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Q13671

- RIN1_HUMAN

UniProt

Q13671 - RIN1_HUMAN

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Protein
Ras and Rab interactor 1
Gene
RIN1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  1. GTPase activator activity Source: UniProtKB-KW
  2. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. endocytosis Source: UniProtKB-KW
  2. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Endocytosis

Enzyme and pathway databases

SignaLinkiQ13671.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras and Rab interactor 1
Alternative name(s):
Ras inhibitor JC99
Ras interaction/interference protein 1
Gene namesi
Name:RIN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:18749. RIN1.

Subcellular locationi

Cytoplasm. Membrane. Cytoplasmcytoskeleton
Note: Some amount is membrane-associated.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytoskeleton Source: UniProtKB-SubCell
  3. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi351 – 3511S → A: Abolishes phosphorylation by PKD and the interaction with 14-3-3 proteins. 1 Publication

Organism-specific databases

PharmGKBiPA38671.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 783783Ras and Rab interactor 1
PRO_0000191317Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei3 – 31Phosphoserine1 Publication
Modified residuei16 – 161Phosphoserine1 Publication
Modified residuei36 – 361Phosphotyrosine; by ABL1 and ABL21 Publication
Modified residuei210 – 2101Phosphoserine1 Publication
Modified residuei258 – 2581Phosphoserine1 Publication
Modified residuei333 – 3331Phosphoserine1 Publication
Modified residuei337 – 3371Phosphoserine3 Publications
Modified residuei351 – 3511Phosphoserine; by PKD/PRKD12 Publications
Modified residuei609 – 6091Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on tyrosine residues by ABL1 and ABL2. Phosphorylation at Ser-351 by PRKD1 induces interaction with 14-3-3 proteins.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13671.
PaxDbiQ13671.
PRIDEiQ13671.

PTM databases

PhosphoSiteiQ13671.

Expressioni

Tissue specificityi

Expressed in all tissues examined with high levels in brain, placenta and pancreas.1 Publication

Gene expression databases

ArrayExpressiQ13671.
BgeeiQ13671.
CleanExiHS_RIN1.
GenevestigatoriQ13671.

Organism-specific databases

HPAiHPA035491.

Interactioni

Subunit structurei

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-351.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005194EBI-366017,EBI-375543
ABL2P426844EBI-366017,EBI-1102694
EGFRP005333EBI-366017,EBI-297353
HRASP011125EBI-366017,EBI-350145
STAM2O758864EBI-366017,EBI-373258

Protein-protein interaction databases

BioGridi114972. 13 interactions.
DIPiDIP-117N.
IntActiQ13671. 15 interactions.
MINTiMINT-1347026.
STRINGi9606.ENSP00000310406.

Structurei

3D structure databases

ProteinModelPortaliQ13671.
SMRiQ13671. Positions 64-149, 508-601.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini69 – 16395SH2
Add
BLAST
Domaini456 – 598143VPS9
Add
BLAST
Domaini624 – 70683Ras-associating
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni294 – 727434Ras and 14-3-3 protein binding region
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi259 – 26810Pro-rich

Sequence similaritiesi

Contains 1 SH2 domain.
Contains 1 VPS9 domain.

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiNOG242233.
HOGENOMiHOG000154128.
HOVERGENiHBG036105.
InParanoidiQ13671.
KOiK17638.
OMAiCATKFRV.
OrthoDBiEOG7PZRWZ.
PhylomeDBiQ13671.
TreeFamiTF331067.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000159. Ras-assoc.
IPR000980. SH2.
IPR003123. VPS9.
IPR013995. VPS9_subgr.
[Graphical view]
PfamiPF00788. RA. 1 hit.
PF02204. VPS9. 1 hit.
[Graphical view]
SMARTiSM00314. RA. 1 hit.
SM00252. SH2. 1 hit.
SM00167. VPS9. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
PROSITEiPS50200. RA. 1 hit.
PS50001. SH2. 1 hit.
PS51205. VPS9. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform RIN1 (identifier: Q13671-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MESPGESGAG SPGAPSPSSF TTGHLAREKP AQDPLYDVPN ASGGQAGGPQ    50
RPGRVVSLRE RLLLTRPVWL QLQANAAAAL HMLRTEPPGT FLVRKSNTRQ 100
CQALCMRLPE ASGPSFVSSH YILESPGGVS LEGSELMFPD LVQLICAYCH 150
TRDILLLPLQ LPRAIHHAAT HKELEAISHL GIEFWSSSLN IKAQRGPAGG 200
PVLPQLKARS PQELDQGTGA ALCFFNPLFP GDLGPTKREK FKRSFKVRVS 250
TETSSPLSPP AVPPPPVPVL PGAVPSQTER LPPCQLLRRE SSVGYRVPAG 300
SGPSLPPMPS LQEVDCGSPS SSEEEGVPGS RGSPATSPHL GRRRPLLRSM 350
SAAFCSLLAP ERQVGRAAAA LMQDRHTAAG QLVQDLLTQV RAGPEPQELQ 400
GIRQALSRAR AMLSAELGPE KLLSPKRLEH VLEKSLHCSV LKPLRPILAA 450
RLRRRLAADG SLGRLAEGLR LARAQGPGAF GSHLSLPSPV ELEQVRQKLL 500
QLLRTYSPSA QVKRLLQACK LLYMALRTQE GEGAGADEFL PLLSLVLAHC 550
DLPELLLEAE YMSELLEPSL LTGEGGYYLT SLSASLALLS GLGQAHTLPL 600
SPVQELRRSL SLWEQRRLPA THCFQHLLRV AYQDPSSGCT SKTLAVPPEA 650
SIATLNQLCA TKFRVTQPNT FGLFLYKEQG YHRLPPGALA HRLPTTGYLV 700
YRRAEWPETQ GAVTEEEGSG QSEARSRGEE QGCQGDGDAG VKASPRDIRE 750
QSETTAEGGQ GQAQEGPAQP GEPEAEGSRA AEE 783
Length:783
Mass (Da):84,099
Last modified:October 17, 2006 - v4
Checksum:i2B4DA70147CDDDFE
GO
Isoform RIN1-delta (identifier: Q13671-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     429-490: Missing.

Note: Shows reduced ability to bind to Ras and 14-3-3 proteins.

Show »
Length:721
Mass (Da):77,500
Checksum:iAF59AA2FCA374ABE
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei429 – 49062Missing in isoform RIN1-delta.
VSP_004377Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti392 – 3954AGPE → DGQR1 Publication
Sequence conflicti392 – 3954AGPE → DGQR1 Publication
Sequence conflicti392 – 3954AGPE → DGQR1 Publication
Sequence conflicti400 – 4001Q → E1 Publication
Sequence conflicti400 – 4001Q → E1 Publication
Sequence conflicti400 – 4001Q → E1 Publication
Sequence conflicti423 – 4231L → V1 Publication
Sequence conflicti423 – 4231L → V1 Publication
Sequence conflicti423 – 4231L → V1 Publication
Sequence conflicti503 – 5031L → V1 Publication
Sequence conflicti503 – 5031L → V1 Publication
Sequence conflicti503 – 5031L → V1 Publication
Sequence conflicti534 – 5341A → S1 Publication
Sequence conflicti534 – 5341A → S1 Publication
Sequence conflicti534 – 5341A → S1 Publication
Sequence conflicti538 – 5381E → G1 Publication
Sequence conflicti538 – 5381E → G1 Publication
Sequence conflicti538 – 5381E → G1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L36463 mRNA. Translation: AAB67270.1.
BC014417 mRNA. Translation: AAH14417.1.
CCDSiCCDS31614.1. [Q13671-1]
PIRiA58613. A38637.
RefSeqiNP_004283.2. NM_004292.2. [Q13671-1]
UniGeneiHs.1030.

Genome annotation databases

EnsembliENST00000311320; ENSP00000310406; ENSG00000174791. [Q13671-1]
GeneIDi9610.
KEGGihsa:9610.
UCSCiuc001ohn.1. human. [Q13671-1]

Polymorphism databases

DMDMi116242760.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L36463 mRNA. Translation: AAB67270.1 .
BC014417 mRNA. Translation: AAH14417.1 .
CCDSi CCDS31614.1. [Q13671-1 ]
PIRi A58613. A38637.
RefSeqi NP_004283.2. NM_004292.2. [Q13671-1 ]
UniGenei Hs.1030.

3D structure databases

ProteinModelPortali Q13671.
SMRi Q13671. Positions 64-149, 508-601.
ModBasei Search...

Protein-protein interaction databases

BioGridi 114972. 13 interactions.
DIPi DIP-117N.
IntActi Q13671. 15 interactions.
MINTi MINT-1347026.
STRINGi 9606.ENSP00000310406.

PTM databases

PhosphoSitei Q13671.

Polymorphism databases

DMDMi 116242760.

Proteomic databases

MaxQBi Q13671.
PaxDbi Q13671.
PRIDEi Q13671.

Protocols and materials databases

DNASUi 9610.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311320 ; ENSP00000310406 ; ENSG00000174791 . [Q13671-1 ]
GeneIDi 9610.
KEGGi hsa:9610.
UCSCi uc001ohn.1. human. [Q13671-1 ]

Organism-specific databases

CTDi 9610.
GeneCardsi GC11M066099.
HGNCi HGNC:18749. RIN1.
HPAi HPA035491.
MIMi 605965. gene.
neXtProti NX_Q13671.
PharmGKBi PA38671.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG242233.
HOGENOMi HOG000154128.
HOVERGENi HBG036105.
InParanoidi Q13671.
KOi K17638.
OMAi CATKFRV.
OrthoDBi EOG7PZRWZ.
PhylomeDBi Q13671.
TreeFami TF331067.

Enzyme and pathway databases

SignaLinki Q13671.

Miscellaneous databases

GeneWikii RIN1.
GenomeRNAii 9610.
NextBioi 36051.
PROi Q13671.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13671.
Bgeei Q13671.
CleanExi HS_RIN1.
Genevestigatori Q13671.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR000159. Ras-assoc.
IPR000980. SH2.
IPR003123. VPS9.
IPR013995. VPS9_subgr.
[Graphical view ]
Pfami PF00788. RA. 1 hit.
PF02204. VPS9. 1 hit.
[Graphical view ]
SMARTi SM00314. RA. 1 hit.
SM00252. SH2. 1 hit.
SM00167. VPS9. 1 hit.
[Graphical view ]
SUPFAMi SSF55550. SSF55550. 1 hit.
PROSITEi PS50200. RA. 1 hit.
PS50001. SH2. 1 hit.
PS51205. VPS9. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of three mammalian cDNAs that interfere with RAS function in Saccharomyces cerevisiae."
    Colicelli J., Nicolette C., Birchmeier C., Rodgers L., Riggs M., Wigler M.
    Proc. Natl. Acad. Sci. U.S.A. 88:2913-2917(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Glial cell.
  2. "A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1."
    Han L., Colicelli J.
    Mol. Cell. Biol. 15:1318-1323(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
  3. "Protein binding and signaling properties of RIN1 suggest a unique effector function."
    Han L., Wong D., Dhaka A., Afar D.E.H., White M., Xie W., Herschman H., Witte O., Colicelli J.
    Proc. Natl. Acad. Sci. U.S.A. 94:4954-4959(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS RIN1 AND RIN1-DELTA), SEQUENCE REVISION, FUNCTION, DOMAINS, PHOSPHORYLATION, TISSUE SPECIFICITY.
    Tissue: Glioblastoma.
  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].
    Tissue: Lung.
  5. "Regulation of the oncogenic activity of BCR-ABL by a tightly bound substrate protein RIN1."
    Afar D.E.H., Han L., McLaughlin J., Wong S., Dhaka A., Parmar K., Rosenberg N., Witte O.N., Colicelli J.
    Immunity 6:773-782(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ABL1, PHOSPHORYLATION BY ABL1.
  6. "Ras-activated endocytosis is mediated by the Rab5 guanine nucleotide exchange activity of RIN1."
    Tall G.G., Barbieri M.A., Stahl P.D., Horazdovsky B.F.
    Dev. Cell 1:73-82(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GEF ACTIVITY.
  7. "The RAS effector RIN1 directly competes with RAF and is regulated by 14-3-3 proteins."
    Wang Y., Waldron R.T., Dhaka A., Patel A., Riley M.M., Rozengurt E., Colicelli J.
    Mol. Cell. Biol. 22:916-926(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-351, MUTAGENESIS OF SER-351.
  8. "RIN1 is an ABL tyrosine kinase activator and a regulator of epithelial-cell adhesion and migration."
    Hu H., Bliss J.M., Wang Y., Colicelli J.
    Curr. Biol. 15:815-823(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ABL1 AND ABL2, PHOSPHORYLATION AT TYR-36.
  9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 AND SER-337, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; SER-258; SER-337; SER-351 AND SER-609, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-16 AND SER-337, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiRIN1_HUMAN
AccessioniPrimary (citable) accession number: Q13671
Secondary accession number(s): O15010, Q00427, Q96CC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 132 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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