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Q13671 (RIN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras and Rab interactor 1
Alternative name(s):
Ras inhibitor JC99
Ras interaction/interference protein 1
Gene names
Name:RIN1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length783 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.3 Ref.5 Ref.8

Subunit structure

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. Ref.5 Ref.8

Subcellular location

Cytoplasm. Membrane. Cytoplasmcytoskeleton. Note: Some amount is membrane-associated. Ref.7

Tissue specificity

Expressed in all tissues examined with high levels in brain, placenta and pancreas. Ref.3

Post-translational modification

Phosphorylated on tyrosine residues by ABL1 and ABL2. Phosphorylation at Ser-351 by PRKD1 induces interaction with 14-3-3 proteins. Ref.3 Ref.5 Ref.7 Ref.8

Sequence similarities

Belongs to the RIN (Ras interaction/interference) family.

Contains 1 Ras-associating domain.

Contains 1 SH2 domain.

Contains 1 VPS9 domain.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   DomainSH2 domain
   Molecular functionGTPase activation
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processendocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

signal transduction

Traceable author statement Ref.3. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Traceable author statement Ref.2Ref.3. Source: ProtInc

   Molecular_functionGTPase activator activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform RIN1 (identifier: Q13671-1)

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.
Isoform RIN1-delta (identifier: Q13671-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 783783Ras and Rab interactor 1
PRO_0000191317

Regions

Domain69 – 16395SH2
Domain456 – 598143VPS9
Domain624 – 70683Ras-associating
Region294 – 727434Ras and 14-3-3 protein binding region
Compositional bias259 – 26810Pro-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11
Modified residue31Phosphoserine Ref.11
Modified residue161Phosphoserine Ref.11
Modified residue361Phosphotyrosine; by ABL1 and ABL2 Ref.8
Modified residue2101Phosphoserine Ref.10
Modified residue2581Phosphoserine Ref.10
Modified residue3331Phosphoserine Ref.9
Modified residue3371Phosphoserine Ref.9 Ref.10 Ref.11
Modified residue3511Phosphoserine; by PKD/PRKD1 Ref.7 Ref.10
Modified residue6091Phosphoserine Ref.10

Natural variations

Alternative sequence429 – 49062Missing in isoform RIN1-delta.
VSP_004377

Experimental info

Mutagenesis3511S → A: Abolishes phosphorylation by PKD and the interaction with 14-3-3 proteins. Ref.7
Sequence conflict392 – 3954AGPE → DGQR Ref.1
Sequence conflict392 – 3954AGPE → DGQR Ref.2
Sequence conflict392 – 3954AGPE → DGQR Ref.3
Sequence conflict4001Q → E Ref.1
Sequence conflict4001Q → E Ref.2
Sequence conflict4001Q → E Ref.3
Sequence conflict4231L → V Ref.1
Sequence conflict4231L → V Ref.2
Sequence conflict4231L → V Ref.3
Sequence conflict5031L → V Ref.1
Sequence conflict5031L → V Ref.2
Sequence conflict5031L → V Ref.3
Sequence conflict5341A → S Ref.1
Sequence conflict5341A → S Ref.2
Sequence conflict5341A → S Ref.3
Sequence conflict5381E → G Ref.1
Sequence conflict5381E → G Ref.2
Sequence conflict5381E → G Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform RIN1 [UniParc].

Last modified October 17, 2006. Version 4.
Checksum: 2B4DA70147CDDDFE

FASTA78384,099
        10         20         30         40         50         60 
MESPGESGAG SPGAPSPSSF TTGHLAREKP AQDPLYDVPN ASGGQAGGPQ RPGRVVSLRE 

        70         80         90        100        110        120 
RLLLTRPVWL QLQANAAAAL HMLRTEPPGT FLVRKSNTRQ CQALCMRLPE ASGPSFVSSH 

       130        140        150        160        170        180 
YILESPGGVS LEGSELMFPD LVQLICAYCH TRDILLLPLQ LPRAIHHAAT HKELEAISHL 

       190        200        210        220        230        240 
GIEFWSSSLN IKAQRGPAGG PVLPQLKARS PQELDQGTGA ALCFFNPLFP GDLGPTKREK 

       250        260        270        280        290        300 
FKRSFKVRVS TETSSPLSPP AVPPPPVPVL PGAVPSQTER LPPCQLLRRE SSVGYRVPAG 

       310        320        330        340        350        360 
SGPSLPPMPS LQEVDCGSPS SSEEEGVPGS RGSPATSPHL GRRRPLLRSM SAAFCSLLAP 

       370        380        390        400        410        420 
ERQVGRAAAA LMQDRHTAAG QLVQDLLTQV RAGPEPQELQ GIRQALSRAR AMLSAELGPE 

       430        440        450        460        470        480 
KLLSPKRLEH VLEKSLHCSV LKPLRPILAA RLRRRLAADG SLGRLAEGLR LARAQGPGAF 

       490        500        510        520        530        540 
GSHLSLPSPV ELEQVRQKLL QLLRTYSPSA QVKRLLQACK LLYMALRTQE GEGAGADEFL 

       550        560        570        580        590        600 
PLLSLVLAHC DLPELLLEAE YMSELLEPSL LTGEGGYYLT SLSASLALLS GLGQAHTLPL 

       610        620        630        640        650        660 
SPVQELRRSL SLWEQRRLPA THCFQHLLRV AYQDPSSGCT SKTLAVPPEA SIATLNQLCA 

       670        680        690        700        710        720 
TKFRVTQPNT FGLFLYKEQG YHRLPPGALA HRLPTTGYLV YRRAEWPETQ GAVTEEEGSG 

       730        740        750        760        770        780 
QSEARSRGEE QGCQGDGDAG VKASPRDIRE QSETTAEGGQ GQAQEGPAQP GEPEAEGSRA 


AEE 

« Hide

Isoform RIN1-delta [UniParc].

Checksum: AF59AA2FCA374ABE
Show »

FASTA72177,500

References

« Hide 'large scale' references
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L36463 mRNA. Translation: AAB67270.1.
BC014417 mRNA. Translation: AAH14417.1.
PIRA38637. A58613.
RefSeqNP_004283.2. NM_004292.2.
UniGeneHs.1030.

3D structure databases

ProteinModelPortalQ13671.
SMRQ13671. Positions 67-163, 508-601.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114972. 13 interactions.
DIPDIP-117N.
IntActQ13671. 15 interactions.
MINTMINT-1347026.
STRING9606.ENSP00000310406.

PTM databases

PhosphoSiteQ13671.

Polymorphism databases

DMDM116242760.

Proteomic databases

PaxDbQ13671.
PRIDEQ13671.

Protocols and materials databases

DNASU9610.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311320; ENSP00000310406; ENSG00000174791. [Q13671-1]
GeneID9610.
KEGGhsa:9610.
UCSCuc001ohn.1. human. [Q13671-1]

Organism-specific databases

CTD9610.
GeneCardsGC11M066099.
HGNCHGNC:18749. RIN1.
HPAHPA035491.
MIM605965. gene.
neXtProtNX_Q13671.
PharmGKBPA38671.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG242233.
HOGENOMHOG000154128.
HOVERGENHBG036105.
InParanoidQ13671.
KOK17638.
OMACATKFRV.
OrthoDBEOG7PZRWZ.
PhylomeDBQ13671.
TreeFamTF331067.

Enzyme and pathway databases

SignaLinkQ13671.

Gene expression databases

ArrayExpressQ13671.
BgeeQ13671.
CleanExHS_RIN1.
GenevestigatorQ13671.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR000159. Ras-assoc.
IPR000980. SH2.
IPR003123. VPS9.
IPR013995. VPS9_subgr.
[Graphical view]
PfamPF00788. RA. 1 hit.
PF02204. VPS9. 1 hit.
[Graphical view]
SMARTSM00314. RA. 1 hit.
SM00252. SH2. 1 hit.
SM00167. VPS9. 1 hit.
[Graphical view]
SUPFAMSSF55550. SSF55550. 1 hit.
PROSITEPS50200. RA. 1 hit.
PS50001. SH2. 1 hit.
PS51205. VPS9. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRIN1.
GenomeRNAi9610.
NextBio36051.
PROQ13671.
SOURCESearch...

Entry information

Entry nameRIN1_HUMAN
AccessionPrimary (citable) accession number: Q13671
Secondary accession number(s): O15010, Q00427, Q96CC8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 129 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM