Full text data of RAB12
RAB12
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Ras-related protein Rab-12
Ras-related protein Rab-12
UniProt
Q6IQ22
ID RAB12_HUMAN Reviewed; 244 AA.
AC Q6IQ22; A6NEF5; Q4KMQ3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 09-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=Ras-related protein Rab-12;
GN Name=RAB12;
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=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
RA Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
RA Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
RA Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
RA Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
RA Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
RA O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP ENZYME REGULATION.
RX PubMed=20937701; DOI=10.1083/jcb.201008051;
RA Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.;
RT "Family-wide characterization of the DENN domain Rab GDP-GTP exchange
RT factors.";
RL J. Cell Biol. 191:367-381(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP INTERACTION WITH RABIF.
RX PubMed=21194374; DOI=10.1515/BC.2011.022;
RA Wixler V., Wixler L., Altenfeld A., Ludwig S., Goody R.S., Itzen A.;
RT "Identification and characterisation of novel Mss4-binding Rab
RT GTPases.";
RL Biol. Chem. 392:239-248(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 36-208 IN COMPLEX WITH
RP MAGNESIUM AND GDP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of a predicted human GTPase in complex with GDP.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: The small GTPases Rab are key regulators of
CC intracellular membrane trafficking, from the formation of
CC transport vesicles to their fusion with membranes. Rabs cycle
CC between an inactive GDP-bound form and an active GTP-bound form
CC that is able to recruit to membranes different set of downstream
CC effectors directly responsible for vesicle formation, movement,
CC tethering and fusion. That Rab may play a role in protein
CC transport from recycling endosomes to lysosomes regulating, for
CC instance, the degradation of the transferrin receptor (By
CC similarity).
CC -!- ENZYME REGULATION: Rab activation is generally mediated by a
CC guanine exchange factor (GEF), while inactivation through
CC hydrolysis of bound GTP is catalyzed by a GTPase activating
CC protein (GAP) (By similarity). That Rab is activated by DENND3, a
CC guanine exchange factor.
CC -!- SUBUNIT: May interact with RABIF.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor;
CC Cytoplasmic side (By similarity). Lysosome membrane; Lipid-anchor;
CC Cytoplasmic side (By similarity). Golgi apparatus membrane (By
CC similarity).
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH71600.2; Type=Miscellaneous discrepancy; Note=Intron retention;
CC Sequence=AAH98407.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC Sequence=BC050338; Type=Frameshift; Positions=195;
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; AP001793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471113; EAX01616.1; -; Genomic_DNA.
DR EMBL; BC050338; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC071600; AAH71600.2; ALT_SEQ; mRNA.
DR EMBL; BC098407; AAH98407.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001020471.2; NM_001025300.2.
DR UniGene; Hs.270074; -.
DR PDB; 2IL1; X-ray; 2.10 A; A=36-208.
DR PDBsum; 2IL1; -.
DR ProteinModelPortal; Q6IQ22; -.
DR SMR; Q6IQ22; 38-208.
DR STRING; 9606.ENSP00000331748; -.
DR PhosphoSite; Q6IQ22; -.
DR DMDM; 122064944; -.
DR PaxDb; Q6IQ22; -.
DR PRIDE; Q6IQ22; -.
DR DNASU; 201475; -.
DR Ensembl; ENST00000329286; ENSP00000331748; ENSG00000206418.
DR GeneID; 201475; -.
DR KEGG; hsa:201475; -.
DR UCSC; uc002knp.3; human.
DR CTD; 201475; -.
DR GeneCards; GC18P008600; -.
DR HGNC; HGNC:31332; RAB12.
DR HPA; HPA040727; -.
DR neXtProt; NX_Q6IQ22; -.
DR PharmGKB; PA142671102; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233968; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q6IQ22; -.
DR KO; K07907; -.
DR OMA; PPRMRCC; -.
DR OrthoDB; EOG769ZKM; -.
DR ChiTaRS; RAB12; human.
DR EvolutionaryTrace; Q6IQ22; -.
DR GenomeRNAi; 201475; -.
DR NextBio; 90147; -.
DR PRO; PR:Q6IQ22; -.
DR Bgee; Q6IQ22; -.
DR CleanEx; HS_RAB12; -.
DR Genevestigator; Q6IQ22; -.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0044257; P:cellular protein catabolic process; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Endosome;
KW Golgi apparatus; GTP-binding; Lipoprotein; Lysosome; Membrane;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 244 Ras-related protein Rab-12.
FT /FTId=PRO_0000271377.
FT NP_BIND 49 57 GTP.
FT NP_BIND 97 101 GTP (By similarity).
FT NP_BIND 155 159 GTP.
FT NP_BIND 187 188 GTP.
FT MOTIF 71 79 Effector region (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 21 21 Phosphoserine (By similarity).
FT MOD_RES 106 106 Phosphoserine (By similarity).
FT LIPID 243 243 S-geranylgeranyl cysteine (By
FT similarity).
FT LIPID 244 244 S-geranylgeranyl cysteine (By
FT similarity).
FT STRAND 40 48
FT HELIX 55 62
FT STRAND 77 86
FT STRAND 89 98
FT HELIX 102 104
FT HELIX 105 114
FT STRAND 116 123
FT HELIX 127 131
FT HELIX 133 143
FT STRAND 149 155
FT HELIX 157 162
FT HELIX 167 175
FT STRAND 181 184
FT TURN 187 190
FT HELIX 193 206
SQ SEQUENCE 244 AA; 27248 MW; B4DC65DD0DCB45C4 CRC64;
MDPGAALQRR AGGGGGLGAG SPALSGGQGR RRKQPPRPAD FKLQVIIIGS RGVGKTSLME
RFTDDTFCEA CKSTVGVDFK IKTVELRGKK IRLQIWDTAG QERFNSITSA YYRSAKGIIL
VYDITKKETF DDLPKWMKMI DKYASEDAEL LLVGNKLDCE TDREITRQQG EKFAQQITGM
RFCEASAKDN FNVDEIFLKL VDDILKKMPL DILRNELSNS ILSLQPEPEI PPELPPPRPH
VRCC
//
ID RAB12_HUMAN Reviewed; 244 AA.
AC Q6IQ22; A6NEF5; Q4KMQ3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 09-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=Ras-related protein Rab-12;
GN Name=RAB12;
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=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
RA Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
RA Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
RA Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
RA Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
RA Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
RA O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP ENZYME REGULATION.
RX PubMed=20937701; DOI=10.1083/jcb.201008051;
RA Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.;
RT "Family-wide characterization of the DENN domain Rab GDP-GTP exchange
RT factors.";
RL J. Cell Biol. 191:367-381(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP INTERACTION WITH RABIF.
RX PubMed=21194374; DOI=10.1515/BC.2011.022;
RA Wixler V., Wixler L., Altenfeld A., Ludwig S., Goody R.S., Itzen A.;
RT "Identification and characterisation of novel Mss4-binding Rab
RT GTPases.";
RL Biol. Chem. 392:239-248(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 36-208 IN COMPLEX WITH
RP MAGNESIUM AND GDP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of a predicted human GTPase in complex with GDP.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: The small GTPases Rab are key regulators of
CC intracellular membrane trafficking, from the formation of
CC transport vesicles to their fusion with membranes. Rabs cycle
CC between an inactive GDP-bound form and an active GTP-bound form
CC that is able to recruit to membranes different set of downstream
CC effectors directly responsible for vesicle formation, movement,
CC tethering and fusion. That Rab may play a role in protein
CC transport from recycling endosomes to lysosomes regulating, for
CC instance, the degradation of the transferrin receptor (By
CC similarity).
CC -!- ENZYME REGULATION: Rab activation is generally mediated by a
CC guanine exchange factor (GEF), while inactivation through
CC hydrolysis of bound GTP is catalyzed by a GTPase activating
CC protein (GAP) (By similarity). That Rab is activated by DENND3, a
CC guanine exchange factor.
CC -!- SUBUNIT: May interact with RABIF.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor;
CC Cytoplasmic side (By similarity). Lysosome membrane; Lipid-anchor;
CC Cytoplasmic side (By similarity). Golgi apparatus membrane (By
CC similarity).
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH71600.2; Type=Miscellaneous discrepancy; Note=Intron retention;
CC Sequence=AAH98407.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC Sequence=BC050338; Type=Frameshift; Positions=195;
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; AP001793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471113; EAX01616.1; -; Genomic_DNA.
DR EMBL; BC050338; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC071600; AAH71600.2; ALT_SEQ; mRNA.
DR EMBL; BC098407; AAH98407.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001020471.2; NM_001025300.2.
DR UniGene; Hs.270074; -.
DR PDB; 2IL1; X-ray; 2.10 A; A=36-208.
DR PDBsum; 2IL1; -.
DR ProteinModelPortal; Q6IQ22; -.
DR SMR; Q6IQ22; 38-208.
DR STRING; 9606.ENSP00000331748; -.
DR PhosphoSite; Q6IQ22; -.
DR DMDM; 122064944; -.
DR PaxDb; Q6IQ22; -.
DR PRIDE; Q6IQ22; -.
DR DNASU; 201475; -.
DR Ensembl; ENST00000329286; ENSP00000331748; ENSG00000206418.
DR GeneID; 201475; -.
DR KEGG; hsa:201475; -.
DR UCSC; uc002knp.3; human.
DR CTD; 201475; -.
DR GeneCards; GC18P008600; -.
DR HGNC; HGNC:31332; RAB12.
DR HPA; HPA040727; -.
DR neXtProt; NX_Q6IQ22; -.
DR PharmGKB; PA142671102; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233968; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q6IQ22; -.
DR KO; K07907; -.
DR OMA; PPRMRCC; -.
DR OrthoDB; EOG769ZKM; -.
DR ChiTaRS; RAB12; human.
DR EvolutionaryTrace; Q6IQ22; -.
DR GenomeRNAi; 201475; -.
DR NextBio; 90147; -.
DR PRO; PR:Q6IQ22; -.
DR Bgee; Q6IQ22; -.
DR CleanEx; HS_RAB12; -.
DR Genevestigator; Q6IQ22; -.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0044257; P:cellular protein catabolic process; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Endosome;
KW Golgi apparatus; GTP-binding; Lipoprotein; Lysosome; Membrane;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 244 Ras-related protein Rab-12.
FT /FTId=PRO_0000271377.
FT NP_BIND 49 57 GTP.
FT NP_BIND 97 101 GTP (By similarity).
FT NP_BIND 155 159 GTP.
FT NP_BIND 187 188 GTP.
FT MOTIF 71 79 Effector region (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 21 21 Phosphoserine (By similarity).
FT MOD_RES 106 106 Phosphoserine (By similarity).
FT LIPID 243 243 S-geranylgeranyl cysteine (By
FT similarity).
FT LIPID 244 244 S-geranylgeranyl cysteine (By
FT similarity).
FT STRAND 40 48
FT HELIX 55 62
FT STRAND 77 86
FT STRAND 89 98
FT HELIX 102 104
FT HELIX 105 114
FT STRAND 116 123
FT HELIX 127 131
FT HELIX 133 143
FT STRAND 149 155
FT HELIX 157 162
FT HELIX 167 175
FT STRAND 181 184
FT TURN 187 190
FT HELIX 193 206
SQ SEQUENCE 244 AA; 27248 MW; B4DC65DD0DCB45C4 CRC64;
MDPGAALQRR AGGGGGLGAG SPALSGGQGR RRKQPPRPAD FKLQVIIIGS RGVGKTSLME
RFTDDTFCEA CKSTVGVDFK IKTVELRGKK IRLQIWDTAG QERFNSITSA YYRSAKGIIL
VYDITKKETF DDLPKWMKMI DKYASEDAEL LLVGNKLDCE TDREITRQQG EKFAQQITGM
RFCEASAKDN FNVDEIFLKL VDDILKKMPL DILRNELSNS ILSLQPEPEI PPELPPPRPH
VRCC
//