB; Q8N1F8; -.
DR PaxDb; Q8N1F8; -.
DR PeptideAtlas; Q8N1F8; -.
DR PRIDE; Q8N1F8; -.
DR ProteomicsDB; 11298; -.
DR Antibodypedia; 34344; 144 antibodies from 26 providers.
DR DNASU; 114790; -.
DR Ensembl; ENST00000456909.6; ENSP00000389383.1; ENSG00000144589.22.
DR GeneID; 114790; -.
DR KEGG; hsa:114790; -.
DR MANE-Select; ENST00000456909.6; ENSP00000389383.1; NM_052902.4; NP_443134.3.
DR UCSC; uc002vml.3; human.
DR CTD; 114790; -.
DR DisGeNET; 114790; -.
DR GeneCards; STK11IP; -.
DR HGNC; HGNC:19184; STK11IP.
DR HPA; ENSG00000144589; Low tissue specificity.
DR MIM; 607172; gene.
DR neXtProt; NX_Q8N1F8; -.
DR OpenTargets; ENSG00000144589; -.
DR PharmGKB; PA38822; -.
DR VEuPathDB; HostDB:ENSG00000144589; -.
DR eggNOG; KOG1859; Eukaryota.
DR GeneTree; ENSGT00940000158471; -.
DR InParanoid; Q8N1F8; -.
DR OMA; VCDPPGH; -.
DR OrthoDB; 1041637at2759; -.
DR PhylomeDB; Q8N1F8; -.
DR TreeFam; TF326448; -.
DR PathwayCommons; Q8N1F8; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q8N1F8; -.
DR BioGRID-ORCS; 114790; 14 hits in 1019 CRISPR screens.
DR GenomeRNAi; 114790; -.
DR Pharos; Q8N1F8; Tdark.
DR PRO; PR:Q8N1F8; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8N1F8; protein.
DR Bgee; ENSG00000144589; Expressed in right testis and 145 other tissues.
DR ExpressionAtlas; Q8N1F8; baseline and differential.
DR Genevisible; Q8N1F8; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0008104; P:protein localization; IDA:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR031782; LIP1_N.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF15904; LIP1; 1.
DR PROSITE; PS51450; LRR; 7.
PE 1: Evidence at protein level;
KW Cytoplasm; Leucine-rich repeat; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1088
FT /note="Serine/threonine-protein kinase 11-interacting
FT protein"
FT /id="PRO_0000317462"
FT REPEAT 109..130
FT /note="LRR 1"
FT REPEAT 132..152
FT /note="LRR 2"
FT REPEAT 164..185
FT /note="LRR 3"
FT REPEAT 187..209
FT /note="LRR 4"
FT REPEAT 210..231
FT /note="LRR 5"
FT REPEAT 233..254
FT /note="LRR 6"
FT REPEAT 255..276
FT /note="LRR 7"
FT REPEAT 280..301
FT /note="LRR 8"
FT REGION 335..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..476
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..531
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 382
FT /note="R -> H (in dbSNP:rs17855575)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038529"
FT VARIANT 399
FT /note="R -> G (in dbSNP:rs17855576)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038530"
FT VARIANT 552
FT /note="V -> I (in dbSNP:rs673951)"
FT /evidence="ECO:0000269|PubMed:12438709,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_038531"
FT VARIANT 741
FT /note="S -> F (in dbSNP:rs627530)"
FT /evidence="ECO:0000269|PubMed:11572484,
FT ECO:0000269|PubMed:11741830, ECO:0000269|PubMed:15489334"
FT /id="VAR_038532"
FT VARIANT 1074
FT /note="I -> V (in dbSNP:rs17853279)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038533"
FT CONFLICT 337
FT /note="S -> N (in Ref. 1; AAL49726)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1088 AA; 120259 MW; B5EA45D6C1B7BEF8 CRC64;
MTTAQRDSLL WKLAGLLRES GDVVLSGCST LSLLTPTLQQ LNHVFELHLG PWGPGQTGFV
ALPSHPADSP VILQLQFLFD VLQKTLSLKL VHVAGPGPTG PIKIFPFKSL RHLELRGVPL
HCLHGLRGIY SQLETLICSR SLQALEELLS ACGGDFCSAL PWLALLSANF SYNALTALDS
SLRLLSALRF LNLSHNQVQD CQGFLMDLCE LHHLDISYNR LHLVPRMGPS GAALGVLILR
GNELRSLHGL EQLRNLRHLD LAYNLLEGHR ELSPLWLLAE LRKLYLEGNP LWFHPEHRAA
TAQYLSPRAR DAATGFLLDG KVLSLTDFQT HTSLGLSPMG PPLPWPVGST PETSGGPDLS
DSLSSGGVVT QPLLHKVKSR VRVRRASISE PSDTDPEPRT LNPSPAGWFV QQHPELELMS
SFRERFGRNW LQYRSHLEPS GNPLPATPTT SAPSAPPASS QGPDTAPRPS PPQEEARGPQ
ESPQKMSEEV RAEPQEEEEE KEGKEEKEEG EMVEQGEEEA GEEEEEEQDQ KEVEAELCRP
LLVCPLEGPE GVRGRECFLR VTSAHLFEVE LQAARTLERL ELQSLEAAEI EPEAQAQRSP
RPTGSDLLPG APILSLRFSY ICPDRQLRRY LVLEPDAHAA VQELLAVLTP VTNVAREQLG
EARDLLLGRF QCLRCGHEFK PEEPRMGLDS EEGWRPLFQK TESPAVCPNC GSDHVVLLAV
SRGTPNRERK QGEQSLAPSP SASPVCHPPG HGDHLDRAKN SPPQAPSTRD HGSWSLSPPP
ERCGLRSVDH RLRLFLDVEV FSDAQEEFQC CLKVPVALAG HTGEFMCLVV VSDRRLYLLK
VTGEMREPPA SWLQLTLAVP LQDLSGIELG LAGQSLRLEW AAGAGRCVLL PRDARHCRAF
LEELLDVLQS LPPAWRNCVS ATEEEVTPQH RLWPLLEKDS SLEARQFFYL RAFLVEGPST
CLVSLLLTPS TLFLLDEDAA GSPAEPSPPA ASGEASEKVP PSGPGPAVRV REQQPLSSLS
SVLLYRSAPE DLRLLFYDEV SRLESFWALR VVCQEQLTAL LAWIREPWEE LFSIGLRTVI
QEALALDR
