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Protein

Rab11 family-interacting protein 2

Gene

RAB11FIP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

A Rab11 effector binding preferentially phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA) and acting in the regulation of the transport of vesicles from the endosomal recycling compartment (ERC) to the plasma membrane. Involved in insulin granule exocytosis. Also involved in receptor-mediated endocytosis and membrane trafficking of recycling endosomes, probably originating from clathrin-coated vesicles. Required in a complex with MYO5B and RAB11 for the transport of NPC1L1 to the plasma membrane. Also acts as a regulator of cell polarity.5 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • Rab GTPase binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-HSA-432040. Vasopressin regulates renal water homeostasis via Aquaporins.

Names & Taxonomyi

Protein namesi
Recommended name:
Rab11 family-interacting protein 2
Short name:
Rab11-FIP2
Alternative name(s):
NRip11
Gene namesi
Name:RAB11FIP2
Synonyms:KIAA0941
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:29152. RAB11FIP2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi223 – 2231S → A: No effect. 1 Publication
Mutagenesisi224 – 2241S → A: No effect. 1 Publication
Mutagenesisi227 – 2271S → A: Abolishes phosphorylation by MARK2 and induces defects in the reestablishment of junctional complexes. 1 Publication
Mutagenesisi229 – 2291S → A: No effect. 1 Publication
Mutagenesisi406 – 4083NPF → AAA: Severe reduction of the interaction with REPS1 and AP2A1. No effects on its subcellular location. Modifies the endocytosis activity. 1 Publication
Mutagenesisi480 – 4823YID → AAA: Abolishes the interaction with REPS1 and AP2A1. Modifies its subcellular location and the endocytosis activity. Enhances homooligomerization. 1 Publication
Mutagenesisi480 – 4801Y → F: No effect on the interaction with RAB11A. Abolishes the vesicular localization. 1 Publication
Mutagenesisi481 – 4811I → E: Abolishes the interaction with RAB11A and the vesicular localization. 1 Publication

Organism-specific databases

PharmGKBiPA134961225.

Polymorphism and mutation databases

BioMutaiRAB11FIP2.
DMDMi67472131.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 512512Rab11 family-interacting protein 2PRO_0000097306Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei227 – 2271Phosphoserine; by MARK21 Publication

Post-translational modificationi

Phosphorylation at Ser-227 by MARK2 regulates epithelial cell polarity.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ7L804.
MaxQBiQ7L804.
PaxDbiQ7L804.
PRIDEiQ7L804.

PTM databases

iPTMnetiQ7L804.
PhosphoSiteiQ7L804.

Expressioni

Gene expression databases

BgeeiQ7L804.
CleanExiHS_RAB11FIP2.
GenevisibleiQ7L804. HS.

Organism-specific databases

HPAiHPA037726.

Interactioni

Subunit structurei

Homooligomerizes in a Rab11-independent manner. Forms a heterooligomeric complex with RAB11FIP4. Interacts with AP2A1, MYO5B, RAB25 and REPS1. Interacts with RAB11A and RAB11B (activated GTP-bound form). Interacts with NPC1L1. Interacts (via NPF motifs) with EHD1 and EHD3.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RAB11AP624913EBI-1049676,EBI-745098

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • Rab GTPase binding Source: GO_Central

Protein-protein interaction databases

BioGridi116514. 39 interactions.
DIPiDIP-29139N.
IntActiQ7L804. 24 interactions.
MINTiMINT-1682199.
STRINGi9606.ENSP00000347839.

Structurei

Secondary structure

1
512
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi453 – 49139Combined sources
Helixi493 – 4964Combined sources
Beta strandi497 – 4993Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GZDX-ray2.44C/D410-512[»]
2GZHX-ray2.47B410-512[»]
2K6SNMR-A/B450-489[»]
3TSOX-ray1.80C/D440-512[»]
4C4PX-ray2.00B410-512[»]
ProteinModelPortaliQ7L804.
SMRiQ7L804. Positions 14-124, 449-502.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7L804.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 102102C2PROSITE-ProRule annotationAdd
BLAST
Domaini437 – 49963FIP-RBDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni15 – 10288Necessary for its cellular translocation to the plasma membraneAdd
BLAST
Regioni465 – 51248Necessary for the interaction with AP2A1, RAB11A, subcellular location, endocytosis activity and homooligomerizationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi323 – 3253NPF 1
Motifi406 – 4083NPF 2
Motifi440 – 4423NPF 3

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 FIP-RBD domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IEZZ. Eukaryota.
ENOG410Z26C. LUCA.
GeneTreeiENSGT00530000063203.
HOGENOMiHOG000234700.
HOVERGENiHBG054920.
InParanoidiQ7L804.
KOiK12484.
OMAiSFHMNPT.
OrthoDBiEOG7WQ7SB.
PhylomeDBiQ7L804.
TreeFamiTF326172.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR019018. Rab-bd_FIP-RBD.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF09457. RBD-FIP. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS51511. FIP_RBD. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q7L804-1) [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

        10         20         30         40         50
MMLSEQAQKW FPTHVQVTVL QAKDLKPKGK SGTNDTYTII QLGKEKYSTS
60 70 80 90 100
VAEKTLEPVW KEEASFELPG LLIQGSPEKY ILFLIVMHRS LVGLDKFLGQ
110 120 130 140 150
VAINLNDIFE DKQRRKTEWF RLESKQGKRI KNRGEIKVNI QFMRNNMTAS
160 170 180 190 200
MFDLSMKDKT RSPFAKLKDK MKGRKNDGTF SDTSSAIIPS THMPDANSEF
210 220 230 240 250
SSGEIQMKSK PKKPFLLGPQ RLSSAHSMSD LSGSHMSSEK LKAGTIGQTH
260 270 280 290 300
LLGHQLDSFG TVPESGSLKS PHRRTLSFDT SKMNQPDSIV DEGELCFGRQ
310 320 330 340 350
NDPFTNVTAS LPQKFATLPR KKNPFEESSE TWDSSMNLFS KPIEIRKENK
360 370 380 390 400
REKREKVSLF ERVTGKKDSR RSDKLNNGGS DSPCDLKSPN AFSENRQDYF
410 420 430 440 450
DYESTNPFTA KFRASNIMPS SSFHMSPTSN EDLRKIPDSN PFDATAGYRS
460 470 480 490 500
LTYEEVLQEL VKHKELLRRK DTHIRELEDY IDNLLVRVME ETPSILRVPY
510
EPSRKAGKFS NS
Length:512
Mass (Da):58,279
Last modified:July 5, 2004 - v1
Checksum:i9EC2DAB0A585BCD3
GO
Isoform 2 (identifier: Q7L804-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     422-422: S → RNTLLTPAVAEWRGSLRWAEL

Show »
Length:532
Mass (Da):60,614
Checksum:i24B23A356BCCC409
GO

Sequence cautioni

The sequence BAA76785.2 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti152 – 1521F → V.
Corresponds to variant rs34028100 [ dbSNP | Ensembl ].
VAR_051316

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei422 – 4221S → RNTLLTPAVAEWRGSLRWAE L in isoform 2. 1 PublicationVSP_056649

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ013303 mRNA. Translation: AAY67796.1.
AY037299 mRNA. Translation: AAK68635.1.
AB023158 mRNA. Translation: BAA76785.2. Different initiation.
AC022395 Genomic DNA. No translation available.
CH471066 Genomic DNA. Translation: EAW49423.1.
BC075073 mRNA. Translation: AAH75073.1.
BC075074 mRNA. Translation: AAH75074.1.
CCDSiCCDS7602.1. [Q7L804-1]
RefSeqiNP_055719.1. NM_014904.2. [Q7L804-1]
XP_005269686.1. XM_005269629.2. [Q7L804-2]
UniGeneiHs.173656.

Genome annotation databases

EnsembliENST00000355624; ENSP00000347839; ENSG00000107560. [Q7L804-1]
ENST00000369199; ENSP00000358200; ENSG00000107560. [Q7L804-2]
GeneIDi22841.
KEGGihsa:22841.
UCSCiuc001ldj.2. human. [Q7L804-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ013303 mRNA. Translation: AAY67796.1.
AY037299 mRNA. Translation: AAK68635.1.
AB023158 mRNA. Translation: BAA76785.2. Different initiation.
AC022395 Genomic DNA. No translation available.
CH471066 Genomic DNA. Translation: EAW49423.1.
BC075073 mRNA. Translation: AAH75073.1.
BC075074 mRNA. Translation: AAH75074.1.
CCDSiCCDS7602.1. [Q7L804-1]
RefSeqiNP_055719.1. NM_014904.2. [Q7L804-1]
XP_005269686.1. XM_005269629.2. [Q7L804-2]
UniGeneiHs.173656.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GZDX-ray2.44C/D410-512[»]
2GZHX-ray2.47B410-512[»]
2K6SNMR-A/B450-489[»]
3TSOX-ray1.80C/D440-512[»]
4C4PX-ray2.00B410-512[»]
ProteinModelPortaliQ7L804.
SMRiQ7L804. Positions 14-124, 449-502.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116514. 39 interactions.
DIPiDIP-29139N.
IntActiQ7L804. 24 interactions.
MINTiMINT-1682199.
STRINGi9606.ENSP00000347839.

PTM databases

iPTMnetiQ7L804.
PhosphoSiteiQ7L804.

Polymorphism and mutation databases

BioMutaiRAB11FIP2.
DMDMi67472131.

Proteomic databases

EPDiQ7L804.
MaxQBiQ7L804.
PaxDbiQ7L804.
PRIDEiQ7L804.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355624; ENSP00000347839; ENSG00000107560. [Q7L804-1]
ENST00000369199; ENSP00000358200; ENSG00000107560. [Q7L804-2]
GeneIDi22841.
KEGGihsa:22841.
UCSCiuc001ldj.2. human. [Q7L804-1]

Organism-specific databases

CTDi22841.
GeneCardsiRAB11FIP2.
HGNCiHGNC:29152. RAB11FIP2.
HPAiHPA037726.
MIMi608599. gene.
neXtProtiNX_Q7L804.
PharmGKBiPA134961225.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEZZ. Eukaryota.
ENOG410Z26C. LUCA.
GeneTreeiENSGT00530000063203.
HOGENOMiHOG000234700.
HOVERGENiHBG054920.
InParanoidiQ7L804.
KOiK12484.
OMAiSFHMNPT.
OrthoDBiEOG7WQ7SB.
PhylomeDBiQ7L804.
TreeFamiTF326172.

Enzyme and pathway databases

ReactomeiR-HSA-432040. Vasopressin regulates renal water homeostasis via Aquaporins.

Miscellaneous databases

ChiTaRSiRAB11FIP2. human.
EvolutionaryTraceiQ7L804.
GeneWikiiRAB11FIP2.
GenomeRNAii22841.
NextBioi43289.
PROiQ7L804.
SOURCEiSearch...

Gene expression databases

BgeeiQ7L804.
CleanExiHS_RAB11FIP2.
GenevisibleiQ7L804. HS.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR019018. Rab-bd_FIP-RBD.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF09457. RBD-FIP. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS51511. FIP_RBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Interactions between EHD proteins and Rab11-FIP2: a role for EHD3 in early endosomal transport."
    Naslavsky N., Rahajeng J., Sharma M., Jovic M., Caplan S.
    Mol. Biol. Cell 17:163-177(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH EHD1 AND EHD3.
  2. "Rip11 and nRip11 are Rab11/25 interacting proteins."
    Prekeris R., Davies J.M., Scheller R.H.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Brain.
  7. Cited for: INTERACTION WITH MYO5B; RAB11A; RAB11B AND RAB25, SUBCELLULAR LOCATION.
  8. "The novel Rab11-FIP/Rip/RCP family of proteins displays extensive homo- and hetero-interacting abilities."
    Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W.
    Biochem. Biophys. Res. Commun. 292:909-915(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  9. "Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its overexpression condenses the Rab11 positive compartment in HeLa cells."
    Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W.
    Biochem. Biophys. Res. Commun. 299:770-779(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  10. "Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain."
    Lindsay A.J., McCaffrey M.W.
    J. Biol. Chem. 277:27193-27199(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH RAB11A, SUBCELLULAR LOCATION.
  11. "Rab11-FIP2, an adaptor protein connecting cellular components involved in internalization and recycling of epidermal growth factor receptors."
    Cullis D.N., Philip B., Baleja J.D., Feig L.A.
    J. Biol. Chem. 277:49158-49166(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RECEPTOR-MEDIATED ENDOCYTOSIS, SUBUNIT, INTERACTION WITH REPS1 AND AP2A1, MUTAGENESIS OF 406-ASN--PHE-408 AND 480-TYR--ASP-482, NPF MOTIF, SUBCELLULAR LOCATION.
  12. "Molecular characterization of Rab11 interactions with members of the family of Rab11-interacting proteins."
    Junutula J.R., Schonteich E., Wilson G.M., Peden A.A., Scheller R.H., Prekeris R.
    J. Biol. Chem. 279:33430-33437(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH GTP-BOUND RAB11A AND GTP-BOUND RAB11B.
  13. "The C2 domains of the class I Rab11 family of interacting proteins target recycling vesicles to the plasma membrane."
    Lindsay A.J., McCaffrey M.W.
    J. Cell Sci. 117:4365-4375(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ENDOSOME TRAFFICKING, INTERACTION WITH PTDINSP3 AND PA, SUBCELLULAR LOCATION.
  14. "MARK2/EMK1/Par-1Balpha phosphorylation of Rab11-family interacting protein 2 is necessary for the timely establishment of polarity in Madin-Darby canine kidney cells."
    Ducharme N.A., Hales C.M., Lapierre L.A., Ham A.J., Oztan A., Apodaca G., Goldenring J.R.
    Mol. Biol. Cell 17:3625-3637(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-227, MUTAGENESIS OF SER-223; SER-224; SER-227 AND SER-229.
  15. "Requirement of myosin Vb.Rab11a.Rab11-FIP2 complex in cholesterol-regulated translocation of NPC1L1 to the cell surface."
    Chu B.-B., Ge L., Xie C., Zhao Y., Miao H.-H., Wang J., Li B.-L., Song B.-L.
    J. Biol. Chem. 284:22481-22490(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NPC1L1.
  16. "Crystal structure of rab11 in complex with rab11 family interacting protein 2."
    Jagoe W.N., Lindsay A.J., Read R.J., McCoy A.J., McCaffrey M.W., Khan A.R.
    Structure 14:1273-1283(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 410-512, INTERACTION WITH RAB11A, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-480 AND ILE-481.

Entry informationi

Entry nameiRFIP2_HUMAN
AccessioniPrimary (citable) accession number: Q7L804
Secondary accession number(s): A6NEI4, Q3I768, Q9Y2F0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: July 5, 2004
Last modified: May 11, 2016
This is version 131 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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.