(data stored in ACNUC4266 zone)

HOVERGEN: RAB21_HUMAN

ID   RAB21_HUMAN             Reviewed;         225 AA.
AC   Q9UL25; Q14466; Q569H3;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-NOV-2009, entry version 93.
DE   RecName: Full=Ras-related protein Rab-21;
GN   Name=RAB21; Synonyms=KIAA0118;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Colon carcinoma;
RX   MEDLINE=20343874; PubMed=10887961; DOI=10.1078/S0171-9335(04)70034-5;
RA   Opdam F.J.M., Kamps G., Croes H., van Bokhoven H., Ginsel L.A.,
RA   Fransen J.A.M.;
RT   "Expression of Rab small GTPases in epithelial Caco-2 cells: Rab21 is
RT   an apically located GTP-binding protein in polarised intestinal
RT   epithelial cells.";
RL   Eur. J. Cell Biol. 79:308-316(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lymph, and 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   [3]
RP   PROTEIN SEQUENCE OF 2-16; 48-59; 91-109 AND 141-157, CLEAVAGE OF
RP   INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V.;
RL   Submitted (JUN-2005) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-225.
RC   TISSUE=Bone marrow;
RX   MEDLINE=95308325; PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA   Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
RA   Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. III.
RT   The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
RT   analysis of cDNA clones from human cell line KG-1.";
RL   DNA Res. 2:37-43(1995).
RN   [5]
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-33 AND GLN-78.
RX   PubMed=15561770; DOI=10.1242/jcs.01560;
RA   Simpson J.C., Griffiths G., Wessling-Resnick M., Fransen J.A.M.,
RA   Bennett H., Jones A.T.;
RT   "A role for the small GTPase Rab21 in the early endocytic pathway.";
RL   J. Cell Sci. 117:6297-6311(2004).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18804435; DOI=10.1016/j.devcel.2008.08.001;
RA   Pellinen T., Tuomi S., Arjonen A., Wolf M., Edgren H., Meyer H.,
RA   Grosse R., Kitzing T., Rantala J.K., Kallioniemi O., Faessler R.,
RA   Kallio M., Ivaska J.;
RT   "Integrin trafficking regulated by Rab21 is necessary for
RT   cytokinesis.";
RL   Dev. Cell 15:371-385(2008).
RN   [7]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: Regulates integrin internalization and recycling, but
CC       does not influence the traffic of endosomally translocated
CC       receptors in general. As a result, may regulate cell adhesion and
CC       migration (By similarity). During the mitosis of adherent cells,
CC       controls the endosomal trafficking of integrins which is required
CC       for the successful completion of cytokinesis.
CC   -!- SUBUNIT: Interacts with the cytoplasmic tail of integrins ITGA1,
CC       ITGA2, ITGA5, ITGA6, ITGA11 and ITGB1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Lipid-anchor
CC       (By similarity). Golgi apparatus membrane. Early endosome
CC       membrane. Cytoplasmic vesicle membrane. Note=In nonpolarized
CC       epithelial Caco-2 cells, found in the endoplasmic reticulum; in
CC       polarized cells, observed in vesicles in the apical cytoplasm.
CC       During mitosis, in mid-telophase, localized in the ingressing
CC       cleavage furrow. In late telophase, detected at the opposite poles
CC       of the daughter cells, in vesicles at the base of lamellipodia
CC       formed by the separating daughter cells.
CC   -!- TISSUE SPECIFICITY: Widely expressed. In jejunal tissue,
CC       predominantly expressed in the apical region of the epithelial
CC       cell layer of the villi, weak expression, if any, in the crypt
CC       epithelium. Capillary endothelium and some cell types in the
CC       lamina propria also show expression.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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CC   -!- GENE_FAMILY: HBG009351 [ FAMILY / ALN / TREE ]
DR   EMBL; AF091035; AAF00048.1; -; mRNA.
DR   EMBL; BC021901; AAH21901.1; -; mRNA.
DR   EMBL; BC092475; AAH92475.1; -; mRNA.
DR   EMBL; D42087; BAA07682.1; -; mRNA.
DR   IPI; IPI00007755; -.
DR   RefSeq; NP_055814.1; -.
DR   UniGene; Hs.524590; -.
DR   PDB; 1YZT; X-ray; 2.05 A; A/B=16-183.
DR   PDB; 1YZU; X-ray; 2.50 A; A/B=16-183.
DR   PDB; 1Z08; X-ray; 1.80 A; A/B/C/D=16-183.
DR   PDB; 1Z0I; X-ray; 2.33 A; A=16-183.
DR   PDB; 2OT3; X-ray; 2.10 A; B=16-183.
DR   PDBsum; 1YZT; -.
DR   PDBsum; 1YZU; -.
DR   PDBsum; 1Z08; -.
DR   PDBsum; 1Z0I; -.
DR   PDBsum; 2OT3; -.
DR   IntAct; Q9UL25; 3.
DR   STRING; Q9UL25; -.
DR   PeptideAtlas; Q9UL25; -.
DR   PRIDE; Q9UL25; -.
DR   Ensembl; ENST00000261263; ENSP00000261263; ENSG00000080371; Homo sapiens.
DR   GeneID; 23011; -.
DR   KEGG; hsa:23011; -.
DR   UCSC; uc001swt.1; human.
DR   CTD; 23011; -.
DR   GeneCards; GC12P070434; -.
DR   H-InvDB; HIX0010822; -.
DR   HGNC; HGNC:18263; RAB21.
DR   HPA; HPA016988; -.
DR   MIM; 612398; gene.
DR   PharmGKB; PA34111; -.
DR   HOGENOM; Q9UL25; -.
DR   HOVERGEN; Q9UL25; -.
DR   OMA; EPQAQTS; -.
DR   BRENDA; 3.6.5.2; 247.
DR   NextBio; 43928; -.
DR   ArrayExpress; Q9UL25; -.
DR   Bgee; Q9UL25; -.
DR   CleanEx; HS_RAB21; -.
DR   Genevestigator; Q9UL25; -.
DR   GermOnline; ENSG00000080371; Homo sapiens.
DR   GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
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; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR015601; Ras_Rab21-like.
DR   InterPro; IPR005225; Small_GTP_bd.
DR   PANTHER; PTHR11708:SF257; Ras_Rab21_like; 1.
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;
DR   PRODOM; Q9UL25.
DR   SWISS-2DPAGE; Q9UL25.
KW   3D-structure; Acetylation; Complete proteome; Cytoplasmic vesicle;
KW   Direct protein sequencing; Endoplasmic reticulum; Endosome;
KW   Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation; Protein transport; Transport.
FT   DOMAIN       18    176       PRODOM:2005.1:PD000015  2217
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    222       Ras-related protein Rab-21.
FT                                /FTId=PRO_0000121205.
FT   PROPEP      223    225       Removed in mature form (Potential).
FT                                /FTId=PRO_0000370768.
FT   NP_BIND      26     33       GTP (By similarity).
FT   NP_BIND      74     78       GTP (By similarity).
FT   NP_BIND     132    135       GTP (By similarity).
FT   MOTIF        48     56       Effector region (By similarity).
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES     222    222       Cysteine methyl ester (Potential).
FT   LIPID       221    221       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       222    222       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   MUTAGEN      33     33       T->N: Defects in GTP-binding.
FT   MUTAGEN      78     78       Q->L: Defects in GTP hydrolysis.
FT   STRAND       18     25
FT   HELIX        32     41
FT   STRAND       55     63
FT   STRAND       66     74
FT   STRAND       93    100
FT   HELIX       104    121
FT   HELIX       122    124
FT   STRAND      125    132
FT   HELIX       134    139
FT   HELIX       144    153
FT   STRAND      157    160
FT   TURN        163    166
FT   HELIX       169    182
SQ   SEQUENCE   225 AA;  24348 MW;  73CA2C127F0CBFD6 CRC64;
     MAAAGGGGGG AAAAGRAYSF KVVLLGEGCV GKTSLVLRYC ENKFNDKHIT TLQASFLTKK
     LNIGGKRVNL AIWDTAGQER FHALGPIYYR DSNGAILVYD ITDEDSFQKV KNWVKELRKM
     LGNEICLCIV GNKIDLEKER HVSIQEAESY AESVGAKHYH TSAKQNKGIE ELFLDLCKRM
     IETAQVDERA KGNGSSQPGT ARRGVQIIDD EPQAQTSGGG CCSSG
//

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