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Q13671

- RIN1_HUMAN

UniProt

Q13671 - RIN1_HUMAN

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
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 4 (17 Oct 2006)
      Previous versions | rss
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    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

    GO - Biological processi

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

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

    GO - Cellular componenti

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

    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 1PRO_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.7 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini69 – 16395SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini456 – 598143VPS9PROSITE-ProRule annotationAdd
    BLAST
    Domaini624 – 70683Ras-associatingPROSITE-ProRule annotationAdd
    BLAST

    Region

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

    Compositional bias

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

    Sequence similaritiesi

    Contains 1 Ras-associating domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation
    Contains 1 VPS9 domain.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti392 – 3954AGPE → DGQR(PubMed:1849280)Curated
    Sequence conflicti392 – 3954AGPE → DGQR(PubMed:7862125)Curated
    Sequence conflicti392 – 3954AGPE → DGQR(PubMed:9144171)Curated
    Sequence conflicti400 – 4001Q → E(PubMed:1849280)Curated
    Sequence conflicti400 – 4001Q → E(PubMed:7862125)Curated
    Sequence conflicti400 – 4001Q → E(PubMed:9144171)Curated
    Sequence conflicti423 – 4231L → V(PubMed:1849280)Curated
    Sequence conflicti423 – 4231L → V(PubMed:7862125)Curated
    Sequence conflicti423 – 4231L → V(PubMed:9144171)Curated
    Sequence conflicti503 – 5031L → V(PubMed:1849280)Curated
    Sequence conflicti503 – 5031L → V(PubMed:7862125)Curated
    Sequence conflicti503 – 5031L → V(PubMed:9144171)Curated
    Sequence conflicti534 – 5341A → S(PubMed:1849280)Curated
    Sequence conflicti534 – 5341A → S(PubMed:7862125)Curated
    Sequence conflicti534 – 5341A → S(PubMed:9144171)Curated
    Sequence conflicti538 – 5381E → G(PubMed:1849280)Curated
    Sequence conflicti538 – 5381E → G(PubMed:7862125)Curated
    Sequence conflicti538 – 5381E → G(PubMed:9144171)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei429 – 49062Missing in isoform RIN1-delta. 1 PublicationVSP_004377Add
    BLAST

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 133 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