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Ras-related protein Rab-7L1 (Rab-7-like protein 1) (Ras-related protein Rab-29)

 RAB7L_HUMAN             Reviewed;         203 AA.
O14966; B4E1K3; C9JE77;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
28-FEB-2018, entry version 170.
RecName: Full=Ras-related protein Rab-7L1;
AltName: Full=Rab-7-like protein 1;
AltName: Full=Ras-related protein Rab-29;
Name=RAB29; Synonyms=RAB7L1;
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).
TISSUE=Placenta;
PubMed=9284931;
Shimizu F., Katagiri T., Suzuki M., Watanabe T.K., Okuno S., Kuga Y.,
Nagata M., Fujiwara T., Nakamura Y., Takahashi E.;
"Cloning and chromosome assignment to 1q32 of a human cDNA (RAB7L1)
encoding a small GTP-binding protein, a member of the RAS
superfamily.";
Cytogenet. Cell Genet. 77:261-263(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Thymus, and Trachea;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Ovary;
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).
[5]
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).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[7]
FUNCTION IN SALMONELLA INFECTION, CLEAVAGE BY GIFSY-2 BACTERIOPHAGE
GTGE, AND SUBCELLULAR LOCATION.
PubMed=22042847; DOI=10.1073/pnas.1111959108;
Spano S., Liu X., Galan J.E.;
"Proteolytic targeting of Rab29 by an effector protein distinguishes
the intracellular compartments of human-adapted and broad-host
Salmonella.";
Proc. Natl. Acad. Sci. U.S.A. 108:18418-18423(2011).
[8]
FUNCTION IN RETROGRADE TRANSPORT, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=24788816; DOI=10.1371/journal.pone.0096242;
Wang S., Ma Z., Xu X., Wang Z., Sun L., Zhou Y., Lin X., Hong W.,
Wang T.;
"A role of rab29 in the integrity of the trans-Golgi network and
retrograde trafficking of mannose-6-phosphate receptor.";
PLoS ONE 9:E96242-E96242(2014).
-!- FUNCTION: Rab GTPase key regulator in vesicle trafficking.
Essential for maintaining the integrity of the endosome-trans-
Golgi network structure. Together with LRRK2, plays a role in the
retrograde trafficking pathway for recycling proteins, such as
mannose 6 phosphate receptor (M6PR), between lysosomes and the
Golgi apparatus in a retromer-dependent manner. Regulates neuronal
process morphology in the intact central nervous system (CNS). May
play a role in the formation of typhoid toxin transport
intermediates during Salmonella enterica serovar Typhi (S.Typhi)
epithelial cell infection. {ECO:0000269|PubMed:22042847,
ECO:0000269|PubMed:24788816}.
-!- SUBUNIT: Interacts with LRRK2. {ECO:0000250}.
-!- INTERACTION:
Q5S007:LRRK2; NbExp=7; IntAct=EBI-372165, EBI-5323863;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm
{ECO:0000269|PubMed:24788816}. Cytoplasm, perinuclear region
{ECO:0000269|PubMed:24788816}. Golgi apparatus
{ECO:0000269|PubMed:22042847}. Golgi apparatus, trans-Golgi
network {ECO:0000269|PubMed:24788816}. Vacuole
{ECO:0000269|PubMed:22042847}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:22042847}. Note=Colocalizes with LRRK2 along
tubular structures emerging from Golgi apparatus (By similarity).
Colocalizes with GM130 at the Golgi apparatus (PubMed:22042847).
Colocalizes with dynamic tubules emerging from and retracting to
the Golgi apparatus (PubMed:22042847). Colocalizes with TGN46 at
the trans-Golgi network (TGN) (PubMed:24788816). In Salmonella
enterica serovar Typhi (S.Typhi) infected epithelial cells, is
recruited and colocalized with both S.Typhi-containing vacuoles
and dynamic tubules as well as those emerging from the vacuole
toward the cell periphery (PubMed:22042847).
{ECO:0000250|UniProtKB:Q63481, ECO:0000269|PubMed:22042847,
ECO:0000269|PubMed:24788816}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O14966-1; Sequence=Displayed;
Name=2;
IsoId=O14966-2; Sequence=VSP_043391;
Note=No experimental confirmation available.;
Name=3;
IsoId=O14966-3; Sequence=VSP_045078;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:24788816}.
-!- PTM: In case of Salmonella enterica serovar Typhimurium
(S.Typhimurium) infection, is proteolytically cleaved between Gly-
41 and Val-42 by the GtgE viral protease encoded on the Gifsy-2
lysogen bacteriophage, which therefore prevents the recruitment of
RAB29 to S.Typhimurium-containing vacuoles. In contrast, no
proteolytically cleavage is detected in S.Typhi-infected cells
(PubMed:22042847). {ECO:0000269|PubMed:22042847}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
{ECO:0000305}.
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EMBL; D84488; BAA22160.1; -; mRNA.
EMBL; AK308359; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK303879; BAG64815.1; -; mRNA.
EMBL; AC119673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002585; AAH02585.1; -; mRNA.
CCDS; CCDS1459.1; -. [O14966-1]
CCDS; CCDS44301.1; -. [O14966-2]
CCDS; CCDS44302.1; -. [O14966-3]
RefSeq; NP_001129134.1; NM_001135662.1. [O14966-1]
RefSeq; NP_001129135.1; NM_001135663.1. [O14966-2]
RefSeq; NP_001129136.1; NM_001135664.1. [O14966-3]
RefSeq; NP_003920.1; NM_003929.2. [O14966-1]
RefSeq; XP_005245626.1; XM_005245569.1. [O14966-1]
RefSeq; XP_005245627.1; XM_005245570.1. [O14966-1]
RefSeq; XP_005245628.1; XM_005245571.1. [O14966-1]
RefSeq; XP_006711668.1; XM_006711605.3. [O14966-3]
RefSeq; XP_006711669.1; XM_006711606.2. [O14966-3]
RefSeq; XP_016858237.1; XM_017002748.1. [O14966-2]
RefSeq; XP_016858238.1; XM_017002749.1. [O14966-2]
RefSeq; XP_016858239.1; XM_017002750.1. [O14966-2]
UniGene; Hs.115325; -.
ProteinModelPortal; O14966; -.
SMR; O14966; -.
BioGrid; 114447; 17.
DIP; DIP-31215N; -.
IntAct; O14966; 10.
STRING; 9606.ENSP00000235932; -.
iPTMnet; O14966; -.
PhosphoSitePlus; O14966; -.
BioMuta; RAB7L1; -.
EPD; O14966; -.
PaxDb; O14966; -.
PeptideAtlas; O14966; -.
PRIDE; O14966; -.
DNASU; 8934; -.
Ensembl; ENST00000235932; ENSP00000235932; ENSG00000117280. [O14966-1]
Ensembl; ENST00000367139; ENSP00000356107; ENSG00000117280. [O14966-1]
Ensembl; ENST00000414729; ENSP00000402910; ENSG00000117280. [O14966-1]
Ensembl; ENST00000437324; ENSP00000416613; ENSG00000117280. [O14966-3]
Ensembl; ENST00000446390; ENSP00000389899; ENSG00000117280. [O14966-2]
GeneID; 8934; -.
KEGG; hsa:8934; -.
UCSC; uc009xbp.4; human. [O14966-1]
CTD; 8934; -.
DisGeNET; 8934; -.
EuPathDB; HostDB:ENSG00000117280.12; -.
GeneCards; RAB29; -.
HGNC; HGNC:9789; RAB29.
HPA; CAB020822; -.
HPA; HPA026303; -.
MIM; 603949; gene.
neXtProt; NX_O14966; -.
OpenTargets; ENSG00000117280; -.
PharmGKB; PA34151; -.
eggNOG; KOG4423; Eukaryota.
eggNOG; ENOG410YITC; LUCA.
GeneTree; ENSGT00760000119125; -.
HOGENOM; HOG000233968; -.
HOVERGEN; HBG009351; -.
InParanoid; O14966; -.
KO; K07916; -.
OMA; QERFISM; -.
OrthoDB; EOG091G0K53; -.
PhylomeDB; O14966; -.
TreeFam; TF324491; -.
Reactome; R-HSA-8873719; RAB geranylgeranylation.
ChiTaRS; RAB29; human.
GenomeRNAi; 8934; -.
PRO; PR:O14966; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117280; -.
CleanEx; HS_RAB7L1; -.
ExpressionAtlas; O14966; baseline and differential.
Genevisible; O14966; HS.
GO; GO:0005801; C:cis-Golgi network; IDA:ParkinsonsUK-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005769; C:early endosome; IDA:ParkinsonsUK-UCL.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:ParkinsonsUK-UCL.
GO; GO:0097708; C:intracellular vesicle; IDA:ParkinsonsUK-UCL.
GO; GO:0042470; C:melanosome; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0055037; C:recycling endosome; IDA:ParkinsonsUK-UCL.
GO; GO:0020003; C:symbiont-containing vacuole; IDA:ParkinsonsUK-UCL.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
GO; GO:0070840; F:dynein complex binding; IDA:ParkinsonsUK-UCL.
GO; GO:0019003; F:GDP binding; IDA:ParkinsonsUK-UCL.
GO; GO:0005525; F:GTP binding; IDA:ParkinsonsUK-UCL.
GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
GO; GO:0019894; F:kinesin binding; IPI:ParkinsonsUK-UCL.
GO; GO:0017137; F:Rab GTPase binding; IDA:ParkinsonsUK-UCL.
GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
GO; GO:0032438; P:melanosome organization; IBA:GO_Central.
GO; GO:0007005; P:mitochondrion organization; IMP:ParkinsonsUK-UCL.
GO; GO:1990967; P:multi-organism toxin transport; IMP:ParkinsonsUK-UCL.
GO; GO:0010977; P:negative regulation of neuron projection development; IDA:ParkinsonsUK-UCL.
GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
GO; GO:0001921; P:positive regulation of receptor recycling; IMP:ParkinsonsUK-UCL.
GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IMP:ParkinsonsUK-UCL.
GO; GO:1903441; P:protein localization to ciliary membrane; ISS:ParkinsonsUK-UCL.
GO; GO:0072657; P:protein localization to membrane; IMP:ParkinsonsUK-UCL.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:1901214; P:regulation of neuron death; ISS:ParkinsonsUK-UCL.
GO; GO:1905279; P:regulation of retrograde transport, endosome to Golgi; IEA:Ensembl.
GO; GO:0009617; P:response to bacterium; IDA:ParkinsonsUK-UCL.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
GO; GO:0007416; P:synapse assembly; IMP:ParkinsonsUK-UCL.
GO; GO:0042110; P:T cell activation; IMP:ParkinsonsUK-UCL.
GO; GO:0039694; P:viral RNA genome replication; IMP:ParkinsonsUK-UCL.
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;
Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
Cytoskeleton; Differentiation; Golgi apparatus; GTP-binding;
Lipoprotein; Membrane; Nucleotide-binding; Prenylation;
Protein transport; Reference proteome; Transport; Vacuole.
CHAIN 1 203 Ras-related protein Rab-7L1.
/FTId=PRO_0000121127.
NP_BIND 14 21 GTP. {ECO:0000250}.
NP_BIND 33 39 GTP. {ECO:0000250}.
NP_BIND 63 67 GTP. {ECO:0000250}.
NP_BIND 125 128 GTP. {ECO:0000250}.
NP_BIND 156 157 GTP. {ECO:0000250}.
MOTIF 36 44 Effector region. {ECO:0000250}.
SITE 41 42 Cleavage; by S.Typhimurium viral protease
GtgE.
LIPID 202 202 S-geranylgeranyl cysteine. {ECO:0000250}.
LIPID 203 203 S-geranylgeranyl cysteine. {ECO:0000250}.
VAR_SEQ 1 72 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045078.
VAR_SEQ 42 65 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043391.
SEQUENCE 203 AA; 23155 MW; 40E7CAB02446DF97 CRC64;
MGSRDHLFKV LVVGDAAVGK TSLVQRYSQD SFSKHYKSTV GVDFALKVLQ WSDYEIVRLQ
LWDIAGQERF TSMTRLYYRD ASACVIMFDV TNATTFSNSQ RWKQDLDSKL TLPNGEPVPC
LLLANKCDLS PWAVSRDQID RFSKENGFTG WTETSVKENK NINEAMRVLI EKMMRNSTED
IMSLSTQGDY INLQTKSSSW SCC


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E1793r ELISA Calgranulin-B,Migration inhibitory factor-related protein 14,Mrp14,MRP-14,Myeloid-related protein 14,p14,Protein S100-A9,Rat,Rattus norvegicus,S100 calcium-binding protein A9,S100a9 96T
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EIAAB29234 Homo sapiens,Human,KIAA0772,ORP2,ORP-2,OSBPL2,OSBP-related protein 2,Oxysterol-binding protein-related protein 2
EIAAB29228 Homo sapiens,Human,ORP11,ORP-11,OSBP12,OSBPL11,OSBP-related protein 11,Oxysterol-binding protein-related protein 11
EIAAB29244 Homo sapiens,Human,ORP9,ORP-9,OSBP4,OSBPL9,OSBP-related protein 9,Oxysterol-binding protein-related protein 9
EIAAB29227 Homo sapiens,Human,ORP10,ORP-10,OSBP9,OSBPL10,OSBP-related protein 10,Oxysterol-binding protein-related protein 10
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
EIAAB30634 Peroxin-5-related protein,Pex2,Pex5l,PEX5-like protein,Pex5r,PEX5-related protein,Pex5Rp,Rat,Rattus norvegicus,TPR-containing Rab8b-interacting protein,Trip8b
EIAAB29231 Homo sapiens,Human,ORP1,ORP-1,OSBP8,OSBPL1,OSBPL1A,OSBPL1B,OSBP-related protein 1,Oxysterol-binding protein-related protein 1


 

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