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Protein

Putative Ras-related protein Rab-1C

Gene

RAB1C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein uncertaini

Functioni

Protein transport. Probably involved in vesicular traffic (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 239GTPBy similarity
Nucleotide bindingi33 – 408GTPBy similarity
Nucleotide bindingi63 – 675GTPBy similarity
Nucleotide bindingi121 – 1244GTPBy similarity
Nucleotide bindingi151 – 1533GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Putative Ras-related protein Rab-1C
Short name:
hRab1c
Gene namesi
Name:RAB1C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:23683. RAB1C.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201Putative Ras-related protein Rab-1CPRO_0000343568Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei76 – 761O-(2-cholinephosphoryl)serine; by Legionella AnkXBy similarity
Lipidationi200 – 2001S-geranylgeranyl cysteineBy similarity
Lipidationi201 – 2011S-geranylgeranyl cysteineBy similarity

Post-translational modificationi

Phosphocholinated at Ser-76 by L.pneumophila AnkX, leading to displace GDP dissociation inhibitors (GDI). Both GDP-bound and GTP-bound forms can be phosphocholinated. Dephosphocholinated by L.pneumophila Lem3, restoring accessibility to L.pneumophila GTPase effector LepB.

Keywords - PTMi

Acetylation, Lipoprotein, Phosphoprotein, Prenylation

Proteomic databases

EPDiQ92928.
PaxDbiQ92928.
PRIDEiQ92928.

PTM databases

iPTMnetiQ92928.
SwissPalmiQ92928.

Expressioni

Organism-specific databases

HPAiHPA056141.

Interactioni

Protein-protein interaction databases

IntActiQ92928. 1 interaction.
STRINGi9606.ENSP00000310226.

Structurei

3D structure databases

ProteinModelPortaliQ92928.
SMRiQ92928. Positions 5-173.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi37 – 459Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiKOG0084. Eukaryota.
ENOG410XQN5. LUCA.
HOVERGENiHBG009351.
InParanoidiQ92928.
PhylomeDBiQ92928.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92928-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPGYDCLFK LLLIGDSGVG KSCLLLRFAD DPYTESYIST IGVDFKIQTI
60 70 80 90 100
ELDGKTIKLQ IWDTAGQERF WTITSSYYRG AHGFLVVYDV TDQESYANVK
110 120 130 140 150
QWLQEIDRHA SENVNKLLVG NKSDLTTKKV VDNTTAKEFA DSLGIPFLET
160 170 180 190 200
SAKNATNVEQ AFMTMAAEIK KQMGPGAASG GERPNLKIDS TPVKPAGGGC

C
Length:201
Mass (Da):22,017
Last modified:July 1, 2008 - v2
Checksum:iD6E22F1D13FBD22C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL513165 Genomic DNA. No translation available.
U66622 mRNA. Translation: AAC51197.1.
UniGeneiHs.651788.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL513165 Genomic DNA. No translation available.
U66622 mRNA. Translation: AAC51197.1.
UniGeneiHs.651788.

3D structure databases

ProteinModelPortaliQ92928.
SMRiQ92928. Positions 5-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ92928. 1 interaction.
STRINGi9606.ENSP00000310226.

PTM databases

iPTMnetiQ92928.
SwissPalmiQ92928.

Proteomic databases

EPDiQ92928.
PaxDbiQ92928.
PRIDEiQ92928.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GeneCardsiRAB1C.
HGNCiHGNC:23683. RAB1C.
HPAiHPA056141.
neXtProtiNX_Q92928.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0084. Eukaryota.
ENOG410XQN5. LUCA.
HOVERGENiHBG009351.
InParanoidiQ92928.
PhylomeDBiQ92928.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "RAB GTPases expressed in human melanoma cells."
    Chen D., Guo J., Gahl W.A.
    Biochim. Biophys. Acta 1355:1-6(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 67-119.
    Tissue: Melanoma.
  3. "Modulation of Rab GTPase function by a protein phosphocholine transferase."
    Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.
    Nature 477:103-106(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH L.PNEUMOPHILA ANKX, PHOSPHORYLATION AT SER-76.
  4. "Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination."
    Tan Y., Arnold R.J., Luo Z.Q.
    Proc. Natl. Acad. Sci. U.S.A. 108:21212-21217(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH L.PNEUMOPHILA LEM3, PHOSPHORYLATION AT SER-76.

Entry informationi

Entry nameiRAB1C_HUMAN
AccessioniPrimary (citable) accession number: Q92928
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 1, 2008
Last modified: May 11, 2016
This is version 96 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

Caution

Could be the product of a pseudogene.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. 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.