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Ras-related protein Rab-32

 RAB32_HUMAN             Reviewed;         225 AA.
Q13637;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 162.
RecName: Full=Ras-related protein Rab-32;
Name=RAB32;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Burke S., Seabra M.C.;
"Cloning of novel Rab proteins with the yeast two-hybrid system.";
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[6]
PROTEIN SEQUENCE OF 2-22; 28-38; 66-72; 77-87; 111-119; 128-144;
164-186 AND 211-217, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Platelet;
Bienvenut W.V., Claeys D.;
Submitted (NOV-2005) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 16-225, TISSUE SPECIFICITY, AND
MUTAGENESIS OF GLN-85.
TISSUE=Platelet;
PubMed=11784320; DOI=10.1046/j.0014-2956.2001.02645.x;
Bao X., Faris A.E., Jang E.K., Haslam R.J.;
"Molecular cloning, bacterial expression and properties of Rab31 and
Rab32.";
Eur. J. Biochem. 269:259-271(2002).
[8]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
THR-39; ALA-185 AND LEU-188.
PubMed=12186851; DOI=10.1083/jcb.200204081;
Alto N.M., Soderling J., Scott J.D.;
"Rab32 is an A-kinase anchoring protein and participates in
mitochondrial dynamics.";
J. Cell Biol. 158:659-668(2002).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
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).
[12]
INTERACTION WITH ANKRD27, AND ENZYME REGULATION.
PubMed=21808068; DOI=10.1074/jbc.M111.261115;
Nottingham R.M., Ganley I.G., Barr F.A., Lambright D.G., Pfeffer S.R.;
"RUTBC1 protein, a Rab9A effector that activates GTP hydrolysis by
Rab32 and Rab33B proteins.";
J. Biol. Chem. 286:33213-33222(2011).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21255211; DOI=10.1111/j.1600-0854.2011.01165.x;
Seto S., Tsujimura K., Koide Y.;
"Rab GTPases regulating phagosome maturation are differentially
recruited to mycobacterial phagosomes.";
Traffic 12:407-420(2011).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23084991; DOI=10.1016/j.cub.2012.09.020;
Gerondopoulos A., Langemeyer L., Liang J.R., Linford A., Barr F.A.;
"BLOC-3 mutated in Hermansky-Pudlak syndrome is a Rab32/38 guanine
nucleotide exchange factor.";
Curr. Biol. 22:2135-2139(2012).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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).
[18]
ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE.
PubMed=25489052; DOI=10.1093/hmg/ddu611;
Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K.,
Arnesen T.;
"Biochemical and cellular analysis of Ogden syndrome reveals
downstream Nt-acetylation defects.";
Hum. Mol. Genet. 24:1956-1976(2015).
[19]
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).
[20]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-225 IN COMPLEX WITH
ANKRD27, AND MUTAGENESIS OF GLY-89; ASN-90; MET-91; ARG-93 AND VAL-94.
PubMed=24856514; DOI=10.1016/j.devcel.2014.04.010;
Hesketh G.G., Perez-Dorado I., Jackson L.P., Wartosch L.,
Schafer I.B., Gray S.R., McCoy A.J., Zeldin O.B., Garman E.F.,
Harbour M.E., Evans P.R., Seaman M.N., Luzio J.P., Owen D.J.;
"VARP is recruited on to endosomes by direct interaction with
retromer, where together they function in export to the cell
surface.";
Dev. Cell 29:591-606(2014).
-!- FUNCTION: Acts as an A-kinase anchoring protein by binding to the
type II regulatory subunit of protein kinase A and anchoring it to
the mitochondrion. Also involved in synchronization of
mitochondrial fission (PubMed:12186851). Plays a role in the
maturation of phagosomes that engulf pathogens, such as S.aureus
and M.tuberculosis (PubMed:21255211). Plays an important role in
the control of melanin production and melanosome biogenesis
(PubMed:23084991). In concert with RAB38, regulates the proper
trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to
melanosomes in melanocytes (By similarity).
{ECO:0000250|UniProtKB:Q9CZE3, ECO:0000269|PubMed:12186851,
ECO:0000269|PubMed:21255211, ECO:0000269|PubMed:23084991}.
-!- ENZYME REGULATION: Regulated by a guanine nucleotide-exchange
factor (GEF) and a GTPase-activating protein (GAP) and alternates
between an inactive GDP-bound and an active GTP-bound form. The
BLOC-3 complex composed of HPS1 and HPS4 acts as its GEF, promotes
the exchange of GDP to GTP, converting it from an inactive GDP-
bound form into an active GTP-bound form (By similarity). SGSM2
acts as its GAP and inactivates it by stimulating its GTPase
activity (PubMed:21269460). {ECO:0000250|UniProtKB:Q9CZE3}.
-!- SUBUNIT: Interacts with ANKRD27 (PubMed:24856514,
PubMed:21269460). A decreased interaction with ANKRD27 seen in the
presence of SGSM2 (PubMed:21269460).
{ECO:0000269|PubMed:24856514}.
-!- INTERACTION:
Q96D03:DDIT4L; NbExp=4; IntAct=EBI-9837586, EBI-742054;
Q5S007:LRRK2; NbExp=6; IntAct=EBI-9837586, EBI-5323863;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12186851}.
Mitochondrion outer membrane {ECO:0000269|PubMed:23084991,
ECO:0000305|PubMed:12186851}; Lipid-anchor
{ECO:0000305|PubMed:12186851}. Cytoplasmic vesicle, phagosome
{ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome
membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic
side {ECO:0000305}. Melanosome {ECO:0000250|UniProtKB:Q9CZE3}.
Melanosome membrane {ECO:0000269|PubMed:23084991}. Note=Recruited
to phagosomes containing S.aureus or M.tuberculosis
(PubMed:21255211). The BLOC-3 complex, a heterodimer of HPS1 and
HPS4 promotes its membrane localization (PubMed:23084991).
{ECO:0000269|PubMed:21255211, ECO:0000269|PubMed:23084991}.
-!- TISSUE SPECIFICITY: Widely expressed with high levels in heart,
liver, kidney, bone marrow, testis, colon and fetal lung.
{ECO:0000269|PubMed:11784320, ECO:0000269|PubMed:12186851}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
{ECO:0000305}.
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EMBL; U71127; AAB09599.1; -; mRNA.
EMBL; AF498958; AAM21106.1; -; mRNA.
EMBL; BT020016; AAV38819.1; -; mRNA.
EMBL; AL133539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC015061; AAH15061.1; -; mRNA.
EMBL; U59878; AAB02833.1; -; mRNA.
CCDS; CCDS5210.1; -.
RefSeq; NP_006825.1; NM_006834.4.
UniGene; Hs.287714; -.
PDB; 4CYM; X-ray; 2.80 A; A/B/C=1-225.
PDB; 4CZ2; X-ray; 2.97 A; A/B/C=1-225.
PDBsum; 4CYM; -.
PDBsum; 4CZ2; -.
ProteinModelPortal; Q13637; -.
SMR; Q13637; -.
BioGrid; 116177; 26.
DIP; DIP-61889N; -.
IntAct; Q13637; 21.
STRING; 9606.ENSP00000356465; -.
iPTMnet; Q13637; -.
PhosphoSitePlus; Q13637; -.
BioMuta; RAB32; -.
DMDM; 2833245; -.
EPD; Q13637; -.
MaxQB; Q13637; -.
PaxDb; Q13637; -.
PeptideAtlas; Q13637; -.
PRIDE; Q13637; -.
DNASU; 10981; -.
Ensembl; ENST00000367495; ENSP00000356465; ENSG00000118508.
GeneID; 10981; -.
KEGG; hsa:10981; -.
UCSC; uc003qln.2; human.
CTD; 10981; -.
DisGeNET; 10981; -.
EuPathDB; HostDB:ENSG00000118508.4; -.
GeneCards; RAB32; -.
HGNC; HGNC:9772; RAB32.
HPA; HPA025731; -.
MIM; 612906; gene.
neXtProt; NX_Q13637; -.
OpenTargets; ENSG00000118508; -.
PharmGKB; PA34123; -.
eggNOG; KOG4423; Eukaryota.
eggNOG; ENOG410YITC; LUCA.
GeneTree; ENSGT00760000119125; -.
HOGENOM; HOG000233968; -.
HOVERGEN; HBG009351; -.
InParanoid; Q13637; -.
KO; K07918; -.
OMA; CDQKKDS; -.
OrthoDB; EOG091G0K53; -.
PhylomeDB; Q13637; -.
TreeFam; TF324491; -.
Reactome; R-HSA-8873719; RAB geranylgeranylation.
Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
GenomeRNAi; 10981; -.
PRO; PR:Q13637; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000118508; -.
CleanEx; HS_RAB32; -.
Genevisible; Q13637; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005769; C:early endosome; IDA:ParkinsonsUK-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0044233; C:ER-mitochondrion membrane contact site; IDA:ParkinsonsUK-UCL.
GO; GO:0042470; C:melanosome; IDA:ParkinsonsUK-UCL.
GO; GO:0033162; C:melanosome membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
GO; GO:0035650; F:AP-1 adaptor complex binding; IPI:ParkinsonsUK-UCL.
GO; GO:0035651; F:AP-3 adaptor complex binding; IPI:ParkinsonsUK-UCL.
GO; GO:0036461; F:BLOC-2 complex binding; IPI:ParkinsonsUK-UCL.
GO; GO:0005525; F:GTP binding; NAS:ParkinsonsUK-UCL.
GO; GO:0030742; F:GTP-dependent protein binding; IPI:ParkinsonsUK-UCL.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0019882; P:antigen processing and presentation; IMP:UniProtKB.
GO; GO:0035646; P:endosome to melanosome transport; IMP:ParkinsonsUK-UCL.
GO; GO:1903232; P:melanosome assembly; IDA:UniProtKB.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0007005; P:mitochondrion organization; IMP:ParkinsonsUK-UCL.
GO; GO:0090382; P:phagosome maturation; IMP:UniProtKB.
GO; GO:0072657; P:protein localization to membrane; IMP:ParkinsonsUK-UCL.
GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
CDD; cd04107; Rab32_Rab38; 1.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR030697; Rab29/Rab38/Rab32.
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; Complete proteome; Cytoplasmic vesicle;
Direct protein sequencing; GTP-binding; Lipoprotein; Membrane;
Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
Phosphoprotein; Prenylation; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000269|PubMed:25489052,
ECO:0000269|Ref.6}.
CHAIN 2 225 Ras-related protein Rab-32.
/FTId=PRO_0000121235.
NP_BIND 32 39 GTP. {ECO:0000250}.
NP_BIND 81 85 GTP. {ECO:0000250}.
NP_BIND 143 146 GTP. {ECO:0000250}.
REGION 178 197 PKA-RII subunit binding domain.
MOTIF 54 62 Effector region. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895,
ECO:0000269|PubMed:25489052,
ECO:0000269|Ref.6}.
MOD_RES 71 71 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
LIPID 224 224 S-geranylgeranyl cysteine. {ECO:0000250}.
LIPID 225 225 S-geranylgeranyl cysteine. {ECO:0000250}.
MUTAGEN 39 39 T->N: Decreased GTP-binding activity.
{ECO:0000269|PubMed:12186851}.
MUTAGEN 85 85 Q->L: No change in GTPase activity.
{ECO:0000269|PubMed:11784320}.
MUTAGEN 89 89 G->T: Impairs interaction with ANKRD27;
when associated with S-90 and L-94.
{ECO:0000269|PubMed:24856514}.
MUTAGEN 90 90 N->S: Impairs interaction with ANKRD27;
when associated with T-89 and L-94.
{ECO:0000269|PubMed:24856514}.
MUTAGEN 91 91 M->S: Impairs interaction with ANKRD27;
when associated with S-93.
{ECO:0000269|PubMed:24856514}.
MUTAGEN 93 93 R->S: Impairs interaction with ANKRD27;
when associated with M-91.
{ECO:0000269|PubMed:24856514}.
MUTAGEN 94 94 V->L: Impairs interaction with ANKRD27;
when associated with T-89 and S-90.
{ECO:0000269|PubMed:24856514}.
MUTAGEN 185 185 A->F: Abolishes binding to protein kinase
A type II regulatory subunit.
{ECO:0000269|PubMed:12186851}.
MUTAGEN 188 188 L->P: Abolishes binding to protein kinase
A type II regulatory subunit.
{ECO:0000269|PubMed:12186851}.
STRAND 23 31 {ECO:0000244|PDB:4CYM}.
HELIX 38 47 {ECO:0000244|PDB:4CYM}.
STRAND 59 68 {ECO:0000244|PDB:4CYM}.
STRAND 70 72 {ECO:0000244|PDB:4CYM}.
STRAND 74 82 {ECO:0000244|PDB:4CYM}.
HELIX 84 88 {ECO:0000244|PDB:4CYM}.
HELIX 92 96 {ECO:0000244|PDB:4CYM}.
STRAND 101 107 {ECO:0000244|PDB:4CYM}.
HELIX 111 115 {ECO:0000244|PDB:4CYM}.
HELIX 117 127 {ECO:0000244|PDB:4CYM}.
STRAND 138 143 {ECO:0000244|PDB:4CYM}.
HELIX 155 164 {ECO:0000244|PDB:4CYM}.
STRAND 167 174 {ECO:0000244|PDB:4CYM}.
TURN 175 178 {ECO:0000244|PDB:4CYM}.
HELIX 181 195 {ECO:0000244|PDB:4CYM}.
SEQUENCE 225 AA; 24997 MW; 91D41BAC1E3434CA CRC64;
MAGGGAGDPG LGAAAAPAPE TREHLFKVLV IGELGVGKTS IIKRYVHQLF SQHYRATIGV
DFALKVLNWD SRTLVRLQLW DIAGQERFGN MTRVYYKEAV GAFVVFDISR SSTFEAVLKW
KSDLDSKVHL PNGSPIPAVL LANKCDQNKD SSQSPSQVDQ FCKEHGFAGW FETSAKDNIN
IEEAARFLVE KILVNHQSFP NEENDVDKIK LDQETLRAEN KSQCC


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18-003-43154 SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related - SMARCE1-related protein; HMG domain protein HMG20B; Structural DNA-binding protein BRAF35; BRCA2 0.05 mg Aff Pur
EIAAB30633 Homo sapiens,Human,Peroxin-5-related protein,Peroxisome biogenesis factor 5-like,PEX2-related protein,PEX5L,PEX5-like protein,PEX5R,PEX5-related protein,Pex5Rp,PXR2
EIAAB33504 Homo sapiens,Human,RAB34,RAB39,RAH,Ras-related protein Rab-34,Ras-related protein Rab-39,Ras-related protein Rah
EIAAB33569 Rab7,Rab7a,Ras-related protein BRL-RAS,Ras-related protein p23,Ras-related protein Rab-7a,Rat,Rattus norvegicus
EIAAB32961 Parathion hydrolase-related protein,Phosphotriesterase-related protein,Pter,Rat,Rattus norvegicus,Resiniferotoxin-binding phosphotriesterase-related protein,Rpr-1
EIAAB30632 Mouse,Mus musculus,Peroxin-5-related protein,Pex2,PEX2-related protein,Pex5l,PEX5-like protein,Pex5r,PEX5-related protein,Pex5Rp,Pxr2
20-272-191608 Tyrosinase Related Protein 75 - Mouse monoclonal [3F388] to Tyrosinase Related Protein 75; EC 1.14.18.-; DHICA oxidase; Tyrosinase-related protein 1; TRP-1; TRP1; TRP; Catalase B; Glycoprotein 75; Mel 0.05 ml
EIAAB38042 Frizzled-related protein 1b,FRP1B,FRP-1b,Homo sapiens,Human,SARP3,SARP-3,Secreted apoptosis-related protein 3,Secreted frizzled-related protein 5,SFRP5,sFRP-5
EIAAB46352 Homo sapiens,Human,PP10631,WAS_WASL-interacting protein family member 2,WASP-interacting protein-related protein,WICH,WIP- and CR16-homologous protein,WIPF2,WIP-related protein,WIRE
EIAAB12793 ELK3,ETS domain-containing protein Elk-3,ETS-related protein ERP,ETS-related protein NET,Homo sapiens,Human,NET,SAP2,SAP-2,Serum response factor accessory protein 2,SRF accessory protein 2
EIAAB08778 COX7A2L,COX7AR,COX7a-related protein,COX7RP,Cytochrome c oxidase subunit 7A-related protein, mitochondrial,Cytochrome c oxidase subunit VIIa-related protein,EB1,Homo sapiens,Human
EIAAB29234 Homo sapiens,Human,KIAA0772,ORP2,ORP-2,OSBPL2,OSBP-related protein 2,Oxysterol-binding protein-related protein 2
EIAAB29227 Homo sapiens,Human,ORP10,ORP-10,OSBP9,OSBPL10,OSBP-related protein 10,Oxysterol-binding protein-related protein 10
EIAAB29244 Homo sapiens,Human,ORP9,ORP-9,OSBP4,OSBPL9,OSBP-related protein 9,Oxysterol-binding protein-related protein 9
EIAAB29228 Homo sapiens,Human,ORP11,ORP-11,OSBP12,OSBPL11,OSBP-related protein 11,Oxysterol-binding protein-related protein 11
EIAAB33753 C21KG,G-22K,GTP-binding protein smg p21A,Homo sapiens,Human,KREV1,RAP1A,Ras-related protein Krev-1,Ras-related protein Rap-1A
EIAAB29236 Homo sapiens,Human,KIAA0704,ORP3,ORP-3,OSBP3,OSBPL3,OSBP-related protein 3,Oxysterol-binding protein-related protein 3
EIAAB29242 Homo sapiens,Human,KIAA1451,ORP8,ORP-8,OSBP10,OSBPL8,OSBP-related protein 8,Oxysterol-binding protein-related protein 8
EIAAB29231 Homo sapiens,Human,ORP1,ORP-1,OSBP8,OSBPL1,OSBPL1A,OSBPL1B,OSBP-related protein 1,Oxysterol-binding protein-related protein 1
18-003-42229 Hairy_enhancer-of-split related with YRPW motif 1 - Hairy and enhancer of split-related protein 1; HESR-1; Cardiovascular helix-loop-helix factor 2; HES-related repressor protein 2; HERP2 Polyclonal 0.1 mg Protein A
15-288-22161 Hairy_enhancer-of-split related with YRPW motif 1 - Hairy and enhancer of split-related protein 1; HESR-1; Cardiovascular helix-loop-helix factor 2; HES-related repressor protein 2; HERP2 Polyclonal 0.05 mg
15-288-22161 Hairy_enhancer-of-split related with YRPW motif 1 - Hairy and enhancer of split-related protein 1; HESR-1; Cardiovascular helix-loop-helix factor 2; HES-related repressor protein 2; HERP2 Polyclonal 0.1 mg
EIAAB29240 Homo sapiens,Human,ORP6,ORP-6,OSBPL6,OSBP-related protein 6,Oxysterol-binding protein-related protein 6
EIAAB29241 Homo sapiens,Human,ORP7,ORP-7,OSBPL7,OSBP-related protein 7,Oxysterol-binding protein-related protein 7


 

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