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Identification
HMDB Protein ID HMDBP08556
Secondary Accession Numbers
  • 14270
Name Ras and Rab interactor 1
Synonyms
  1. Ras inhibitor JC99
  2. Ras interaction/interference protein 1
Gene Name RIN1
Protein Type Unknown
Biological Properties
General Function Involved in signal transduction
Specific 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
Pathways Not Available
Reactions Not Available
GO Classification
Function
binding
protein binding
Process
biological regulation
regulation of biological process
regulation of cellular process
signal transduction
Cellular Location
  1. Cytoplasm
  2. Cytoplasm
  3. Membrane
  4. cytoskeleton
Gene Properties
Chromosome Location Chromosome:1
Locus 11q13.2
SNPs RIN1
Gene Sequence
>2352 bp
ATGGAAAGCCCTGGAGAGTCAGGCGCGGGCTCTCCTGGAGCCCCCAGCCCGTCCAGCTTC
ACTACTGGGCACCTGGCGAGAGAAAAGCCAGCCCAGGACCCACTGTATGACGTGCCCAAT
GCCAGCGGCGGGCAGGCAGGCGGGCCGCAGCGGCCGGGGCGCGTTGTGAGCCTGCGGGAG
CGCCTGCTGCTCACCCGGCCCGTGTGGCTGCAGCTGCAAGCCAACGCAGCGGCCGCACTG
CACATGCTGAGGACCGAGCCCCCGGGGACGTTCCTCGTGCGGAAATCTAACACCCGCCAG
TGCCAGGCCCTGTGCATGCGGTTGCCTGAAGCCAGTGGCCCCTCCTTCGTCTCCAGCCAC
TACATCCTGGAGAGCCCTGGCGGCGTCTCCTTGGAGGGCTCGGAGCTCATGTTCCCAGAC
CTAGTCCAGCTCATCTGTGCCTACTGCCACACCCGGGACATCCTTCTCCTCCCGCTGCAG
CTCCCCAGAGCCATCCACCACGCAGCCACTCACAAAGAGCTGGAGGCCATCTCCCATCTG
GGCATTGAGTTCTGGAGCTCCTCCCTCAACATCAAGGCTCAGCGGGGCCCGGCTGGAGGC
CCAGTGTTGCCCCAGCTGAAGGCCCGGTCCCCTCAAGAGCTGGACCAGGGCACCGGAGCC
GCCTTGTGCTTCTTCAACCCCCTGTTCCCGGGGGACCTAGGGCCCACCAAGCGGGAGAAA
TTCAAGAGAAGCTTCAAAGTGCGCGTGTCCACAGAGACCTCCAGCCCCCTGTCTCCACCT
GCCGTGCCACCTCCCCCCGTCCCCGTGCTGCCAGGGGCAGTCCCCAGCCAGACAGAGCGG
CTGCCCCCTTGCCAGCTGCTACGGAGGGAGAGCTCAGTGGGGTACCGCGTGCCAGCAGGC
AGTGGCCCTAGCCTTCCGCCTATGCCCTCCCTCCAAGAGGTGGACTGCGGCTCCCCCAGC
AGCTCCGAGGAGGAGGGGGTGCCAGGGTCCCGGGGGAGCCCAGCGACCTCACCCCACCTG
GGCCGCCGACGACCTCTGCTTCGGTCCATGAGCGCCGCCTTCTGCTCCCTACTGGCACCG
GAGCGGCAGGTGGGCCGGGCTGCGGCAGCACTGATGCAGGACCGACACACAGCCGCGGGC
CAGCTGGTGCAGGACCTACTGACCCAGGTGCGGGCTGGGCCCGAGCCCCAGGAGCTGCAG
GGCATCCGTCAGGCGCTGAGCCGGGCCCGGGCCATGCTGAGTGCGGAGCTGGGCCCTGAG
AAGCTGCTGTCGCCTAAGAGGCTGGAACATGTCCTGGAGAAGTCATTGCATTGCTCTGTG
CTCAAGCCTCTCCGGCCCATCCTGGCAGCCCGCCTGCGGCGCCGGCTTGCCGCAGACGGC
TCCCTGGGCCGCCTAGCTGAGGGCCTCCGCCTGGCCCGGGCCCAGGGCCCCGGAGCCTTC
GGGTCCCACCTGAGCCTGCCCTCCCCAGTAGAGTTGGAGCAAGTGCGCCAGAAGCTGCTG
CAGCTGCTCCGCACCTACTCACCCAGCGCCCAGGTCAAGCGGCTCCTGCAGGCCTGCAAG
CTGCTCTACATGGCCCTGAGGACCCAGGAAGGGGAGGGCGCGGGTGCCGACGAGTTCCTG
CCTCTGCTGAGCCTCGTCTTGGCCCACTGTGACCTTCCTGAGCTGCTGCTGGAGGCCGAG
TACATGTCGGAGCTGCTGGAGCCCAGCCTGCTTACTGGAGAGGGTGGCTACTACCTGACC
AGCCTCTCTGCCAGCCTGGCCCTGCTGAGTGGCCTGGGTCAGGCCCACACCCTCCCACTG
AGCCCCGTGCAGGAGCTACGGCGCTCCCTCAGCCTCTGGGAGCAGCGCCGCCTGCCTGCC
ACCCACTGCTTCCAGCACCTCCTCCGAGTAGCCTATCAGGATCCCAGCAGTGGCTGCACC
TCCAAGACCCTGGCCGTGCCCCCAGAGGCCTCGATTGCCACCCTGAACCAGCTCTGTGCC
ACCAAGTTCCGAGTGACCCAGCCCAACACTTTTGGCCTCTTCCTGTACAAGGAGCAGGGC
TACCACCGCCTGCCCCCTGGGGCCCTGGCCCACAGGCTGCCCACCACTGGCTACCTCGTC
TACCGCCGGGCAGAGTGGCCTGAGACCCAGGGGGCTGTGACAGAGGAGGAGGGCAGTGGG
CAGTCAGAGGCAAGAAGCAGAGGGGAGGAGCAAGGGTGCCAGGGAGATGGGGATGCTGGG
GTCAAAGCCAGCCCCAGGGACATTCGGGAACAGTCTGAGACAACTGCTGAAGGGGGCCAG
GGTCAAGCCCAGGAAGGCCCTGCTCAGCCAGGGGAACCAGAGGCAGAGGGAAGCCGGGCA
GCAGAGGAGTAG
Protein Properties
Number of Residues 783
Molecular Weight 84098.0
Theoretical pI 8.08
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Ras and Rab interactor 1
MESPGESGAGSPGAPSPSSFTTGHLAREKPAQDPLYDVPNASGGQAGGPQRPGRVVSLRE
RLLLTRPVWLQLQANAAAALHMLRTEPPGTFLVRKSNTRQCQALCMRLPEASGPSFVSSH
YILESPGGVSLEGSELMFPDLVQLICAYCHTRDILLLPLQLPRAIHHAATHKELEAISHL
GIEFWSSSLNIKAQRGPAGGPVLPQLKARSPQELDQGTGAALCFFNPLFPGDLGPTKREK
FKRSFKVRVSTETSSPLSPPAVPPPPVPVLPGAVPSQTERLPPCQLLRRESSVGYRVPAG
SGPSLPPMPSLQEVDCGSPSSSEEEGVPGSRGSPATSPHLGRRRPLLRSMSAAFCSLLAP
ERQVGRAAAALMQDRHTAAGQLVQDLLTQVRAGPEPQELQGIRQALSRARAMLSAELGPE
KLLSPKRLEHVLEKSLHCSVLKPLRPILAARLRRRLAADGSLGRLAEGLRLARAQGPGAF
GSHLSLPSPVELEQVRQKLLQLLRTYSPSAQVKRLLQACKLLYMALRTQEGEGAGADEFL
PLLSLVLAHCDLPELLLEAEYMSELLEPSLLTGEGGYYLTSLSASLALLSGLGQAHTLPL
SPVQELRRSLSLWEQRRLPATHCFQHLLRVAYQDPSSGCTSKTLAVPPEASIATLNQLCA
TKFRVTQPNTFGLFLYKEQGYHRLPPGALAHRLPTTGYLVYRRAEWPETQGAVTEEEGSG
QSEARSRGEEQGCQGDGDAGVKASPRDIREQSETTAEGGQGQAQEGPAQPGEPEAEGSRA
AEE
GenBank ID Protein 15680148
UniProtKB/Swiss-Prot ID Q13671
UniProtKB/Swiss-Prot Entry Name RIN1_HUMAN
PDB IDs Not Available
GenBank Gene ID BC014417
GeneCard ID RIN1
GenAtlas ID RIN1
HGNC ID HGNC:18749
References
General References
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  2. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  3. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed:16964243 ]
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  5. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed:17053785 ]
  6. Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM: Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics. 2005 Sep;4(9):1240-50. Epub 2005 Jun 11. [PubMed:15951569 ]
  7. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. doi: 10.1021/pr900044c. [PubMed:19534553 ]
  8. Wang Y, Waldron RT, Dhaka A, Patel A, Riley MM, Rozengurt E, Colicelli J: The RAS effector RIN1 directly competes with RAF and is regulated by 14-3-3 proteins. Mol Cell Biol. 2002 Feb;22(3):916-26. [PubMed:11784866 ]
  9. Han L, Wong D, Dhaka A, Afar D, 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. 1997 May 13;94(10):4954-9. [PubMed:9144171 ]
  10. 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. 1991 Apr 1;88(7):2913-7. [PubMed:1849280 ]
  11. Tall GG, Barbieri MA, Stahl PD, Horazdovsky BF: Ras-activated endocytosis is mediated by the Rab5 guanine nucleotide exchange activity of RIN1. Dev Cell. 2001 Jul;1(1):73-82. [PubMed:11703925 ]
  12. Han L, Colicelli J: A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1. Mol Cell Biol. 1995 Mar;15(3):1318-23. [PubMed:7862125 ]
  13. Afar DE, Han L, McLaughlin J, Wong S, Dhaka A, Parmar K, Rosenberg N, Witte ON, Colicelli J: Regulation of the oncogenic activity of BCR-ABL by a tightly bound substrate protein RIN1. Immunity. 1997 Jun;6(6):773-82. [PubMed:9208849 ]