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Protein

Rab3 GTPase-activating protein non-catalytic subunit

Gene

RAB3GAP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of a GTPase activating protein that has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones. Rab3 GTPase-activating complex specifically converts active Rab3-GTP to the inactive form Rab3-GDP. Required for normal eye and brain development. May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters.1 Publication

GO - Molecular functioni

  • enzyme activator activity Source: ProtInc
  • enzyme regulator activity Source: UniProtKB
  • GTPase activator activity Source: ProtInc
  • protein heterodimerization activity Source: UniProtKB
  • Rab GTPase binding Source: UniProtKB

GO - Biological processi

  • establishment of protein localization to endoplasmic reticulum membrane Source: UniProtKB
  • intracellular protein transport Source: ProtInc
  • positive regulation of autophagosome assembly Source: GO_Central
  • positive regulation of catalytic activity Source: GOC
  • positive regulation of endoplasmic reticulum tubular network organization Source: UniProtKB
  • positive regulation of GTPase activity Source: GOC
  • positive regulation of protein lipidation Source: GO_Central
  • regulation of GTPase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
Rab3 GTPase-activating protein non-catalytic subunit
Alternative name(s):
RGAP-iso
Rab3 GTPase-activating protein 150 kDa subunit
Rab3-GAP p150
Short name:
Rab3-GAP150
Rab3-GAP regulatory subunit
Gene namesi
Name:RAB3GAP2
Synonyms:KIAA0839
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:17168. RAB3GAP2.

Subcellular locationi

  • Cytoplasm

  • Note: In neurons, it is enriched in the synaptic soluble fraction.

GO - Cellular componenti

  • cytoplasm Source: HPA
  • plasma membrane Source: HPA
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Martsolf syndrome (MARTS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionCharacterized by congenital cataracts, mental retardation, and hypogonadism. Inheritance is autosomal recessive.
See also OMIM:212720
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1052 – 10521G → C in MARTS; may cause exon skipping. 1 Publication
VAR_029881
Warburg micro syndrome 2 (WARBM2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare syndrome characterized by microcephaly, microphthalmia, microcornia, congenital cataracts, optic atrophy, cortical dysplasia, in particular corpus callosum hypoplasia, severe mental retardation, spastic diplegia, and hypogonadism.
See also OMIM:614225
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti167 – 1693Missing in WARBM2. 1 Publication
VAR_066675

Keywords - Diseasei

Cataract, Disease mutation, Mental retardation

Organism-specific databases

MalaCardsiRAB3GAP2.
MIMi212720. phenotype.
614225. phenotype.
Orphaneti401830. Autosomal recessive spastic paraplegia type 69.
1387. Cataract - intellectual disability - hypogonadism.
2510. Micro syndrome.
PharmGKBiPA142671105.

Polymorphism and mutation databases

BioMutaiRAB3GAP2.
DMDMi62511132.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13931393Rab3 GTPase-activating protein non-catalytic subunitPRO_0000191662Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391PhosphoserineBy similarity
Modified residuei450 – 4501PhosphoserineCombined sources
Modified residuei901 – 9011PhosphothreonineCombined sources
Modified residuei978 – 9781PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9H2M9.
MaxQBiQ9H2M9.
PaxDbiQ9H2M9.
PRIDEiQ9H2M9.

PTM databases

iPTMnetiQ9H2M9.
PhosphoSiteiQ9H2M9.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9H2M9.
CleanExiHS_RAB3GAP2.
ExpressionAtlasiQ9H2M9. baseline and differential.
GenevisibleiQ9H2M9. HS.

Organism-specific databases

HPAiHPA026273.
HPA027299.

Interactioni

Subunit structurei

The Rab3 GTPase-activating complex is a heterodimer composed of RAB3GAP and RAB3-GAP150. The Rab3 GTPase-activating complex interacts with DMXL2 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PTP4A3O753651EBI-536107,EBI-1043866

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB
  • Rab GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi117317. 21 interactions.
IntActiQ9H2M9. 2 interactions.
STRINGi9606.ENSP00000351832.

Structurei

3D structure databases

ProteinModelPortaliQ9H2M9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Rab3-GAP regulatory subunit family.Curated

Phylogenomic databases

eggNOGiKOG2727. Eukaryota.
ENOG410XTJ2. LUCA.
GeneTreeiENSGT00390000005794.
HOGENOMiHOG000290717.
HOVERGENiHBG067039.
InParanoidiQ9H2M9.
KOiK19937.
OMAiWWQQMRT.
OrthoDBiEOG7TTQ71.
PhylomeDBiQ9H2M9.
TreeFamiTF314817.

Family and domain databases

InterProiIPR026059. Rab3-gap_reg.
IPR029257. RAB3GAP2_C.
IPR032839. RAB3GAP_N.
[Graphical view]
PANTHERiPTHR12472. PTHR12472. 1 hit.
PfamiPF14656. RAB3GAP2_C. 1 hit.
PF14655. RAB3GAP2_N. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H2M9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MACSIVQFCY FQDLQAARDF LFPHLREEIL SGALRRDPSK STDWEDDGWG
60 70 80 90 100
AWEENEPQEP EEEGNTCKTQ KTSWLQDCVL SLSPTNDLMV IAREQKAVFL
110 120 130 140 150
VPKWKYSDKG KEEMQFAVGW SGSLNVEEGE CVTSALCIPL ASQKRSSTGR
160 170 180 190 200
PDWTCIVVGF TSGYVRFYTE NGVLLLAQLL NEDPVLQLKC RTYEIPRHPG
210 220 230 240 250
VTEQNEELSI LYPAAIVTID GFSLFQSLRA CRNQVAKAAA SGNENIQPPP
260 270 280 290 300
LAYKKWGLQD IDTIIDHASV GIMTLSPFDQ MKTASNIGGF NAAIKNSPPA
310 320 330 340 350
MSQYITVGSN PFTGFFYALE GSTQPLLSHV ALAVASKLTS ALFNAASGWL
360 370 380 390 400
GWKSKHEEEA VQKQKPKVEP ATPLAVRFGL PDSRRHGESI CLSPCNTLAA
410 420 430 440 450
VTDDFGRVIL LDVARGIAIR MWKGYRDAQI GWIQTVEDLH ERVPEKADFS
460 470 480 490 500
PFGNSQGPSR VAQFLVIYAP RRGILEVWST QQGPRVGAFN VGKHCRLLYP
510 520 530 540 550
GYKIMGLNNV TSQSWQPQTY QICLVDPVSG SVKTVNVPFH LALSDKKSER
560 570 580 590 600
AKDMHLVKKL AALLKTKSPN LDLVETEIKE LILDIKYPAT KKQALESILA
610 620 630 640 650
SERLPFSCLR NITQTLMDTL KSQELESVDE GLLQFCANKL KLLQLYESVS
660 670 680 690 700
QLNSLDFHLD TPFSDNDLAL LLRLDEKELL KLQALLEKYK QENTRTNVRF
710 720 730 740 750
SDDKDGVLPV KTFLEYLEYE KDVLNIKKIS EEEYVALGSF FFWKCLHGES
760 770 780 790 800
STEDMCHTLE SAGLSPQLLL SLLLSVWLSK EKDILDKPQS ICCLHTMLSL
810 820 830 840 850
LSKMKVAIDE TWDSQSVSPW WQQMRTACIQ SENNGAALLS AHVGHSVAAQ
860 870 880 890 900
ISNNMTEKKF SQTVLGADSE ALTDSWEALS LDTEYWKLLL KQLEDCLILQ
910 920 930 940 950
TLLHSKGNTQ TSKVSSLQAE PLPRLSVKKL LEGGKGGIAD SVAKWIFKQD
960 970 980 990 1000
FSPEVLKLAN EERDAENPDE PKEGVNRSFL EVSEMEMDLG AIPDLLHLAY
1010 1020 1030 1040 1050
EQFPCSLELD VLHAHCCWEY VVQWNKDPEE ARFFVRSIEH LKQIFNAHVQ
1060 1070 1080 1090 1100
NGIALMMWNT FLVKRFSAAT YLMDKVGKSP KDRLCRRDVG MSDTAMTSFL
1110 1120 1130 1140 1150
GSCLDLLQIL MEADVSRDEI QVPVLDTEDA WLSVEGPISI VELALEQKHI
1160 1170 1180 1190 1200
HYPLVEHHSI LCSILYAVMR FSLKTVKPLS LFDSKGKNAF FKDLTSIQLL
1210 1220 1230 1240 1250
PSGEMDPNFI SVRQQFLLKV VSAAVQAQHS ATKVKDPTEE ATPTPFGKDQ
1260 1270 1280 1290 1300
DWPALAVDLA HHLQVSEDVV RRHYVGELYN YGVDHLGEEA ILQVHDKEVL
1310 1320 1330 1340 1350
ASQLLVLTGQ RLAHALLHTQ TKEGMELLAR LPPTLCTWLK AMDPQDLQNT
1360 1370 1380 1390
EVPIATTAKL VNKVIELLPE KHGQYGLALH LIEAVEAISL PSL
Length:1,393
Mass (Da):155,985
Last modified:March 1, 2001 - v1
Checksum:i4138F60B5199211E
GO
Isoform 2 (identifier: Q9H2M9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     205-206: NE → VV
     207-1393: Missing.

Note: No experimental confirmation available.
Show »
Length:206
Mass (Da):23,361
Checksum:iF2E1A380FC809649
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti289 – 2891G → R in AAC35881 (PubMed:9733780).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti167 – 1693Missing in WARBM2. 1 Publication
VAR_066675
Natural varianti863 – 8631T → A.
Corresponds to variant rs12045447 [ dbSNP | Ensembl ].
VAR_021588
Natural varianti1052 – 10521G → C in MARTS; may cause exon skipping. 1 Publication
VAR_029881
Natural varianti1092 – 10921S → T.
Corresponds to variant rs2289189 [ dbSNP | Ensembl ].
VAR_021589

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei205 – 2062NE → VV in isoform 2. 1 PublicationVSP_013311
Alternative sequencei207 – 13931187Missing in isoform 2. 1 PublicationVSP_013312Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004828 mRNA. Translation: AAC35881.1.
AF255648 mRNA. Translation: AAG44636.1.
AB020646 mRNA. Translation: BAA74862.2.
AK021928 mRNA. Translation: BAB13939.1.
AK291234 mRNA. Translation: BAF83923.1.
AL445435, AC103590 Genomic DNA. Translation: CAI15808.1.
CH471100 Genomic DNA. Translation: EAW93304.1.
BC146760 mRNA. Translation: AAI46761.1.
AL117631 mRNA. Translation: CAB56022.1.
CCDSiCCDS31028.1. [Q9H2M9-1]
PIRiT17332.
RefSeqiNP_036546.2. NM_012414.3. [Q9H2M9-1]
UniGeneiHs.654849.
Hs.708165.

Genome annotation databases

EnsembliENST00000358951; ENSP00000351832; ENSG00000118873. [Q9H2M9-1]
GeneIDi25782.
KEGGihsa:25782.
UCSCiuc057pnr.1. human. [Q9H2M9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004828 mRNA. Translation: AAC35881.1.
AF255648 mRNA. Translation: AAG44636.1.
AB020646 mRNA. Translation: BAA74862.2.
AK021928 mRNA. Translation: BAB13939.1.
AK291234 mRNA. Translation: BAF83923.1.
AL445435, AC103590 Genomic DNA. Translation: CAI15808.1.
CH471100 Genomic DNA. Translation: EAW93304.1.
BC146760 mRNA. Translation: AAI46761.1.
AL117631 mRNA. Translation: CAB56022.1.
CCDSiCCDS31028.1. [Q9H2M9-1]
PIRiT17332.
RefSeqiNP_036546.2. NM_012414.3. [Q9H2M9-1]
UniGeneiHs.654849.
Hs.708165.

3D structure databases

ProteinModelPortaliQ9H2M9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117317. 21 interactions.
IntActiQ9H2M9. 2 interactions.
STRINGi9606.ENSP00000351832.

PTM databases

iPTMnetiQ9H2M9.
PhosphoSiteiQ9H2M9.

Polymorphism and mutation databases

BioMutaiRAB3GAP2.
DMDMi62511132.

Proteomic databases

EPDiQ9H2M9.
MaxQBiQ9H2M9.
PaxDbiQ9H2M9.
PRIDEiQ9H2M9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358951; ENSP00000351832; ENSG00000118873. [Q9H2M9-1]
GeneIDi25782.
KEGGihsa:25782.
UCSCiuc057pnr.1. human. [Q9H2M9-1]

Organism-specific databases

CTDi25782.
GeneCardsiRAB3GAP2.
HGNCiHGNC:17168. RAB3GAP2.
HPAiHPA026273.
HPA027299.
MalaCardsiRAB3GAP2.
MIMi212720. phenotype.
609275. gene.
614225. phenotype.
neXtProtiNX_Q9H2M9.
Orphaneti401830. Autosomal recessive spastic paraplegia type 69.
1387. Cataract - intellectual disability - hypogonadism.
2510. Micro syndrome.
PharmGKBiPA142671105.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2727. Eukaryota.
ENOG410XTJ2. LUCA.
GeneTreeiENSGT00390000005794.
HOGENOMiHOG000290717.
HOVERGENiHBG067039.
InParanoidiQ9H2M9.
KOiK19937.
OMAiWWQQMRT.
OrthoDBiEOG7TTQ71.
PhylomeDBiQ9H2M9.
TreeFamiTF314817.

Miscellaneous databases

ChiTaRSiRAB3GAP2. human.
GeneWikiiRAB3GAP2.
GenomeRNAii25782.
NextBioi46935.
PROiQ9H2M9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H2M9.
CleanExiHS_RAB3GAP2.
ExpressionAtlasiQ9H2M9. baseline and differential.
GenevisibleiQ9H2M9. HS.

Family and domain databases

InterProiIPR026059. Rab3-gap_reg.
IPR029257. RAB3GAP2_C.
IPR032839. RAB3GAP_N.
[Graphical view]
PANTHERiPTHR12472. PTHR12472. 1 hit.
PfamiPF14656. RAB3GAP2_C. 1 hit.
PF14655. RAB3GAP2_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of the noncatalytic subunit of the Rab3 subfamily-specific GTPase-activating protein."
    Nagano F., Sasaki T., Fukui K., Asakura T., Imazumi K., Takai Y.
    J. Biol. Chem. 273:24781-24785(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Dendritic cell.
  3. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Embryo.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    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.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 930-1393.
    Tissue: Testis.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-901, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Mutation in Rab3 GTPase-activating protein (RAB3GAP) noncatalytic subunit in a kindred with Martsolf syndrome."
    Aligianis I.A., Morgan N.V., Mione M., Johnson C.A., Rosser E., Hennekam R.C.M., Adams G., Trembath R.C., Pilz D.T., Stoodley N., Moore A.T., Wilson S., Maher E.R.
    Am. J. Hum. Genet. 78:702-707(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MARTS CYS-1052.
  16. Cited for: VARIANT WARBM2 167-PHE--THR-169 DEL.

Entry informationi

Entry nameiRBGPR_HUMAN
AccessioniPrimary (citable) accession number: Q9H2M9
Secondary accession number(s): A6H8V0
, O75872, Q9HAB0, Q9UFJ7, Q9UQ15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.