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RAB41_HUMAN
ID   RAB41_HUMAN             Reviewed;         222 AA.
AC   Q5JT25; Q17RQ0;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Ras-related protein Rab-41;
GN   Name=RAB41;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=15018353; DOI=10.1080/10425170310001617902;
RA   Guo J.H., Chen L., Chen S., Liu X., Saiyin H., Deng Q., Zhuang Y., Wan B.,
RA   Yu L., Zhao S.Y.;
RT   "Isolation, expression pattern of a novel human RAB gene RAB41 and
RT   characterization of its intronless homolog RAB41P.";
RL   DNA Seq. 14:431-435(2003).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=23936529; DOI=10.1371/journal.pone.0071886;
RA   Liu S., Hunt L., Storrie B.;
RT   "Rab41 is a novel regulator of Golgi apparatus organization that is needed
RT   for ER-to-Golgi trafficking and cell growth.";
RL   PLoS ONE 8:E71886-E71886(2013).
CC   -!- FUNCTION: Required for normal Golgi ribbon organization and ER-to-Golgi
CC       trafficking. {ECO:0000269|PubMed:23936529}.
CC   -!- INTERACTION:
CC       Q5JT25; Q04864: REL; NbExp=3; IntAct=EBI-10244509, EBI-307352;
CC       Q5JT25; P15884: TCF4; NbExp=3; IntAct=EBI-10244509, EBI-533224;
CC       Q5JT25-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12315199, EBI-16439278;
CC       Q5JT25-2; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-12315199, EBI-742388;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23936529}.
CC       Note=punctate localization concentrated in ruffled regions at the cell
CC       periphery.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5JT25-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5JT25-2; Sequence=VSP_037051;
CC   -!- TISSUE SPECIFICITY: Widely expressed in brain, testis, lung, heart,
CC       ovary, colon, kidney, uterus and spleen but not in liver.
CC       {ECO:0000269|PubMed:15018353}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AL357752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC117239; AAI17240.1; -; mRNA.
DR   CCDS; CCDS35322.2; -. [Q5JT25-2]
DR   CCDS; CCDS87756.1; -. [Q5JT25-1]
DR   RefSeq; NP_001027898.2; NM_001032726.2. [Q5JT25-2]
DR   RefSeq; XP_016884977.1; XM_017029488.1.
DR   AlphaFoldDB; Q5JT25; -.
DR   SMR; Q5JT25; -.
DR   BioGRID; 131446; 7.
DR   IntAct; Q5JT25; 7.
DR   STRING; 9606.ENSP00000276066; -.
DR   iPTMnet; Q5JT25; -.
DR   PhosphoSitePlus; Q5JT25; -.
DR   BioMuta; RAB41; -.
DR   jPOST; Q5JT25; -.
DR   MassIVE; Q5JT25; -.
DR   MaxQB; Q5JT25; -.
DR   PaxDb; Q5JT25; -.
DR   PeptideAtlas; Q5JT25; -.
DR   PRIDE; Q5JT25; -.
DR   ProteomicsDB; 63193; -. [Q5JT25-1]
DR   ProteomicsDB; 63194; -. [Q5JT25-2]
DR   Antibodypedia; 422; 167 antibodies from 28 providers.
DR   DNASU; 347517; -.
DR   Ensembl; ENST00000276066.4; ENSP00000276066.4; ENSG00000147127.8. [Q5JT25-2]
DR   Ensembl; ENST00000374473.6; ENSP00000363597.2; ENSG00000147127.8. [Q5JT25-1]
DR   GeneID; 347517; -.
DR   KEGG; hsa:347517; -.
DR   MANE-Select; ENST00000374473.6; ENSP00000363597.2; NM_001363807.1; NP_001350736.1.
DR   UCSC; uc010nkv.3; human. [Q5JT25-1]
DR   CTD; 347517; -.
DR   DisGeNET; 347517; -.
DR   GeneCards; RAB41; -.
DR   HGNC; HGNC:18293; RAB41.
DR   HPA; ENSG00000147127; Tissue enriched (retina).
DR   neXtProt; NX_Q5JT25; -.
DR   PharmGKB; PA34140; -.
DR   VEuPathDB; HostDB:ENSG00000147127; -.
DR   eggNOG; KOG0094; Eukaryota.
DR   GeneTree; ENSGT00940000163684; -.
DR   HOGENOM; CLU_041217_10_2_1; -.
DR   InParanoid; Q5JT25; -.
DR   OMA; GNRSYCS; -.
DR   OrthoDB; 1277051at2759; -.
DR   PhylomeDB; Q5JT25; -.
DR   TreeFam; TF300803; -.
DR   PathwayCommons; Q5JT25; -.
DR   Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR   Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR   SignaLink; Q5JT25; -.
DR   BioGRID-ORCS; 347517; 21 hits in 696 CRISPR screens.
DR   ChiTaRS; RAB41; human.
DR   GenomeRNAi; 347517; -.
DR   Pharos; Q5JT25; Tdark.
DR   PRO; PR:Q5JT25; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q5JT25; protein.
DR   Bgee; ENSG00000147127; Expressed in substantia nigra and 95 other tissues.
DR   ExpressionAtlas; Q5JT25; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; GTP-binding; Lipoprotein;
KW   Nucleotide-binding; Prenylation; Reference proteome.
FT   CHAIN           1..222
FT                   /note="Ras-related protein Rab-41"
FT                   /id="PRO_0000244618"
FT   MOTIF           60..68
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         38..45
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         86..90
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         144..147
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           222
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         42
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_037051"
SQ   SEQUENCE   222 AA;  25038 MW;  91F90E1749A7C39E CRC64;
     MSAFGHDEAW MEAGGFGLEA AERTEYQSLC KSKLLFLGEQ SVGKTSIISR FMYNSFGCAC
     QATVGIDFLS KTMYLEDQIV QLQLWDTAGQ ERFHSLIPSY IRDSTIAVVV YDITNINSFK
     ETDKWVEHVR AERGDDVVIM LLGNKIDLDN KRQVTAEQGE EKSRNLNVMF IETSAKTGYN
     VKKLFRRVAS ALLSTRTSPP PKEGTVEIEL ESFEESGNRS YC
 
 
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