Rin1

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 (By similarity).By similarity

GO - Molecular functionⁱ

GTPase activator activity Source: UniProtKB-KW

Complete GO annotation...

GO - Biological processⁱ

endocytosis Source: UniProtKB-KW
signal transduction Source: InterPro

Complete GO annotation...

Keywordsⁱ

Molecular function	GTPase activation
Biological process	Endocytosis

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Ras and Rab interactor 1 Alternative name(s): Ras interaction/interference protein 1
Gene namesⁱ	Name:Rin1
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Unplaced

Organism-specific databases

Rat genome database More...RGDⁱ	620006. Rin1.

RGDⁱ

620006. Rin1.

Subcellular locationⁱ

Cytoplasm By similarity
Membrane By similarity
Cytoplasm › cytoskeleton By similarity

Note:

Some amount is membrane-associated.By similarity

GO - Cellular componentⁱ

cytoplasm Source: UniProtKB-SubCell
cytoskeleton Source: UniProtKB-SubCell
membrane Source: UniProtKB-SubCell

Complete GO annotation...

Keywords - Cellular componentⁱ

Cytoplasm, Cytoskeleton, Membrane

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000191319	1 – 774	Ras and Rab interactor 1Add BLAST		774

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	1	N-acetylmethionineBy similarity	1
Modified residueⁱ	16	PhosphoserineBy similarity	1
Modified residueⁱ	35	Phosphotyrosine; by ABL1 and ABL2By similarity	1
Modified residueⁱ	209	PhosphoserineBy similarity	1
Modified residueⁱ	257	PhosphoserineBy similarity	1
Modified residueⁱ	330	PhosphoserineBy similarity	1
Modified residueⁱ	334	PhosphoserineBy similarity	1
Modified residueⁱ	351	Phosphoserine; by PKD/PRKD1By similarity	1
Modified residueⁱ	609	PhosphoserineBy similarity	1
Modified residueⁱ	692	Omega-N-methylarginineBy similarity	1

Post-translational modificationⁱ

Phosphorylated on tyrosine residues by ABL1 and ABL2. Phosphorylation at Ser-351 by PRKD1 induces interaction with 14-3-3 proteins (By similarity).By similarity

Keywords - PTMⁱ

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbⁱ	P97680.
PRIDEⁱ	P97680.

PTM databases

iPTMnetⁱ	P97680.
PhosphoSitePlusⁱ	P97680.

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 (By similarity).By similarity

Protein-protein interaction databases

IntActⁱ	P97680. 1 interactor.
STRINGⁱ	10116.ENSRNOP00000066064.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P97680.
SMRⁱ	P97680.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	68 – 162	SH2PROSITE-ProRule annotationAdd BLAST	95
Domainⁱ	456 – 598	VPS9PROSITE-ProRule annotationAdd BLAST	143
Domainⁱ	624 – 706	Ras-associatingPROSITE-ProRule annotationAdd BLAST	83

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	258 – 267	Pro-rich		10
Compositional biasⁱ	413 – 612	Leu-richAdd BLAST		200

Sequence similaritiesⁱ

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

Keywords - Domainⁱ

SH2 domain

Phylogenomic databases

eggNOGⁱ	KOG2320. Eukaryota. ENOG410ZZW5. LUCA.
HOGENOMⁱ	HOG000154128.
HOVERGENⁱ	HBG036105.
InParanoidⁱ	P97680.
KEGG Orthology (KO) More...KOⁱ	K17638.
PhylomeDBⁱ	P97680.

Family and domain databases

Gene3Dⁱ	3.30.505.10. 1 hit.
InterProⁱ	View protein in InterPro IPR000159. RA_dom. IPR000980. SH2. IPR003123. VPS9.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02204. VPS9. 1 hit.
SMARTⁱ	View protein in SMART SM00314. RA. 1 hit. SM00252. SH2. 1 hit. SM00167. VPS9. 1 hit.
SUPFAMⁱ	SSF55550. SSF55550. 1 hit.
PROSITEⁱ	View protein in PROSITE PS50200. RA. 1 hit. PS50001. SH2. 1 hit. PS51205. VPS9. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

P97680-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MEDPGETEAH PLGATSLNFV PGYQQEEKPS PDPLYDTPDA RGVQAGGSQQ 
        60         70         80         90        100
PARTVSLRER LLITRPVWLQ LRANAAAALH VLRTEPPGTF LVRKSNTRQC 
       110        120        130        140        150
QTLCVRLPEA SGPSFVSSHY LQESPGGISL EGSELTFPDL VQLICAYCHT 
       160        170        180        190        200
RDILLLPLPL PRAIHQAATH KELEAISHLG MEFWSSSLNT KNQQRPSEAP 
       210        220        230        240        250
QIPRLKARSP QELDQGTGAA LCFFNPLFPG DLGPTKREKF KRSFKVRVST 
       260        270        280        290        300
ETSSPLSPPA VPPPPVPVLP GTSSSQTERL PPRQLLQRES SVGYRVPGSA 
       310        320        330        340        350
SGPSLPPLPS LQEVDCCSPS SSEEEGSSGS PTTSPRLSRP RHRRPLLRSM 
       360        370        380        390        400
SSAFCSLLAP ERQVGRAATM LMQNRYTAVG QLVQDLLTQV RVGPESRELQ 
       410        420        430        440        450
GIRQALSRAR AMLSAELGPE KLLPPERLEL VLEKSLHRSV LKPLRPILAA 
       460        470        480        490        500
RLRRRLSTDG SLGRLAEGFR LARTQGPGAF GSHLNLSSPV EIEPVRQKLL 
       510        520        530        540        550
QLLRAYSPSA QIKWLLQACK LLYTALKTQA GENAGADEFL PLLSLVLAQC 
       560        570        580        590        600
DLPDLLLEAE YMSELLEPTL LTGEGGYYLT SLSASLALLS GLSQAHALPL 
       610        620        630        640        650
SPAQELQRSL ALWEQRRLPA THNFQHLLRV AYQDPSTGCT SKTLAVPPGS 
       660        670        680        690        700
SIATLSQLCA TKFRVTQPDA FGLFLYKDQG YHRLPPEALV HRLPTTGYLI 
       710        720        730        740        750
YRRAERPETQ RAATEKTKTG NERPERGAWE EEKGGLNGEG KSEIAVDQEG 
       760        770 
KDQARGGHMQ LEEQKAEGCP ALEE

Length:774

Mass (Da):84,727

Last modified:February 1, 2003 - v2

Checksum:ⁱ33900CEEDBF8E658

GO

Sequence cautionⁱ

The sequence AAB58256 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U80076 mRNA. Translation: AAB58256.1. Different initiation.
NCBI Reference Sequences More...RefSeqⁱ	NP_620607.1. NM_139038.1.
UniGeneⁱ	Rn.16006.

Genome annotation databases

GeneIDⁱ	207119.
KEGGⁱ	rno:207119.
UCSC genome browser More...UCSCⁱ	RGD:620006. rat.

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U80076 mRNA. Translation: AAB58256.1. Different initiation.
NCBI Reference Sequences More...RefSeqⁱ	NP_620607.1. NM_139038.1.
UniGeneⁱ	Rn.16006.

3D structure databases

ProteinModelPortalⁱ	P97680.
SMRⁱ	P97680.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

IntActⁱ	P97680. 1 interactor.
STRINGⁱ	10116.ENSRNOP00000066064.

PTM databases

iPTMnetⁱ	P97680.
PhosphoSitePlusⁱ	P97680.

Proteomic databases

PaxDbⁱ	P97680.
PRIDEⁱ	P97680.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	207119.
KEGGⁱ	rno:207119.
UCSC genome browser More...UCSCⁱ	RGD:620006. rat.

Organism-specific databases

CTDⁱ	9610.
Rat genome database More...RGDⁱ	620006. Rin1.

Phylogenomic databases

eggNOGⁱ	KOG2320. Eukaryota. ENOG410ZZW5. LUCA.
HOGENOMⁱ	HOG000154128.
HOVERGENⁱ	HBG036105.
InParanoidⁱ	P97680.
KEGG Orthology (KO) More...KOⁱ	K17638.
PhylomeDBⁱ	P97680.

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P97680.

PROⁱ

PR:P97680.

Family and domain databases

Gene3Dⁱ	3.30.505.10. 1 hit.
InterProⁱ	View protein in InterPro IPR000159. RA_dom. IPR000980. SH2. IPR003123. VPS9.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02204. VPS9. 1 hit.
SMARTⁱ	View protein in SMART SM00314. RA. 1 hit. SM00252. SH2. 1 hit. SM00167. VPS9. 1 hit.
SUPFAMⁱ	SSF55550. SSF55550. 1 hit.
PROSITEⁱ	View protein in PROSITE PS50200. RA. 1 hit. PS50001. SH2. 1 hit. PS51205. VPS9. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RIN1_RAT
Accessionⁱ	P97680Primary (citable) accession number: P97680
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
	Last sequence update:	February 1, 2003
	Last modified:	May 10, 2017
	This is version 114 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P97680 (RIN1_RAT)

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Ras and Rab interactor 1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Compositional bias

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ