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Ras and Rab interactor 2 (Ras association domain family 4) (Ras inhibitor JC265) (Ras interaction/interference protein 2)

 RIN2_HUMAN              Reviewed;         895 AA.
Q8WYP3; Q00425; Q5TFT8; Q9BQL3; Q9H071;
01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
28-MAR-2018, entry version 136.
RecName: Full=Ras and Rab interactor 2;
AltName: Full=Ras association domain family 4;
AltName: Full=Ras inhibitor JC265;
AltName: Full=Ras interaction/interference protein 2;
Name=RIN2; Synonyms=RASSF4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION,
AND INTERACTION WITH RAB5B.
TISSUE=Leukocyte;
PubMed=11733506; DOI=10.1074/jbc.M106276200;
Saito K., Murai J., Kajiho H., Kontani K., Kurosu H., Katada T.;
"A novel binding protein composed of homophilic tetramer exhibits
unique properties for the small GTPase Rab5.";
J. Biol. Chem. 277:3412-3418(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-852 (ISOFORM 2), AND
VARIANT THR-197.
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-895 (ISOFORMS 1/2).
TISSUE=Uterus;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 425-895 (ISOFORMS 1/2), AND INTERACTION
WITH RAS.
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[7]
INVOLVEMENT IN MACS SYNDROME.
PubMed=19631308; DOI=10.1016/j.ajhg.2009.07.001;
Basel-Vanagaite L., Sarig O., Hershkovitz D., Fuchs-Telem D.,
Rapaport D., Gat A., Isman G., Shirazi I., Shohat M., Enk C.D.,
Birk E., Kohlhase J., Matysiak-Scholze U., Maya I., Knopf C.,
Peffekoven A., Hennies H.-C., Bergman R., Horowitz M.,
Ishida-Yamamoto A., Sprecher E.;
"RIN2 deficiency results in macrocephaly, alopecia, cutis laxa, and
scoliosis: MACS syndrome.";
Am. J. Hum. Genet. 85:254-263(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Ras effector protein. May function as an upstream
activator and/or downstream effector for RAB5B in endocytic
pathway. May function as a guanine nucleotide exchange (GEF) of
RAB5B, required for activating the RAB5 proteins by exchanging
bound GDP for free GTP. {ECO:0000269|PubMed:11733506}.
-!- SUBUNIT: Homotetramer; probably composed of anti-parallel linkage
of two parallel dimers. Interacts with Ras. Interacts with RAB5B,
with a much higher affinity for GTP-bound activated RAB5B. Does
not interact with other members of the Rab family.
{ECO:0000269|PubMed:11733506, ECO:0000269|PubMed:1849280}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8WYP3-1; Sequence=Displayed;
Name=2;
IsoId=Q8WYP3-2; Sequence=VSP_015145;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in heart, kidney,
lung placenta. Expressed at low level in skeletal muscle, spleen
and peripheral blood. {ECO:0000269|PubMed:11733506}.
-!- DISEASE: MACS syndrome (MACS) [MIM:613075]: A complex disorder of
elastic tissue characterized by sagging skin and occasionally by
life-threatening visceral complications.
{ECO:0000269|PubMed:19631308}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the RIN (Ras interaction/interference)
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB66858.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB060339; BAB84317.1; -; mRNA.
EMBL; AL049538; CAI19340.1; -; Genomic_DNA.
EMBL; AL132821; CAI19340.1; JOINED; Genomic_DNA.
EMBL; AL132821; CAI23572.1; -; Genomic_DNA.
EMBL; AL049538; CAI23572.1; JOINED; Genomic_DNA.
EMBL; AK094884; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AL136924; CAB66858.1; ALT_INIT; mRNA.
EMBL; M37190; AAA36553.1; -; mRNA.
CCDS; CCDS56182.1; -. [Q8WYP3-2]
PIR; B38637; B38637.
RefSeq; NP_001229510.1; NM_001242581.1. [Q8WYP3-2]
RefSeq; NP_061866.1; NM_018993.3. [Q8WYP3-1]
RefSeq; XP_005260788.1; XM_005260731.2. [Q8WYP3-1]
RefSeq; XP_006723637.1; XM_006723574.3. [Q8WYP3-1]
RefSeq; XP_006723638.1; XM_006723575.3. [Q8WYP3-1]
RefSeq; XP_006723640.1; XM_006723577.2. [Q8WYP3-1]
RefSeq; XP_011527559.1; XM_011529257.1. [Q8WYP3-1]
RefSeq; XP_011527560.1; XM_011529258.2. [Q8WYP3-1]
RefSeq; XP_016883376.1; XM_017027887.1. [Q8WYP3-2]
RefSeq; XP_016883377.1; XM_017027888.1. [Q8WYP3-2]
RefSeq; XP_016883379.1; XM_017027890.1. [Q8WYP3-1]
UniGene; Hs.472270; -.
UniGene; Hs.733605; -.
ProteinModelPortal; Q8WYP3; -.
BioGrid; 119960; 10.
IntAct; Q8WYP3; 3.
MINT; Q8WYP3; -.
STRING; 9606.ENSP00000255006; -.
iPTMnet; Q8WYP3; -.
PhosphoSitePlus; Q8WYP3; -.
BioMuta; RIN2; -.
DMDM; 28201876; -.
MaxQB; Q8WYP3; -.
PaxDb; Q8WYP3; -.
PeptideAtlas; Q8WYP3; -.
PRIDE; Q8WYP3; -.
Ensembl; ENST00000255006; ENSP00000255006; ENSG00000132669. [Q8WYP3-2]
GeneID; 54453; -.
KEGG; hsa:54453; -.
UCSC; uc002wro.3; human. [Q8WYP3-1]
CTD; 54453; -.
DisGeNET; 54453; -.
EuPathDB; HostDB:ENSG00000132669.12; -.
GeneCards; RIN2; -.
HGNC; HGNC:18750; RIN2.
HPA; HPA034641; -.
MalaCards; RIN2; -.
MIM; 610222; gene.
MIM; 613075; phenotype.
neXtProt; NX_Q8WYP3; -.
OpenTargets; ENSG00000132669; -.
Orphanet; 217335; MACS syndrome.
PharmGKB; PA38672; -.
eggNOG; KOG2320; Eukaryota.
eggNOG; ENOG410ZZW5; LUCA.
GeneTree; ENSGT00530000063053; -.
HOVERGEN; HBG023719; -.
InParanoid; Q8WYP3; -.
OMA; RTPNANG; -.
OrthoDB; EOG091G02V2; -.
PhylomeDB; Q8WYP3; -.
TreeFam; TF331067; -.
Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
ChiTaRS; RIN2; human.
GenomeRNAi; 54453; -.
PRO; PR:Q8WYP3; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000132669; -.
CleanEx; HS_RASSF4; -.
CleanEx; HS_RIN2; -.
ExpressionAtlas; Q8WYP3; baseline and differential.
Genevisible; Q8WYP3; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
GO; GO:0030695; F:GTPase regulator activity; NAS:UniProtKB.
GO; GO:0017112; F:Rab guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0007264; P:small GTPase mediated signal transduction; NAS:UniProtKB.
CDD; cd10394; SH2_RIN2; 1.
Gene3D; 1.20.1050.80; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR000159; RA_dom.
InterPro; IPR035868; RIN2_SH2.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR003123; VPS9.
InterPro; IPR037191; VPS9_dom_sf.
Pfam; PF00788; RA; 1.
Pfam; PF02204; VPS9; 1.
SMART; SM00314; RA; 1.
SMART; SM00167; VPS9; 1.
SUPFAM; SSF109993; SSF109993; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50200; RA; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS51205; VPS9; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Endocytosis;
GTPase activation; Phosphoprotein; Polymorphism; Reference proteome;
SH2 domain.
CHAIN 1 895 Ras and Rab interactor 2.
/FTId=PRO_0000191320.
DOMAIN 97 190 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 618 757 VPS9. {ECO:0000255|PROSITE-
ProRule:PRU00550}.
DOMAIN 787 878 Ras-associating. {ECO:0000255|PROSITE-
ProRule:PRU00166}.
COMPBIAS 307 314 Poly-Pro.
MOD_RES 366 366 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D684}.
MOD_RES 501 501 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D684}.
MOD_RES 509 509 Phosphothreonine.
{ECO:0000244|PubMed:18318008}.
VAR_SEQ 1 1 M -> MLDSFSQESTLPFREARKRTSFQPVQVWRNFTASQT
TESPACSGASLGEM (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_015145.
VARIANT 197 197 S -> T (in dbSNP:rs3803981).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_024694.
VARIANT 643 643 A -> T (in dbSNP:rs199603).
/FTId=VAR_052945.
CONFLICT 192 192 I -> V (in Ref. 3; AK094884).
{ECO:0000305}.
SEQUENCE 895 AA; 100163 MW; 0DECDBF8D2629EE4 CRC64;
MTAWTMGARG LDKRGSFFKL IDTIASEIGE LKQEMVRTDV NLENGLEPAE THSMVRHKDG
GYSEEEDVKT CARDSGYDSL SNRLSILDRL LHTHPIWLQL SLSEEEAAEV LQAQPPGIFL
VHKSTKMQKK VLSLRLPCEF GAPLKEFAIK ESTYTFSLEG SGISFADLFR LIAFYCISRD
VLPFTLKLPY AISTAKSEAQ LEELAQMGLN FWSSPADSKP PNLPPPHRPL SSDGVCPASL
RQLCLINGVH SIKTRTPSEL ECSQTNGALC FINPLFLKVH SQDLSGGLKR PSTRTPNANG
TERTRSPPPR PPPPAINSLH TSPRLARTET QTSMPETVNH NKHGNVALPG TKPTPIPPPR
LKKQASFLEA EGGAKTLSGG RPGAGPELEL GTAGSPGGAP PEAAPGDCTR APPPSSESRP
PCHGGRQRLS DMSISTSSSD SLEFDRSMPL FGYEADTNSS LEDYEGESDQ ETMAPPIKSK
KKRSSSFVLP KLVKSQLQKV SGVFSSFMTP EKRMVRRIAE LSRDKCTYFG CLVQDYVSFL
QENKECHVSS TDMLQTIRQF MTQVKNYLSQ SSELDPPIES LIPEDQIDVV LEKAMHKCIL
KPLKGHVEAM LKDFHMADGS WKQLKENLQL VRQRNPQELG VFAPTPDFVD VEKIKVKFMT
MQKMYSPEKK VMLLLRVCKL IYTVMENNSG RMYGADDFLP VLTYVIAQCD MLELDTEIEY
MMELLDPSLL HGEGGYYLTS AYGALSLIKN FQEEQAARLL SSETRDTLRQ WHKRRTTNRT
IPSVDDFQNY LRVAFQEVNS GCTGKTLLVR PYITTEDVCQ ICAEKFKVGD PEEYSLFLFV
DETWQQLAED TYPQKIKAEL HSRPQPHIFH FVYKRIKNDP YGIIFQNGEE DLTTS


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