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Ras-related protein Rab-1A (YPT1-related protein)

 RAB1A_HUMAN             Reviewed;         205 AA.
P62820; P11476; Q6FIE7; Q96N61; Q9Y3T2;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
31-JAN-2018, entry version 155.
RecName: Full=Ras-related protein Rab-1A;
AltName: Full=YPT1-related protein;
Name=RAB1A; Synonyms=RAB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2501306;
Zahraoui A., Touchot N., Chardin P., Tavitian A.;
"The human Rab genes encode a family of GTP-binding proteins related
to yeast YPT1 and SEC4 products involved in secretion.";
J. Biol. Chem. 264:12394-12401(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 2-30; 52-58; 62-72; 75-111; 176-187 AND 192-198,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Platelet;
Bienvenut W.V., Claeys D.;
Submitted (NOV-2005) to UniProtKB.
[10]
PHOSPHORYLATION BY CDK1.
PubMed=1902553; DOI=10.1038/350715a0;
Bailly E., McCaffrey M., Touchot N., Zahraoui A., Goud B., Bornens M.;
"Phosphorylation of two small GTP-binding proteins of the Rab family
by p34cdc2.";
Nature 350:715-718(1991).
[11]
ISOPRENYLATION AT CYS-204 AND CYS-205, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=7991565; DOI=10.1073/pnas.91.25.11963;
Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A.;
"Rab geranylgeranyl transferase catalyzes the geranylgeranylation of
adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A.";
Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994).
[12]
REVIEW.
PubMed=19603039; DOI=10.1038/nrm2728;
Stenmark H.;
"Rab GTPases as coordinators of vesicle traffic.";
Nat. Rev. Mol. Cell Biol. 10:513-525(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
FUNCTION, AND MUTAGENESIS OF ASN-124.
PubMed=20861236; DOI=10.1210/en.2010-0422;
Zhuang X., Adipietro K.A., Datta S., Northup J.K., Ray K.;
"Rab1 small GTP-binding protein regulates cell surface trafficking of
the human calcium-sensing receptor.";
Endocrinology 151:5114-5123(2010).
[15]
FUNCTION.
PubMed=20639577; DOI=10.1074/jbc.M110.141440;
Wang C., Yoo Y., Fan H., Kim E., Guan K.L., Guan J.L.;
"Regulation of integrin beta 1 recycling to lipid rafts by Rab1a to
promote cell migration.";
J. Biol. Chem. 285:29398-29405(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21303926; DOI=10.1242/jcs.079020;
Mukhopadhyay A., Nieves E., Che F.Y., Wang J., Jin L., Murray J.W.,
Gordon K., Angeletti R.H., Wolkoff A.W.;
"Proteomic analysis of endocytic vesicles: Rab1a regulates motility of
early endocytic vesicles.";
J. Cell Sci. 124:765-775(2011).
[18]
INTERACTION WITH L.PNEUMOPHILA ANKX, AND PHOSPHORYLATION AT SER-79.
PubMed=21822290; DOI=10.1038/nature10335;
Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.;
"Modulation of Rab GTPase function by a protein phosphocholine
transferase.";
Nature 477:103-106(2011).
[19]
INTERACTION WITH L.PNEUMOPHILA LEM3, AND PHOSPHORYLATION AT SER-79.
PubMed=22158903; DOI=10.1073/pnas.1114023109;
Tan Y., Arnold R.J., Luo Z.Q.;
"Legionella pneumophila regulates the small GTPase Rab1 activity by
reversible phosphorylcholination.";
Proc. Natl. Acad. Sci. U.S.A. 108:21212-21217(2011).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
SUBCELLULAR LOCATION, AND INTERACTION WITH GDI1.
PubMed=23815289; DOI=10.3109/09687688.2013.818725;
Kirsten M.L., Baron R.A., Seabra M.C., Ces O.;
"Rab1a and Rab5a preferentially bind to binary lipid compositions with
higher stored curvature elastic energy.";
Mol. Membr. Biol. 30:303-314(2013).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[24]
INTERACTION WITH C9ORF72.
PubMed=27334615; DOI=10.15252/embj.201694401;
Webster C.P., Smith E.F., Bauer C.S., Moller A., Hautbergue G.M.,
Ferraiuolo L., Myszczynska M.A., Higginbottom A., Walsh M.J.,
Whitworth A.J., Kaspar B.K., Meyer K., Shaw P.J., Grierson A.J.,
De Vos K.J.;
"The C9orf72 protein interacts with Rab1a and the ULK1 complex to
regulate initiation of autophagy.";
EMBO J. 35:1656-1676(2016).
[25]
X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 6-177 IN COMPLEX WITH GDP.
Structural genomics consortium (SGC);
"Crystal structure of human RAB1A in complex with GDP.";
Submitted (FEB-2009) to the PDB data bank.
[26]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 4-178 OF MUTANT ILE-124 IN
COMPLEX WITH L.PNEUMOPHILA DRRA, GTP-BINDING, SUBCELLULAR LOCATION,
AND INTERACTION WITH GDI1 AND L.PNEUMOPHILA DRRA.
PubMed=19942850; DOI=10.1038/emboj.2009.347;
Suh H.Y., Lee D.W., Lee K.H., Ku B., Choi S.J., Woo J.S., Kim Y.G.,
Oh B.H.;
"Structural insights into the dual nucleotide exchange and GDI
displacement activity of SidM/DrrA.";
EMBO J. 29:496-504(2010).
[27]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-177 IN COMPLEX WITH
L.PNEUMOPHILA DRRA, AND INTERACTION WITH GDI1 AND L.PNEUMOPHILA DRRA.
PubMed=20176951; DOI=10.1073/pnas.0914231107;
Zhu Y., Hu L., Zhou Y., Yao Q., Liu L., Shao F.;
"Structural mechanism of host Rab1 activation by the bifunctional
Legionella type IV effector SidM/DrrA.";
Proc. Natl. Acad. Sci. U.S.A. 107:4699-4704(2010).
[28]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 6-176 IN COMPLEXES WITH GDP;
ARF6; E.COLI ESPG AND S.FLEXNERI VIRA, FUNCTION, SUBCELLULAR LOCATION,
IDENTIFICATION IN A COMPLEX WITH ARF6 AND E.COLI ESPG, AND INTERACTION
WITH E.COLI ESPG AND S.FLEXNERI VIRA.
PubMed=22939626; DOI=10.1016/j.cell.2012.06.050;
Dong N., Zhu Y., Lu Q., Hu L., Zheng Y., Shao F.;
"Structurally distinct bacterial TBC-like GAPs link Arf GTPase to Rab1
inactivation to counteract host defenses.";
Cell 150:1029-1041(2012).
[29]
X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 1-176 IN COMPLEXES WITH GTP;
GDP AND L.PNEUMOPHILA LIDA, AND INTERACTION WITH L.PNEUMOPHILA LIDA.
PubMed=22416225; DOI=10.1371/journal.ppat.1002528;
Cheng W., Yin K., Lu D., Li B., Zhu D., Chen Y., Zhang H., Xu S.,
Chai J., Gu L.;
"Structural insights into a unique Legionella pneumophila effector
LidA recognizing both GDP and GTP bound Rab1 in their active state.";
PLoS Pathog. 8:E1002528-E1002528(2012).
[30]
X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS) OF 1-177 IN COMPLEX WITH GDP
AND L.DRANCOURTII LEPB, AND INTERACTION WITH L.PNEUMOPHILA AND
L.DRANCOURTII LEPB.
PubMed=23588383; DOI=10.1038/cr.2013.54;
Yu Q., Hu L., Yao Q., Zhu Y., Dong N., Wang D.C., Shao F.;
"Structural analyses of Legionella LepB reveal a new GAP fold that
catalytically mimics eukaryotic RasGAP.";
Cell Res. 23:775-787(2013).
[31]
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 4-177 IN COMPLEX WITH GDP
AND L.PNEUMOPHILA LEPB, AND INTERACTION WITH L.PNEUMOPHILA LEPB.
PubMed=23821544; DOI=10.1074/jbc.M113.470625;
Mishra A.K., Del Campo C.M., Collins R.E., Roy C.R., Lambright D.G.;
"The Legionella pneumophila GTPase activating protein LepB accelerates
Rab1 deactivation by a non-canonical hydrolytic mechanism.";
J. Biol. Chem. 288:24000-24011(2013).
-!- FUNCTION: The small GTPases Rab are key regulators of
intracellular membrane trafficking, from the formation of
transport vesicles to their fusion with membranes. Rabs cycle
between an inactive GDP-bound form and an active GTP-bound form
that is able to recruit to membranes different sets of downstream
effectors directly responsible for vesicle formation, movement,
tethering and fusion. RAB1A regulates vesicular protein transport
from the endoplasmic reticulum (ER) to the Golgi compartment and
on to the cell surface, and plays a role in IL-8 and growth
hormone secretion. Regulates the level of CASR present at the cell
membrane. Plays a role in cell adhesion and cell migration, via
its role in protein trafficking. Plays a role in autophagosome
assembly and cellular defense reactions against pathogenic
bacteria. Plays a role in microtubule-dependent protein transport
by early endosomes and in anterograde melanosome transport.
{ECO:0000269|PubMed:20639577, ECO:0000269|PubMed:20861236,
ECO:0000269|PubMed:21303926, ECO:0000269|PubMed:22939626}.
-!- SUBUNIT: May interact with YIPF5 (By similarity). Interacts with
C9orf72; the interaction mediates recruitment of RAB1A to the
ATG1/ULK1 kinase complex (PubMed:27334615). Interacts with GDI1;
this promotes dissociation from membranes (PubMed:23815289,
PubMed:20176951). {ECO:0000250|UniProtKB:P62822,
ECO:0000269|PubMed:20176951, ECO:0000269|PubMed:23815289,
ECO:0000269|PubMed:27334615}.
-!- SUBUNIT: (Microbial infection) Interacts with L.pneumophila AnkX.
{ECO:0000269|PubMed:21822290}.
-!- SUBUNIT: (Microbial infection) Interacts with L.pneumophila Lem3.
{ECO:0000269|PubMed:22158903}.
-!- SUBUNIT: (Microbial infection) Interacts with L.pneumophila LidA.
{ECO:0000269|PubMed:22416225}.
-!- SUBUNIT: (Microbial infection) Interacts with L.pneumophila DrrA;
this disrupts the interaction between RAB1A and GDI1 and promotes
the exchange of RAB1A-bound GDP with GTP.
{ECO:0000269|PubMed:19942850, ECO:0000269|PubMed:20176951}.
-!- SUBUNIT: (Microbial infection) Interacts with E.coli EspG and
S.flexneri VirA; this impairs ER to Golgi trafficking and protein
secretion. {ECO:0000269|PubMed:22939626}.
-!- SUBUNIT: (Microbial infection) Interacts with L.pneumophila and
L.drancourtii LepB; this enhances RAB1A GTPase activity.
{ECO:0000269|PubMed:23588383, ECO:0000269|PubMed:23821544}.
-!- SUBUNIT: (Microbial infection) Identified in a complex composed of
RAB1A, ARF6 and E.coli EspG. {ECO:0000269|PubMed:22939626}.
-!- INTERACTION:
Q29ST3:drrA (xeno); NbExp=3; IntAct=EBI-15666813, EBI-15838677;
Q5ZSQ3:drrA (xeno); NbExp=7; IntAct=EBI-716845, EBI-7632432;
P31150:GDI1; NbExp=2; IntAct=EBI-716845, EBI-946999;
P50395:GDI2; NbExp=2; IntAct=EBI-15666813, EBI-1049143;
Q6X1Y7:lepB (xeno); NbExp=2; IntAct=EBI-15666813, EBI-15666803;
P42345:MTOR; NbExp=4; IntAct=EBI-716845, EBI-359260;
Q01968:OCRL; NbExp=8; IntAct=EBI-716845, EBI-6148898;
Q8N122:RPTOR; NbExp=4; IntAct=EBI-716845, EBI-1567928;
-!- SUBCELLULAR LOCATION: Golgi apparatus
{ECO:0000269|PubMed:22939626}. Endoplasmic reticulum
{ECO:0000269|PubMed:22939626}. Early endosome
{ECO:0000269|PubMed:21303926}. Cytoplasm, cytosol
{ECO:0000303|PubMed:19942850}. Membrane
{ECO:0000269|PubMed:19942850, ECO:0000269|PubMed:23815289}.
Melanosome {ECO:0000250|UniProtKB:P62821}. Note=Alternates between
membrane-associated and cytosolic forms.
{ECO:0000303|PubMed:19942850}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P62820-1, P11476-1;
Sequence=Displayed;
Name=2;
IsoId=P62820-2, P11476-2;
Sequence=VSP_005525;
Note=No experimental confirmation available.;
Name=3;
IsoId=P62820-3, P11476-3;
Sequence=VSP_005526;
-!- PTM: Phosphorylated by CDK1 kinase during mitosis.
{ECO:0000269|PubMed:1902553, ECO:0000269|PubMed:21822290,
ECO:0000269|PubMed:22158903}.
-!- PTM: Phosphocholinated at Ser-79 by L.pneumophila AnkX, leading to
displace GDP dissociation inhibitors (GDI). Both GDP-bound and
GTP-bound forms can be phosphocholinated. Dephosphocholinated by
L.pneumophila Lem3, restoring accessibility to L.pneumophila
GTPase effector LepB.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
{ECO:0000305}.
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EMBL; M28209; AAA60240.1; -; mRNA.
EMBL; AL050268; CAB43369.1; -; mRNA.
EMBL; BX571747; CAE11872.1; -; mRNA.
EMBL; AK055927; BAB71048.1; -; mRNA.
EMBL; AF498929; AAM21077.1; -; mRNA.
EMBL; CR533479; CAG38510.1; -; mRNA.
EMBL; CH471053; EAW99921.1; -; Genomic_DNA.
EMBL; BC000905; AAH00905.1; -; mRNA.
CCDS; CCDS46305.1; -. [P62820-3]
CCDS; CCDS46306.1; -.
PIR; A34323; TVHUYP.
RefSeq; NP_004152.1; NM_004161.4. [P62820-1]
RefSeq; NP_056358.1; NM_015543.1. [P62820-3]
UniGene; Hs.310645; -.
PDB; 2FOL; X-ray; 2.63 A; A=6-177.
PDB; 2WWX; X-ray; 1.50 A; A=4-178.
PDB; 3L0I; X-ray; 2.85 A; B/D=1-177.
PDB; 3SFV; X-ray; 1.73 A; A=1-176.
PDB; 3TKL; X-ray; 2.18 A; A=1-191.
PDB; 4FMB; X-ray; 3.20 A; B/D/F=6-176.
PDB; 4FMC; X-ray; 2.80 A; B/D=6-176, F=14-115.
PDB; 4FMD; X-ray; 3.05 A; B/D=6-176, F=13-176.
PDB; 4FME; X-ray; 4.10 A; B/E=6-176.
PDB; 4IRU; X-ray; 3.20 A; B/D/F=4-177.
PDB; 4JVS; X-ray; 2.78 A; B=1-177.
PDBsum; 2FOL; -.
PDBsum; 2WWX; -.
PDBsum; 3L0I; -.
PDBsum; 3SFV; -.
PDBsum; 3TKL; -.
PDBsum; 4FMB; -.
PDBsum; 4FMC; -.
PDBsum; 4FMD; -.
PDBsum; 4FME; -.
PDBsum; 4IRU; -.
PDBsum; 4JVS; -.
ProteinModelPortal; P62820; -.
SMR; P62820; -.
BioGrid; 111799; 163.
DIP; DIP-1063N; -.
IntAct; P62820; 52.
MINT; MINT-1343792; -.
STRING; 9606.ENSP00000387286; -.
iPTMnet; P62820; -.
PhosphoSitePlus; P62820; -.
SwissPalm; P62820; -.
BioMuta; RAB1A; -.
DMDM; 51338603; -.
EPD; P62820; -.
PaxDb; P62820; -.
PeptideAtlas; P62820; -.
PRIDE; P62820; -.
DNASU; 5861; -.
Ensembl; ENST00000398529; ENSP00000381540; ENSG00000138069. [P62820-3]
Ensembl; ENST00000409784; ENSP00000387286; ENSG00000138069. [P62820-1]
Ensembl; ENST00000409892; ENSP00000386451; ENSG00000138069. [P62820-2]
GeneID; 5861; -.
KEGG; hsa:5861; -.
UCSC; uc002sdn.4; human.
CTD; 5861; -.
DisGeNET; 5861; -.
EuPathDB; HostDB:ENSG00000138069.16; -.
GeneCards; RAB1A; -.
HGNC; HGNC:9758; RAB1A.
HPA; CAB005331; -.
HPA; HPA056141; -.
MIM; 179508; gene.
neXtProt; NX_P62820; -.
OpenTargets; ENSG00000138069; -.
PharmGKB; PA34107; -.
eggNOG; KOG0084; Eukaryota.
eggNOG; ENOG410XQN5; LUCA.
GeneTree; ENSGT00900000140786; -.
HOGENOM; HOG000233968; -.
HOVERGEN; HBG009351; -.
InParanoid; P62820; -.
KO; K07874; -.
OMA; VTDNDTF; -.
OrthoDB; EOG091G0LA6; -.
PhylomeDB; P62820; -.
TreeFam; TF300097; -.
Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
Reactome; R-HSA-204005; COPII (Coat Protein 2) Mediated Vesicle Transport.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
Reactome; R-HSA-8873719; RAB geranylgeranylation.
Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
ChiTaRS; RAB1A; human.
EvolutionaryTrace; P62820; -.
GeneWiki; RAB1A; -.
GenomeRNAi; 5861; -.
PRO; PR:P62820; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000138069; -.
CleanEx; HS_RAB1A; -.
ExpressionAtlas; P62820; baseline and differential.
Genevisible; P62820; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
GO; GO:0006914; P:autophagy; IMP:UniProtKB.
GO; GO:0090110; P:cargo loading into COPII-coated vesicle; IMP:UniProtKB.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IMP:UniProtKB.
GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
GO; GO:0030252; P:growth hormone secretion; IMP:UniProtKB.
GO; GO:0072606; P:interleukin-8 secretion; IMP:UniProtKB.
GO; GO:0032402; P:melanosome transport; IEA:Ensembl.
GO; GO:1903020; P:positive regulation of glycoprotein metabolic process; IGI:UniProtKB.
GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
GO; GO:0047496; P:vesicle transport along microtubule; IMP:UniProtKB.
GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
GO; GO:0019068; P:virion assembly; IMP:UniProtKB.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51419; RAB; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Autophagy;
Complete proteome; Cytoplasm; Direct protein sequencing;
Endoplasmic reticulum; Endosome; ER-Golgi transport; Golgi apparatus;
GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
Phosphoprotein; Prenylation; Protein transport; Reference proteome;
Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.9}.
CHAIN 2 205 Ras-related protein Rab-1A.
/FTId=PRO_0000121056.
NP_BIND 18 26 GTP. {ECO:0000244|PDB:2FOL,
ECO:0000244|PDB:3SFV,
ECO:0000244|PDB:3TKL,
ECO:0000244|PDB:4FMB,
ECO:0000244|PDB:4FMC,
ECO:0000244|PDB:4FMD,
ECO:0000244|PDB:4FME,
ECO:0000244|PDB:4IRU,
ECO:0000244|PDB:4JVS,
ECO:0000269|PubMed:22416225,
ECO:0000269|PubMed:22939626,
ECO:0000269|PubMed:23588383,
ECO:0000269|PubMed:23821544}.
NP_BIND 36 43 GTP. {ECO:0000244|PDB:2FOL,
ECO:0000244|PDB:3SFV,
ECO:0000244|PDB:3TKL,
ECO:0000244|PDB:4FMC,
ECO:0000244|PDB:4FME,
ECO:0000244|PDB:4IRU,
ECO:0000244|PDB:4JVS,
ECO:0000269|PubMed:22416225,
ECO:0000269|PubMed:22939626,
ECO:0000269|PubMed:23588383,
ECO:0000269|PubMed:23821544}.
NP_BIND 66 70 GTP. {ECO:0000244|PDB:3TKL,
ECO:0000269|PubMed:22416225}.
NP_BIND 124 127 GTP. {ECO:0000244|PDB:2FOL,
ECO:0000244|PDB:3SFV,
ECO:0000244|PDB:3TKL,
ECO:0000244|PDB:4FMB,
ECO:0000244|PDB:4FMC,
ECO:0000244|PDB:4FMD,
ECO:0000244|PDB:4FME,
ECO:0000244|PDB:4IRU,
ECO:0000244|PDB:4JVS,
ECO:0000269|PubMed:22416225,
ECO:0000269|PubMed:22939626,
ECO:0000269|PubMed:23588383,
ECO:0000269|PubMed:23821544}.
NP_BIND 154 156 GTP. {ECO:0000244|PDB:2FOL,
ECO:0000244|PDB:3SFV,
ECO:0000244|PDB:3TKL,
ECO:0000244|PDB:4FMB,
ECO:0000244|PDB:4FMC,
ECO:0000244|PDB:4FMD,
ECO:0000244|PDB:4FME,
ECO:0000244|PDB:4IRU,
ECO:0000244|PDB:4JVS,
ECO:0000269|PubMed:22416225,
ECO:0000269|PubMed:22939626,
ECO:0000269|PubMed:23588383,
ECO:0000269|PubMed:23821544}.
MOTIF 40 48 Effector region. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.9}.
MOD_RES 79 79 O-(2-cholinephosphoryl)serine.
{ECO:0000269|PubMed:21822290,
ECO:0000269|PubMed:22158903}.
MOD_RES 194 194 Phosphoserine; by CDK1.
{ECO:0000305|PubMed:1902553}.
LIPID 204 204 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:7991565}.
LIPID 205 205 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:7991565}.
VAR_SEQ 33 96 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_005525.
VAR_SEQ 65 140 Missing (in isoform 3).
{ECO:0000303|PubMed:11230166,
ECO:0000303|Ref.6}.
/FTId=VSP_005526.
MUTAGEN 124 124 N->I: Dominant negative mutant. Strongly
reduces the levels of CASR present at the
cell-surface.
{ECO:0000269|PubMed:20861236}.
STRAND 10 17 {ECO:0000244|PDB:2WWX}.
HELIX 24 28 {ECO:0000244|PDB:2WWX}.
STRAND 30 32 {ECO:0000244|PDB:3L0I}.
HELIX 39 44 {ECO:0000244|PDB:2WWX}.
STRAND 47 55 {ECO:0000244|PDB:2WWX}.
STRAND 58 65 {ECO:0000244|PDB:2WWX}.
HELIX 70 72 {ECO:0000244|PDB:2WWX}.
HELIX 78 80 {ECO:0000244|PDB:2WWX}.
TURN 81 83 {ECO:0000244|PDB:3SFV}.
STRAND 85 92 {ECO:0000244|PDB:2WWX}.
HELIX 96 112 {ECO:0000244|PDB:2WWX}.
STRAND 117 125 {ECO:0000244|PDB:2WWX}.
HELIX 129 131 {ECO:0000244|PDB:3SFV}.
HELIX 136 145 {ECO:0000244|PDB:2WWX}.
STRAND 150 154 {ECO:0000244|PDB:2WWX}.
TURN 155 157 {ECO:0000244|PDB:3SFV}.
HELIX 159 175 {ECO:0000244|PDB:2WWX}.
SEQUENCE 205 AA; 22678 MW; B2A8F4E3B0FB17D6 CRC64;
MSSMNPEYDY LFKLLLIGDS GVGKSCLLLR FADDTYTESY ISTIGVDFKI RTIELDGKTI
KLQIWDTAGQ ERFRTITSSY YRGAHGIIVV YDVTDQESFN NVKQWLQEID RYASENVNKL
LVGNKCDLTT KKVVDYTTAK EFADSLGIPF LETSAKNATN VEQSFMTMAA EIKKRMGPGA
TAGGAEKSNV KIQSTPVKQS GGGCC


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