ID   RAB12_HUMAN             Reviewed;         244 AA.
AC   Q6IQ22; A6NEF5; Q4KMQ3;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   16-MAY-2012, entry version 81.
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-25, AND MASS
RP   SPECTROMETRY.
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
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   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   [7]
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   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor (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;
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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   IPI; IPI00419932; -.
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; Q6IQ22; -.
DR   PhosphoSite; Q6IQ22; -.
DR   DMDM; 122064944; -.
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   GeneTree; ENSGT00650000093150; -.
DR   HOGENOM; HOG000233968; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; Q6IQ22; -.
DR   KO; K07907; -.
DR   OMA; CEVDREI; -.
DR   OrthoDB; EOG45757M; -.
DR   EvolutionaryTrace; Q6IQ22; -.
DR   NextBio; 90147; -.
DR   ArrayExpress; Q6IQ22; -.
DR   Bgee; Q6IQ22; -.
DR   CleanEx; HS_RAB12; -.
DR   Genevestigator; Q6IQ22; -.
DR   GO; GO:0000139; C:Golgi 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; 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   TIGRFAMs; TIGR00231; Small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Golgi apparatus; GTP-binding;
KW   Lipoprotein; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Prenylation; Protein transport; 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      21     21       Phosphoserine.
FT   MOD_RES      25     25       Phosphoserine.
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        56     62
FT   STRAND       78     85
FT   STRAND       90     97
FT   HELIX       102    104
FT   HELIX       105    114
FT   STRAND      119    121
FT   HELIX       127    131
FT   HELIX       133    143
FT   STRAND      151    153
FT   HELIX       157    162
FT   HELIX       172    175
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
//