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Protein

Guanine nucleotide exchange factor MSS4

Gene

RABIF

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

Functioni

Guanine-nucleotide-releasing protein that acts on members of the SEC4/YPT1/RAB subfamily. Stimulates GDP release from both YPT1 and RAB3A, but is less active on these proteins than on the SEC4 protein. Might play a general role in vesicular transport.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi23 – 231ZincPROSITE-ProRule annotation
Metal bindingi26 – 261ZincPROSITE-ProRule annotation
Metal bindingi94 – 941ZincPROSITE-ProRule annotation
Metal bindingi97 – 971ZincPROSITE-ProRule annotation

GO - Molecular functioni

  • guanyl-nucleotide exchange factor activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • membrane fusion Source: ProtInc
  • protein transport Source: UniProtKB-KW
  • small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide exchange factor MSS4
Alternative name(s):
Rab-interacting factor
Gene namesi
Name:RABIF
Synonyms:MSS4, RASGRF3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9797. RABIF.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34158.

Polymorphism and mutation databases

BioMutaiRABIF.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 123123Guanine nucleotide exchange factor MSS4PRO_0000174174Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP47224.
MaxQBiP47224.
PaxDbiP47224.
PeptideAtlasiP47224.
PRIDEiP47224.
TopDownProteomicsiP47224.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiP47224.
CleanExiHS_RABIF.
GenevisibleiP47224. HS.

Organism-specific databases

HPAiHPA027715.
HPA054936.

Interactioni

Subunit structurei

Interacts with RAB8A.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RAB3AP203363EBI-713992,EBI-1045943
RAB8AP610062EBI-713992,EBI-722293
RASSF5Q8WWW03EBI-713992,EBI-367390
RELQ048643EBI-713992,EBI-307352
TCF4P158843EBI-713992,EBI-533224
TERF2IPQ9NYB02EBI-713992,EBI-750109

Protein-protein interaction databases

BioGridi111815. 30 interactions.
IntActiP47224. 12 interactions.
MINTiMINT-1396805.
STRINGi9606.ENSP00000356231.

Structurei

Secondary structure

1
123
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 228Combined sources
Turni24 – 263Combined sources
Beta strandi29 – 313Combined sources
Beta strandi37 – 393Combined sources
Beta strandi43 – 464Combined sources
Beta strandi62 – 654Combined sources
Beta strandi68 – 725Combined sources
Helixi74 – 763Combined sources
Beta strandi78 – 836Combined sources
Beta strandi89 – 935Combined sources
Turni95 – 973Combined sources
Beta strandi103 – 1064Combined sources
Beta strandi113 – 1164Combined sources
Helixi117 – 1193Combined sources
Beta strandi120 – 1234Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FWQNMR-A1-123[»]
2FU5X-ray2.00A/B11-123[»]
ProteinModelPortaliP47224.
SMRiP47224. Positions 9-123.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP47224.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 123115MSS4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the DSS4/MSS4 family.PROSITE-ProRule annotation
Contains 1 MSS4 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4113. Eukaryota.
ENOG4111UFA. LUCA.
GeneTreeiENSGT00390000016889.
HOGENOMiHOG000007903.
HOVERGENiHBG006402.
InParanoidiP47224.
KOiK19952.
OMAiGWHSLDD.
OrthoDBiEOG76DTVD.
PhylomeDBiP47224.
TreeFamiTF314029.

Family and domain databases

Gene3Di2.170.150.10. 1 hit.
InterProiIPR007515. Mss4.
IPR011057. Mss4-like.
IPR011323. Mss4/transl-control_tumor.
[Graphical view]
PfamiPF04421. Mss4. 1 hit.
[Graphical view]
SUPFAMiSSF51316. SSF51316. 1 hit.
PROSITEiPS51796. MSS4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P47224-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPAEQPSEL VSAEGRNRKA VLCQRCGSRV LQPGTALFSR RQLFLPSMRK
60 70 80 90 100
KPALSDGSNP DGDLLQEHWL VEDMFIFENV GFTKDVGNIK FLVCADCEIG
110 120
PIGWHCLDDK NSFYVALERV SHE
Length:123
Mass (Da):13,839
Last modified:November 1, 1997 - v2
Checksum:i78E98395FAE10257
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 62EQ → DE in AAB34955 (PubMed:7619808).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S78873 mRNA. Translation: AAB34955.1.
U74324 mRNA. Translation: AAB18264.1.
BT007133 mRNA. Translation: AAP35797.1.
AK311900 mRNA. Translation: BAG34841.1.
CH471067 Genomic DNA. Translation: EAW91443.1.
BC018488 mRNA. Translation: AAH18488.1.
BC037392 mRNA. Translation: AAH37392.1.
CCDSiCCDS1428.1.
PIRiI52427.
RefSeqiNP_002862.2. NM_002871.4.
UniGeneiHs.90875.

Genome annotation databases

EnsembliENST00000367262; ENSP00000356231; ENSG00000183155.
GeneIDi5877.
KEGGihsa:5877.
UCSCiuc001gyl.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S78873 mRNA. Translation: AAB34955.1.
U74324 mRNA. Translation: AAB18264.1.
BT007133 mRNA. Translation: AAP35797.1.
AK311900 mRNA. Translation: BAG34841.1.
CH471067 Genomic DNA. Translation: EAW91443.1.
BC018488 mRNA. Translation: AAH18488.1.
BC037392 mRNA. Translation: AAH37392.1.
CCDSiCCDS1428.1.
PIRiI52427.
RefSeqiNP_002862.2. NM_002871.4.
UniGeneiHs.90875.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FWQNMR-A1-123[»]
2FU5X-ray2.00A/B11-123[»]
ProteinModelPortaliP47224.
SMRiP47224. Positions 9-123.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111815. 30 interactions.
IntActiP47224. 12 interactions.
MINTiMINT-1396805.
STRINGi9606.ENSP00000356231.

Polymorphism and mutation databases

BioMutaiRABIF.

Proteomic databases

EPDiP47224.
MaxQBiP47224.
PaxDbiP47224.
PeptideAtlasiP47224.
PRIDEiP47224.
TopDownProteomicsiP47224.

Protocols and materials databases

DNASUi5877.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367262; ENSP00000356231; ENSG00000183155.
GeneIDi5877.
KEGGihsa:5877.
UCSCiuc001gyl.4. human.

Organism-specific databases

CTDi5877.
GeneCardsiRABIF.
HGNCiHGNC:9797. RABIF.
HPAiHPA027715.
HPA054936.
MIMi603417. gene.
neXtProtiNX_P47224.
PharmGKBiPA34158.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4113. Eukaryota.
ENOG4111UFA. LUCA.
GeneTreeiENSGT00390000016889.
HOGENOMiHOG000007903.
HOVERGENiHBG006402.
InParanoidiP47224.
KOiK19952.
OMAiGWHSLDD.
OrthoDBiEOG76DTVD.
PhylomeDBiP47224.
TreeFamiTF314029.

Miscellaneous databases

EvolutionaryTraceiP47224.
GeneWikiiRABIF.
GenomeRNAii5877.
PROiP47224.
SOURCEiSearch...

Gene expression databases

BgeeiP47224.
CleanExiHS_RABIF.
GenevisibleiP47224. HS.

Family and domain databases

Gene3Di2.170.150.10. 1 hit.
InterProiIPR007515. Mss4.
IPR011057. Mss4-like.
IPR011323. Mss4/transl-control_tumor.
[Graphical view]
PfamiPF04421. Mss4. 1 hit.
[Graphical view]
SUPFAMiSSF51316. SSF51316. 1 hit.
PROSITEiPS51796. MSS4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, Zn2+ binding, and structural characterization of the guanine nucleotide exchange factor human Mss4."
    Yu H., Schreiber S.L.
    Biochemistry 34:9103-9110(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Cloning of novel transcripts of the human guanine-nucleotide-exchange factor Mss4: in situ chromosomal mapping and expression in pancreatic cancer."
    Mueller-Pillasch F., Zimmerhackl F., Lacher U., Schultz N., Hameister H., Varga G., Friess H., Buechler M., Adler G., Gress T.M.
    Genomics 46:389-396(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Spleen.
  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].
    Tissue: Brain and Prostate.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Structure of guanine-nucleotide-exchange factor human Mss4 and identification of its Rab-interacting surface."
    Yu H., Schreiber S.L.
    Nature 376:788-791(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  11. "Nucleotide exchange via local protein unfolding--structure of Rab8 in complex with MSS4."
    Itzen A., Pylypenko O., Goody R.S., Alexandrov K., Rak A.
    EMBO J. 25:1445-1455(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 11-123 IN COMPLEX WITH RAB8A, INTERACTION WITH RAB8A.

Entry informationi

Entry nameiMSS4_HUMAN
AccessioniPrimary (citable) accession number: P47224
Secondary accession number(s): B2R4P4, Q92992
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 140 of the entry and version 2 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 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.