Full text data of RAB1C
RAB1C
[Confidence: low (only semi-automatic identification from reviews)]
Putative Ras-related protein Rab-1C; hRab1c
Putative Ras-related protein Rab-1C; hRab1c
UniProt
Q92928
ID RAB1C_HUMAN Reviewed; 201 AA.
AC Q92928;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-2008, sequence version 2.
DT 22-JAN-2014, entry version 83.
DE RecName: Full=Putative Ras-related protein Rab-1C;
DE Short=hRab1c;
GN Name=RAB1C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 67-119.
RC TISSUE=Melanoma;
RX PubMed=9030196; DOI=10.1016/S0167-4889(96)00169-3;
RA Chen D., Guo J., Gahl W.A.;
RT "RAB GTPases expressed in human melanoma cells.";
RL Biochim. Biophys. Acta 1355:1-6(1997).
RN [3]
RP INTERACTION WITH L.PNEUMOPHILA ANKX, AND CHOLINEPHOSPHORYLATION AT
RP SER-76.
RX PubMed=21822290; DOI=10.1038/nature10335;
RA Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.;
RT "Modulation of Rab GTPase function by a protein phosphocholine
RT transferase.";
RL Nature 477:103-106(2011).
RN [4]
RP INTERACTION WITH L.PNEUMOPHILA LEM3, AND DECHOLINEPHOSPHORYLATION AT
RP SER-76.
RX PubMed=22158903; DOI=10.1073/pnas.1114023109;
RA Tan Y., Arnold R.J., Luo Z.Q.;
RT "Legionella pneumophila regulates the small GTPase Rab1 activity by
RT reversible phosphorylcholination.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:21212-21217(2011).
CC -!- FUNCTION: Protein transport. Probably involved in vesicular
CC traffic (By similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor; Cytoplasmic side.
CC Cytoplasm (By similarity).
CC -!- PTM: Phosphocholinated at Ser-76 by L.pneumophila AnkX, leading to
CC displace GDP dissociation inhibitors (GDI). Both GDP-bound and
CC GTP-bound forms can be phosphocholinated. Dephosphocholinated by
CC L.pneumophila Lem3, restoring accessibility to L.pneumophila
CC GTPase effector LepB.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC -!- CAUTION: Could be the product of a pseudogene.
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; AL513165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U66622; AAC51197.1; -; mRNA.
DR UniGene; Hs.651788; -.
DR ProteinModelPortal; Q92928; -.
DR SMR; Q92928; 5-173.
DR IntAct; Q92928; 1.
DR DMDM; 193806493; -.
DR PRIDE; Q92928; -.
DR GeneCards; GC09M037629; -.
DR HGNC; HGNC:23683; RAB1C.
DR HPA; CAB010225; -.
DR neXtProt; NX_Q92928; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q92928; -.
DR Genevestigator; Q92928; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003579; Small_GTPase_Rab_type.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 5: Uncertain;
KW Complete proteome; Cytoplasm; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 201 Putative Ras-related protein Rab-1C.
FT /FTId=PRO_0000343568.
FT NP_BIND 15 22 GTP (By similarity).
FT NP_BIND 63 67 GTP (By similarity).
FT NP_BIND 121 124 GTP (By similarity).
FT MOTIF 37 45 Effector region (By similarity).
FT MOD_RES 76 76 O-(2-cholinephosphoryl)serine; by
FT Legionella AnkX (By similarity).
FT LIPID 200 200 S-geranylgeranyl cysteine (By
FT similarity).
FT LIPID 201 201 S-geranylgeranyl cysteine (By
FT similarity).
SQ SEQUENCE 201 AA; 22017 MW; D6E22F1D13FBD22C CRC64;
MNPGYDCLFK LLLIGDSGVG KSCLLLRFAD DPYTESYIST IGVDFKIQTI ELDGKTIKLQ
IWDTAGQERF WTITSSYYRG AHGFLVVYDV TDQESYANVK QWLQEIDRHA SENVNKLLVG
NKSDLTTKKV VDNTTAKEFA DSLGIPFLET SAKNATNVEQ AFMTMAAEIK KQMGPGAASG
GERPNLKIDS TPVKPAGGGC C
//
ID RAB1C_HUMAN Reviewed; 201 AA.
AC Q92928;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-2008, sequence version 2.
DT 22-JAN-2014, entry version 83.
DE RecName: Full=Putative Ras-related protein Rab-1C;
DE Short=hRab1c;
GN Name=RAB1C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 67-119.
RC TISSUE=Melanoma;
RX PubMed=9030196; DOI=10.1016/S0167-4889(96)00169-3;
RA Chen D., Guo J., Gahl W.A.;
RT "RAB GTPases expressed in human melanoma cells.";
RL Biochim. Biophys. Acta 1355:1-6(1997).
RN [3]
RP INTERACTION WITH L.PNEUMOPHILA ANKX, AND CHOLINEPHOSPHORYLATION AT
RP SER-76.
RX PubMed=21822290; DOI=10.1038/nature10335;
RA Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.;
RT "Modulation of Rab GTPase function by a protein phosphocholine
RT transferase.";
RL Nature 477:103-106(2011).
RN [4]
RP INTERACTION WITH L.PNEUMOPHILA LEM3, AND DECHOLINEPHOSPHORYLATION AT
RP SER-76.
RX PubMed=22158903; DOI=10.1073/pnas.1114023109;
RA Tan Y., Arnold R.J., Luo Z.Q.;
RT "Legionella pneumophila regulates the small GTPase Rab1 activity by
RT reversible phosphorylcholination.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:21212-21217(2011).
CC -!- FUNCTION: Protein transport. Probably involved in vesicular
CC traffic (By similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor; Cytoplasmic side.
CC Cytoplasm (By similarity).
CC -!- PTM: Phosphocholinated at Ser-76 by L.pneumophila AnkX, leading to
CC displace GDP dissociation inhibitors (GDI). Both GDP-bound and
CC GTP-bound forms can be phosphocholinated. Dephosphocholinated by
CC L.pneumophila Lem3, restoring accessibility to L.pneumophila
CC GTPase effector LepB.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC -!- CAUTION: Could be the product of a pseudogene.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AL513165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U66622; AAC51197.1; -; mRNA.
DR UniGene; Hs.651788; -.
DR ProteinModelPortal; Q92928; -.
DR SMR; Q92928; 5-173.
DR IntAct; Q92928; 1.
DR DMDM; 193806493; -.
DR PRIDE; Q92928; -.
DR GeneCards; GC09M037629; -.
DR HGNC; HGNC:23683; RAB1C.
DR HPA; CAB010225; -.
DR neXtProt; NX_Q92928; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q92928; -.
DR Genevestigator; Q92928; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003579; Small_GTPase_Rab_type.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 5: Uncertain;
KW Complete proteome; Cytoplasm; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 201 Putative Ras-related protein Rab-1C.
FT /FTId=PRO_0000343568.
FT NP_BIND 15 22 GTP (By similarity).
FT NP_BIND 63 67 GTP (By similarity).
FT NP_BIND 121 124 GTP (By similarity).
FT MOTIF 37 45 Effector region (By similarity).
FT MOD_RES 76 76 O-(2-cholinephosphoryl)serine; by
FT Legionella AnkX (By similarity).
FT LIPID 200 200 S-geranylgeranyl cysteine (By
FT similarity).
FT LIPID 201 201 S-geranylgeranyl cysteine (By
FT similarity).
SQ SEQUENCE 201 AA; 22017 MW; D6E22F1D13FBD22C CRC64;
MNPGYDCLFK LLLIGDSGVG KSCLLLRFAD DPYTESYIST IGVDFKIQTI ELDGKTIKLQ
IWDTAGQERF WTITSSYYRG AHGFLVVYDV TDQESYANVK QWLQEIDRHA SENVNKLLVG
NKSDLTTKKV VDNTTAKEFA DSLGIPFLET SAKNATNVEQ AFMTMAAEIK KQMGPGAASG
GERPNLKIDS TPVKPAGGGC C
//