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Ras and Rab interactor 1 (Ras inhibitor JC99) (Ras interaction/interference protein 1)

 RIN1_HUMAN              Reviewed;         783 AA.
Q13671; O15010; Q00427; Q96CC8;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 4.
12-SEP-2018, entry version 170.
RecName: Full=Ras and Rab interactor 1;
AltName: Full=Ras inhibitor JC99;
AltName: Full=Ras interaction/interference protein 1;
Name=RIN1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Glial cell;
PubMed=1849280; DOI=10.1073/pnas.88.7.2913;
Colicelli J., Nicolette C., Birchmeier C., Rodgers L., Riggs M.,
Wigler M.;
"Expression of three mammalian cDNAs that interfere with RAS function
in Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 88:2913-2917(1991).
[2]
PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7862125; DOI=10.1128/MCB.15.3.1318;
Han L., Colicelli J.;
"A human protein selected for interference with Ras function interacts
directly with Ras and competes with Raf1.";
Mol. Cell. Biol. 15:1318-1323(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS RIN1 AND RIN1-DELTA), SEQUENCE
REVISION, FUNCTION, DOMAINS, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
TISSUE=Glioblastoma;
PubMed=9144171; DOI=10.1073/pnas.94.10.4954;
Han L., Wong D., Dhaka A., Afar D.E.H., White M., Xie W.,
Herschman H., Witte O., Colicelli J.;
"Protein binding and signaling properties of RIN1 suggest a unique
effector function.";
Proc. Natl. Acad. Sci. U.S.A. 94:4954-4959(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, INTERACTION WITH ABL1, AND PHOSPHORYLATION BY ABL1.
PubMed=9208849; DOI=10.1016/S1074-7613(00)80452-5;
Afar D.E.H., Han L., McLaughlin J., Wong S., Dhaka A., Parmar K.,
Rosenberg N., Witte O.N., Colicelli J.;
"Regulation of the oncogenic activity of BCR-ABL by a tightly bound
substrate protein RIN1.";
Immunity 6:773-782(1997).
[6]
GEF ACTIVITY.
PubMed=11703925; DOI=10.1016/S1534-5807(01)00008-9;
Tall G.G., Barbieri M.A., Stahl P.D., Horazdovsky B.F.;
"Ras-activated endocytosis is mediated by the Rab5 guanine nucleotide
exchange activity of RIN1.";
Dev. Cell 1:73-82(2001).
[7]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-351, AND MUTAGENESIS OF
SER-351.
PubMed=11784866; DOI=10.1128/MCB.22.13.4638-4651.2002;
Wang Y., Waldron R.T., Dhaka A., Patel A., Riley M.M., Rozengurt E.,
Colicelli J.;
"The RAS effector RIN1 directly competes with RAF and is regulated by
14-3-3 proteins.";
Mol. Cell. Biol. 22:916-926(2002).
[8]
FUNCTION, INTERACTION WITH ABL1 AND ABL2, AND PHOSPHORYLATION AT
TYR-36.
PubMed=15886098; DOI=10.1016/j.cub.2005.03.049;
Hu H., Bliss J.M., Wang Y., Colicelli J.;
"RIN1 is an ABL tyrosine kinase activator and a regulator of
epithelial-cell adhesion and migration.";
Curr. Biol. 15:815-823(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 AND SER-337, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; SER-258; SER-337;
SER-351 AND SER-609, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-3; SER-16 AND SER-337, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-351; SER-609
AND SER-611, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-692, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Ras effector protein, which may serve as an inhibitory
modulator of neuronal plasticity in aversive memory formation. Can
affect Ras signaling at different levels. First, by competing with
RAF1 protein for binding to activated Ras. Second, by enhancing
signaling from ABL1 and ABL2, which regulate cytoskeletal
remodeling. Third, by activating RAB5A, possibly by functioning as
a guanine nucleotide exchange factor (GEF) for RAB5A, by
exchanging bound GDP for free GTP, and facilitating Ras-activated
receptor endocytosis. {ECO:0000269|PubMed:15886098,
ECO:0000269|PubMed:9144171, ECO:0000269|PubMed:9208849}.
-!- SUBUNIT: Interacts with the GTP-bound form of Ras proteins (NRAS,
HRAS and KRAS). This interaction prevents the association between
RAF1 and Ras. Interacts with 14-3-3 proteins YWHAB, YWHAE and
YWHAZ when phosphorylated on Ser-351. Interacts with the SH3
domain of ABL1 and ABL2. Interacts with RAB5A. The interaction
with Ras is probably regulated and antagonized by the interaction
with 14-3-3 proteins. The interaction with 14-3-3 proteins is
regulated by phosphorylation on Ser-351.
{ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:9208849}.
-!- INTERACTION:
P00519:ABL1; NbExp=4; IntAct=EBI-366017, EBI-375543;
P42684:ABL2; NbExp=4; IntAct=EBI-366017, EBI-1102694;
Q49AR9:ANKS1A; NbExp=4; IntAct=EBI-366017, EBI-11954519;
Q13137:CALCOCO2; NbExp=4; IntAct=EBI-366017, EBI-739580;
P00533:EGFR; NbExp=3; IntAct=EBI-366017, EBI-297353;
P01112:HRAS; NbExp=5; IntAct=EBI-366017, EBI-350145;
Q9BRK4:LZTS2; NbExp=8; IntAct=EBI-366017, EBI-741037;
P01111:NRAS; NbExp=4; IntAct=EBI-366017, EBI-721993;
O75886:STAM2; NbExp=4; IntAct=EBI-366017, EBI-373258;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11784866}.
Membrane {ECO:0000269|PubMed:11784866}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:11784866}. Note=Some amount is membrane-
associated.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=RIN1;
IsoId=Q13671-1; Sequence=Displayed;
Name=RIN1-delta;
IsoId=Q13671-2; Sequence=VSP_004377;
Note=Shows reduced ability to bind to Ras and 14-3-3 proteins.;
-!- TISSUE SPECIFICITY: Expressed in all tissues examined with high
levels in brain, placenta and pancreas.
{ECO:0000269|PubMed:9144171}.
-!- PTM: Phosphorylated on tyrosine residues by ABL1 and ABL2.
Phosphorylation at Ser-351 by PRKD1 induces interaction with 14-3-
3 proteins. {ECO:0000269|PubMed:11784866,
ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:9144171,
ECO:0000269|PubMed:9208849}.
-!- SIMILARITY: Belongs to the RIN (Ras interaction/interference)
family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; L36463; AAB67270.1; -; mRNA.
EMBL; BC014417; AAH14417.1; -; mRNA.
CCDS; CCDS31614.1; -. [Q13671-1]
PIR; A58613; A38637.
RefSeq; NP_004283.2; NM_004292.2. [Q13671-1]
UniGene; Hs.1030; -.
ProteinModelPortal; Q13671; -.
SMR; Q13671; -.
BioGrid; 114972; 30.
CORUM; Q13671; -.
DIP; DIP-117N; -.
IntAct; Q13671; 52.
MINT; Q13671; -.
STRING; 9606.ENSP00000310406; -.
iPTMnet; Q13671; -.
PhosphoSitePlus; Q13671; -.
BioMuta; RIN1; -.
DMDM; 116242760; -.
EPD; Q13671; -.
MaxQB; Q13671; -.
PaxDb; Q13671; -.
PeptideAtlas; Q13671; -.
PRIDE; Q13671; -.
ProteomicsDB; 59652; -.
ProteomicsDB; 59653; -. [Q13671-2]
DNASU; 9610; -.
Ensembl; ENST00000311320; ENSP00000310406; ENSG00000174791. [Q13671-1]
GeneID; 9610; -.
KEGG; hsa:9610; -.
UCSC; uc001ohn.2; human. [Q13671-1]
CTD; 9610; -.
DisGeNET; 9610; -.
EuPathDB; HostDB:ENSG00000174791.10; -.
GeneCards; RIN1; -.
HGNC; HGNC:18749; RIN1.
HPA; HPA035491; -.
MIM; 605965; gene.
neXtProt; NX_Q13671; -.
OpenTargets; ENSG00000174791; -.
PharmGKB; PA38671; -.
eggNOG; KOG2320; Eukaryota.
eggNOG; ENOG410ZZW5; LUCA.
GeneTree; ENSGT00530000063053; -.
HOGENOM; HOG000154128; -.
HOVERGEN; HBG036105; -.
InParanoid; Q13671; -.
KO; K17638; -.
OMA; FFNPLFP; -.
OrthoDB; EOG091G02V2; -.
PhylomeDB; Q13671; -.
TreeFam; TF331067; -.
Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
SignaLink; Q13671; -.
SIGNOR; Q13671; -.
ChiTaRS; RIN1; human.
GeneWiki; RIN1; -.
GenomeRNAi; 9610; -.
PRO; PR:Q13671; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000174791; Expressed in 218 organ(s), highest expression level in parotid gland.
CleanEx; HS_RIN1; -.
ExpressionAtlas; Q13671; baseline and differential.
Genevisible; Q13671; HS.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
GO; GO:0017112; F:Rab guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0008306; P:associative learning; IEA:Ensembl.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0031914; P:negative regulation of synaptic plasticity; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd10393; SH2_RIN1; 1.
Gene3D; 1.20.1050.80; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR000159; RA_dom.
InterPro; IPR035867; RIN1_SH2.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR003123; VPS9.
InterPro; IPR037191; VPS9_dom_sf.
Pfam; PF00788; RA; 1.
Pfam; PF02204; VPS9; 1.
SMART; SM00314; RA; 1.
SMART; SM00252; SH2; 1.
SMART; SM00167; VPS9; 1.
SUPFAM; SSF109993; SSF109993; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50200; RA; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS51205; VPS9; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Cytoskeleton; Endocytosis; GTPase activation; Membrane; Methylation;
Phosphoprotein; Reference proteome; SH2 domain.
CHAIN 1 783 Ras and Rab interactor 1.
/FTId=PRO_0000191317.
DOMAIN 69 163 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 456 598 VPS9. {ECO:0000255|PROSITE-
ProRule:PRU00550}.
DOMAIN 624 706 Ras-associating. {ECO:0000255|PROSITE-
ProRule:PRU00166}.
REGION 294 727 Ras and 14-3-3 protein binding region.
COMPBIAS 259 268 Pro-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 36 36 Phosphotyrosine; by ABL1 and ABL2.
{ECO:0000269|PubMed:15886098}.
MOD_RES 210 210 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 258 258 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 333 333 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:23186163}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 351 351 Phosphoserine; by PKD/PRKD1.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11784866}.
MOD_RES 609 609 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 611 611 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 692 692 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
VAR_SEQ 429 490 Missing (in isoform RIN1-delta).
{ECO:0000303|PubMed:9144171}.
/FTId=VSP_004377.
MUTAGEN 351 351 S->A: Abolishes phosphorylation by PKD
and the interaction with 14-3-3 proteins.
{ECO:0000269|PubMed:11784866}.
CONFLICT 392 395 AGPE -> DGQR (in Ref. 1, 2 and 3).
{ECO:0000305}.
CONFLICT 400 400 Q -> E (in Ref. 1, 2 and 3).
{ECO:0000305}.
CONFLICT 423 423 L -> V (in Ref. 1, 2 and 3).
{ECO:0000305}.
CONFLICT 503 503 L -> V (in Ref. 1, 2 and 3).
{ECO:0000305}.
CONFLICT 534 534 A -> S (in Ref. 1, 2 and 3).
{ECO:0000305}.
CONFLICT 538 538 E -> G (in Ref. 1, 2 and 3).
{ECO:0000305}.
SEQUENCE 783 AA; 84099 MW; 2B4DA70147CDDDFE CRC64;
MESPGESGAG SPGAPSPSSF TTGHLAREKP AQDPLYDVPN ASGGQAGGPQ RPGRVVSLRE
RLLLTRPVWL QLQANAAAAL HMLRTEPPGT FLVRKSNTRQ CQALCMRLPE ASGPSFVSSH
YILESPGGVS LEGSELMFPD LVQLICAYCH TRDILLLPLQ LPRAIHHAAT HKELEAISHL
GIEFWSSSLN IKAQRGPAGG PVLPQLKARS PQELDQGTGA ALCFFNPLFP GDLGPTKREK
FKRSFKVRVS TETSSPLSPP AVPPPPVPVL PGAVPSQTER LPPCQLLRRE SSVGYRVPAG
SGPSLPPMPS LQEVDCGSPS SSEEEGVPGS RGSPATSPHL GRRRPLLRSM SAAFCSLLAP
ERQVGRAAAA LMQDRHTAAG QLVQDLLTQV RAGPEPQELQ GIRQALSRAR AMLSAELGPE
KLLSPKRLEH VLEKSLHCSV LKPLRPILAA RLRRRLAADG SLGRLAEGLR LARAQGPGAF
GSHLSLPSPV ELEQVRQKLL QLLRTYSPSA QVKRLLQACK LLYMALRTQE GEGAGADEFL
PLLSLVLAHC DLPELLLEAE YMSELLEPSL LTGEGGYYLT SLSASLALLS GLGQAHTLPL
SPVQELRRSL SLWEQRRLPA THCFQHLLRV AYQDPSSGCT SKTLAVPPEA SIATLNQLCA
TKFRVTQPNT FGLFLYKEQG YHRLPPGALA HRLPTTGYLV YRRAEWPETQ GAVTEEEGSG
QSEARSRGEE QGCQGDGDAG VKASPRDIRE QSETTAEGGQ GQAQEGPAQP GEPEAEGSRA
AEE


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