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Protein

Rab11 family-interacting protein 5

Gene

RAB11FIP5

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

Functioni

Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis.2 Publications

GO - Molecular functioni

  • gamma-tubulin binding Source: UniProtKB
  • Rab GTPase binding Source: GO_Central

GO - Biological processi

  • cellular response to acidic pH Source: UniProtKB
  • insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  • negative regulation of adiponectin secretion Source: CACAO
  • regulated secretory pathway Source: UniProtKB
  • regulation of protein localization to cell surface Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Rab11 family-interacting protein 5
Short name:
Rab11-FIP5
Alternative name(s):
Gamma-SNAP-associated factor 1
Short name:
Gaf-1
Phosphoprotein pp75
Rab11-interacting protein Rip11
Gene namesi
Name:RAB11FIP5
Synonyms:GAF1, KIAA0857, RIP11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:24845. RAB11FIP5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endosome, Golgi apparatus, Membrane, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134971129.

Polymorphism and mutation databases

BioMutaiRAB11FIP5.
DMDMi34223002.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 653653Rab11 family-interacting protein 5PRO_0000097307Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei176 – 1761Phosphoserine1 Publication
Modified residuei307 – 3071Phosphoserine2 Publications
Modified residuei357 – 3571PhosphoserineBy similarity
Modified residuei494 – 4941Phosphoserine1 Publication
Modified residuei538 – 5381Phosphoserine2 Publications
Modified residuei547 – 5471PhosphoserineBy similarity
Modified residuei553 – 5531PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on serine and threonine residues. Phosphorylation at Ser-357 is PKA-dependent.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BXF6.
PaxDbiQ9BXF6.
PRIDEiQ9BXF6.

PTM databases

PhosphoSiteiQ9BXF6.

Expressioni

Tissue specificityi

Detected at low levels in heart, brain, placenta, lung, liver, adipocytes, kidney, spleen, skeletal muscle and pancreas.2 Publications

Gene expression databases

BgeeiQ9BXF6.
CleanExiHS_RAB11FIP5.
GenevisibleiQ9BXF6. HS.

Organism-specific databases

HPAiHPA036406.
HPA036407.

Interactioni

Subunit structurei

Forms a heterooligomeric complex with RAB11FIP4. Binds NAPG and TROVE2. Binds RAB11A that has been activated by GTP binding.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
KIF3AQ9Y4962EBI-1387068,EBI-1104844
SNX18Q96RF03EBI-1387068,EBI-298169

Protein-protein interaction databases

BioGridi117518. 19 interactions.
IntActiQ9BXF6. 14 interactions.
STRINGi9606.ENSP00000258098.

Structurei

3D structure databases

ProteinModelPortaliQ9BXF6.
SMRiQ9BXF6. Positions 600-651.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 128123C2PROSITE-ProRule annotationAdd
BLAST
Domaini586 – 64863FIP-RBDPROSITE-ProRule annotationAdd
BLAST

Domaini

Binds to vesicles enriched in neutral phospholipids via its C2 domain. The interaction is favored by Mg2+ rather than Ca2+.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG84049.
GeneTreeiENSGT00530000063203.
HOGENOMiHOG000234700.
HOVERGENiHBG079127.
InParanoidiQ9BXF6.
KOiK12484.
OMAiVEKTHGC.
OrthoDBiEOG7WQ7SB.
PhylomeDBiQ9BXF6.
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]

Sequencei

Sequence statusi: Complete.

Q9BXF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALVRGAEPA AGPSRWLPTH VQVTVLRARG LRGKSSGAGS TSDAYTVIQV
60 70 80 90 100
GREKYSTSVV EKTHGCPEWR EECSFELPPG ALDGLLRAQE ADAGPAPWAA
110 120 130 140 150
SSAAACELVL TTMHRSLIGV DKFLGQATVA LDEVFGAGRA QHTQWYKLHS
160 170 180 190 200
KPGKKEKERG EIEVTIQFTR NNLSASMFDL SMKDKPRSPF SKIRDKMKGK
210 220 230 240 250
KKYDLESASA ILPSSAIEDP DLGSLGKMGK AKGFFLRNKL RKSSLTQSNT
260 270 280 290 300
SLGSDSTLSS ASGSLAYQGP GAELLTRSPS RSSWLSTEGG RDSAQSPKLF
310 320 330 340 350
THKRTYSDEA NQMRVAPPRA LLDLQGHLDA ASRSSLCVNG SHIYNEEPQG
360 370 380 390 400
PVRHRSSISG SLPSSGSLQA VSSRFSEEGP RSTDDTWPRG SRSNSSSEAV
410 420 430 440 450
LGQEELSAQA KVLAPGASHP GEEEGARLPE GKPVQVATPI VASSEAVAEK
460 470 480 490 500
EGARKEERKP RMGLFHHHHQ GLSRSELGRR SSLGEKGGPI LGASPHHSSS
510 520 530 540 550
GEEKAKSSWF GLREAKDPTQ KPSPHPVKPL SAAPVEGSPD RKQSRSSLSI
560 570 580 590 600
ALSSGLEKLK TVTSGSIQPV TQAPQAGQMV DTKRLKDSAV LDQSAKYYHL
610 620 630 640 650
THDELISLLL QRERELSQRD EHVQELESYI DRLLVRIMET SPTLLQIPPG

PPK
Length:653
Mass (Da):70,415
Last modified:June 1, 2001 - v1
Checksum:i716725537AA9D86E
GO

Sequence cautioni

The sequence BAA74880.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761Missing in AAH35013 (PubMed:15489334).Curated
Sequence conflicti503 – 5031E → G in AAH35013 (PubMed:15489334).Curated
Sequence conflicti599 – 5991H → N in AAH35013 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF334812 mRNA. Translation: AAK20892.1.
AB020664 mRNA. Translation: BAA74880.1. Different initiation.
BC035013 mRNA. Translation: AAH35013.1.
AF153085 mRNA. Translation: AAF34356.1.
CCDSiCCDS1923.1.
PIRiT17312.
RefSeqiNP_056285.1. NM_015470.2.
UniGeneiHs.24557.

Genome annotation databases

EnsembliENST00000258098; ENSP00000258098; ENSG00000135631.
GeneIDi26056.
KEGGihsa:26056.
UCSCiuc002sit.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF334812 mRNA. Translation: AAK20892.1.
AB020664 mRNA. Translation: BAA74880.1. Different initiation.
BC035013 mRNA. Translation: AAH35013.1.
AF153085 mRNA. Translation: AAF34356.1.
CCDSiCCDS1923.1.
PIRiT17312.
RefSeqiNP_056285.1. NM_015470.2.
UniGeneiHs.24557.

3D structure databases

ProteinModelPortaliQ9BXF6.
SMRiQ9BXF6. Positions 600-651.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117518. 19 interactions.
IntActiQ9BXF6. 14 interactions.
STRINGi9606.ENSP00000258098.

PTM databases

PhosphoSiteiQ9BXF6.

Polymorphism and mutation databases

BioMutaiRAB11FIP5.
DMDMi34223002.

Proteomic databases

MaxQBiQ9BXF6.
PaxDbiQ9BXF6.
PRIDEiQ9BXF6.

Protocols and materials databases

DNASUi26056.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258098; ENSP00000258098; ENSG00000135631.
GeneIDi26056.
KEGGihsa:26056.
UCSCiuc002sit.4. human.

Organism-specific databases

CTDi26056.
GeneCardsiGC02M073212.
HGNCiHGNC:24845. RAB11FIP5.
HPAiHPA036406.
HPA036407.
MIMi605536. gene.
neXtProtiNX_Q9BXF6.
PharmGKBiPA134971129.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG84049.
GeneTreeiENSGT00530000063203.
HOGENOMiHOG000234700.
HOVERGENiHBG079127.
InParanoidiQ9BXF6.
KOiK12484.
OMAiVEKTHGC.
OrthoDBiEOG7WQ7SB.
PhylomeDBiQ9BXF6.
TreeFamiTF326172.

Miscellaneous databases

GeneWikiiRAB11FIP5.
GenomeRNAii26056.
NextBioi47930.
PROiQ9BXF6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BXF6.
CleanExiHS_RAB11FIP5.
GenevisibleiQ9BXF6. 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. "A Rab11/Rip11 protein complex regulates apical membrane trafficking via recycling endosomes."
    Prekeris R., Klumperman J., Scheller R.H.
    Mol. Cell 6:1437-1448(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RAB11A, SUBCELLULAR LOCATION.
  2. "Prediction of the coding sequences of unidentified human genes. XII. 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. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "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: Testis.
  4. "Defining a novel 75-kDa phosphoprotein associated with SS-A/Ro and identification of distinct human autoantibodies."
    Wang D., Buyon J.P., Zhu W., Chan E.K.L.
    J. Clin. Invest. 104:1265-1275(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 105-653, INTERACTION WITH TROVE2, IDENTIFICATION AS ANTIGEN IN AUTOIMMUNE DISEASES, TISSUE SPECIFICITY, PHOSPHORYLATION.
    Tissue: Keratinocyte.
  5. "Gaf-1, a gamma-SNAP-binding protein associated with the mitochondria."
    Chen D., Xu W., He P., Medrano E.E., Whiteheart S.W.
    J. Biol. Chem. 276:13127-13135(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NAPG, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  6. "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.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307 AND SER-538, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; SER-307; SER-494 AND SER-538, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Rab11b and its effector Rip11 regulate the acidosis-induced traffic of V-ATPase in salivary ducts."
    Oehlke O., Martin H.W., Osterberg N., Roussa E.
    J. Cell. Physiol. 226:638-651(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRFIP5_HUMAN
AccessioniPrimary (citable) accession number: Q9BXF6
Secondary accession number(s): O94939, Q9P0M1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 123 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

Miscellaneous

Antibodies against RIP11 are found in sera from patients with autoimmune diseases such as systemic lupus erythematosus (SLE) or Sjoegren syndrome (SS). It is also found in the sera from mothers of children with neonatal lupus erythematosus (NLE).

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

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 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.