Q9NPQ8 (RIC8A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Synembryn-A

Alternative name(s):
Protein Ric-8A

Gene names

Name:

RIC8A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	531 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex By similarity. Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation. Ref.8
Subunit structure	Interacts with GDP-bound G alpha proteins GNAI1, GNAO1 and GNAQ, and with GNA13 with lower affinity. Does not interact with G-alpha proteins when they are in complex with subunits beta and gamma. Interacts (via C-terminus) with RGS14; the interaction stimulates the dissociation of the complex between RGS14 and the active GTP-bound form of GNAI1 By similarity.
Subcellular location	Cytoplasm By similarity. Cell membrane By similarity. Note: Colocalizes with RIC8A in CA2 hippocampal neurons. Colocalizes with GNAI1 and RGS14 at the plasma membrane By similarity.
Sequence similarities	Belongs to the synembryn family.
Sequence caution	The sequence BAB14282.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB14282.1 differs from that shown. Reason: Frameshift at position 397. The sequence BAB15653.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB55126.1 differs from that shown. Reason: Frameshift at position 48.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing
Molecular function	Guanine-nucleotide releasing factor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara basement membrane organization Inferred from electronic annotation. Source: Compara cell migration involved in gastrulation Inferred from electronic annotation. Source: Compara cell-cell adhesion involved in gastrulation Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara vasculature development Inferred from electronic annotation. Source: Compara visual learning Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	guanyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NPQ8-1)

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.

Isoform 2 (identifier: Q9NPQ8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: MEPRAVAEAV...FDDAQQEDRK → MMPNRRTGRW...WWSRSSPCPQ

Isoform 3 (identifier: Q9NPQ8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     354-354: A → AQGWPPP

Isoform 4 (identifier: Q9NPQ8-4)

The sequence of this isoform differs from the canonical sequence as follows:
     209-209: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 531	531	Synembryn-A		PRO_0000235890
Amino acid modifications
	Modified residue	199	1	Phosphothreonine By similarity
	Modified residue	436	1	Phosphoserine Ref.11 Ref.13 Ref.14
	Modified residue	441	1	Phosphothreonine Ref.11 Ref.13 Ref.14
	Modified residue	502	1	Phosphoserine Ref.14 Ref.16
	Modified residue	523	1	Phosphoserine Ref.11
	Modified residue	524	1	Phosphoserine Ref.11
	Modified residue	528	1	Phosphoserine Ref.11
Natural variations
	Alternative sequence	1 – 44	44	MEPRA…QEDRK → MMPNRRTGRWVLAQGVKGQG RVAPGRRAWWSRSSPCPQ in isoform 2.		VSP_018507
	Alternative sequence	209	1	Missing in isoform 4.		VSP_039849
	Alternative sequence	354	1	A → AQGWPPP in isoform 3.		VSP_018508
Experimental info
	Sequence conflict	48	1	E → V in BAB55126. Ref.2
	Sequence conflict	405	1	P → L in CAD98025. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 5, 2010. Version 3. Checksum: 2BAF3E2791F6E021	FASTA	531	59,710
	10 20 30 40 50 60 MEPRAVAEAV ETGEEDVIME ALRSYNQEHS QSFTFDDAQQ EDRKRLAELL VSVLEQGLPP 70 80 90 100 110 120 SHRVIWLQSV RILSRDRNCL DPFTSRQSLQ ALACYADISV SEGSVPESAD MDVVLESLKC 130 140 150 160 170 180 LCNLVLSSPV AQMLAAEARL VVKLTERVGL YRERSFPHDV QFFDLRLLFL LTALRTDVRQ 190 200 210 220 230 240 QLFQELKGVR LLTDTLELTL GVTPEGNPPP TLLPSQETER AMEILKVLFN ITLDSIKGEV 250 260 270 280 290 300 DEEDAALYRH LGTLLRHCVM IATAGDRTEE FHGHAVNLLG NLPLKCLDVL LTLEPHGDST 310 320 330 340 350 360 EFMGVNMDVI RALLIFLEKR LHKTHRLKES VAPVLSVLTE CARMHRPARK FLKAQVLPPL 370 380 390 400 410 420 RDVRTRPEVG EMLRNKLVRL MTHLDTDVKR VAAEFLFVLC SESVPRFIKY TGYGNAAGLL 430 440 450 460 470 480 AARGLMAGGR PEGQYSEDED TDTDEYKEAK ASINPVTGRV EEKPPNPMEG MTEEQKEHEA 490 500 510 520 530 MKLVTMFDKL SRNRVIQPMG MSPRGHLTSL QDAMCETMEQ QLSSDPDSDP D
	Isoform 2 [UniParc]. Checksum: 823D0B28817F594D	FASTA	525	58,943
	10 20 30 40 50 60 MMPNRRTGRW VLAQGVKGQG RVAPGRRAWW SRSSPCPQRL AELLVSVLEQ GLPPSHRVIW 70 80 90 100 110 120 LQSVRILSRD RNCLDPFTSR QSLQALACYA DISVSEGSVP ESADMDVVLE SLKCLCNLVL 130 140 150 160 170 180 SSPVAQMLAA EARLVVKLTE RVGLYRERSF PHDVQFFDLR LLFLLTALRT DVRQQLFQEL 190 200 210 220 230 240 KGVRLLTDTL ELTLGVTPEG NPPPTLLPSQ ETERAMEILK VLFNITLDSI KGEVDEEDAA 250 260 270 280 290 300 LYRHLGTLLR HCVMIATAGD RTEEFHGHAV NLLGNLPLKC LDVLLTLEPH GDSTEFMGVN 310 320 330 340 350 360 MDVIRALLIF LEKRLHKTHR LKESVAPVLS VLTECARMHR PARKFLKAQV LPPLRDVRTR 370 380 390 400 410 420 PEVGEMLRNK LVRLMTHLDT DVKRVAAEFL FVLCSESVPR FIKYTGYGNA AGLLAARGLM 430 440 450 460 470 480 AGGRPEGQYS EDEDTDTDEY KEAKASINPV TGRVEEKPPN PMEGMTEEQK EHEAMKLVTM 490 500 510 520 FDKLSRNRVI QPMGMSPRGH LTSLQDAMCE TMEQQLSSDP DSDPD
	Isoform 3 [UniParc]. Checksum: C46E2F66B44DE40D	FASTA	537	60,372
	10 20 30 40 50 60 MEPRAVAEAV ETGEEDVIME ALRSYNQEHS QSFTFDDAQQ EDRKRLAELL VSVLEQGLPP 70 80 90 100 110 120 SHRVIWLQSV RILSRDRNCL DPFTSRQSLQ ALACYADISV SEGSVPESAD MDVVLESLKC 130 140 150 160 170 180 LCNLVLSSPV AQMLAAEARL VVKLTERVGL YRERSFPHDV QFFDLRLLFL LTALRTDVRQ 190 200 210 220 230 240 QLFQELKGVR LLTDTLELTL GVTPEGNPPP TLLPSQETER AMEILKVLFN ITLDSIKGEV 250 260 270 280 290 300 DEEDAALYRH LGTLLRHCVM IATAGDRTEE FHGHAVNLLG NLPLKCLDVL LTLEPHGDST 310 320 330 340 350 360 EFMGVNMDVI RALLIFLEKR LHKTHRLKES VAPVLSVLTE CARMHRPARK FLKAQGWPPP 370 380 390 400 410 420 QVLPPLRDVR TRPEVGEMLR NKLVRLMTHL DTDVKRVAAE FLFVLCSESV PRFIKYTGYG 430 440 450 460 470 480 NAAGLLAARG LMAGGRPEGQ YSEDEDTDTD EYKEAKASIN PVTGRVEEKP PNPMEGMTEE 490 500 510 520 530 QKEHEAMKLV TMFDKLSRNR VIQPMGMSPR GHLTSLQDAM CETMEQQLSS DPDSDPD
	Isoform 4 [UniParc]. Checksum: 46ED334ED07C9EA8	FASTA	530	59,612
	10 20 30 40 50 60 MEPRAVAEAV ETGEEDVIME ALRSYNQEHS QSFTFDDAQQ EDRKRLAELL VSVLEQGLPP 70 80 90 100 110 120 SHRVIWLQSV RILSRDRNCL DPFTSRQSLQ ALACYADISV SEGSVPESAD MDVVLESLKC 130 140 150 160 170 180 LCNLVLSSPV AQMLAAEARL VVKLTERVGL YRERSFPHDV QFFDLRLLFL LTALRTDVRQ 190 200 210 220 230 240 QLFQELKGVR LLTDTLELTL GVTPEGNPPT LLPSQETERA MEILKVLFNI TLDSIKGEVD 250 260 270 280 290 300 EEDAALYRHL GTLLRHCVMI ATAGDRTEEF HGHAVNLLGN LPLKCLDVLL TLEPHGDSTE 310 320 330 340 350 360 FMGVNMDVIR ALLIFLEKRL HKTHRLKESV APVLSVLTEC ARMHRPARKF LKAQVLPPLR 370 380 390 400 410 420 DVRTRPEVGE MLRNKLVRLM THLDTDVKRV AAEFLFVLCS ESVPRFIKYT GYGNAAGLLA 430 440 450 460 470 480 ARGLMAGGRP EGQYSEDEDT DTDEYKEAKA SINPVTGRVE EKPPNPMEGM TEEQKEHEAM 490 500 510 520 530 KLVTMFDKLS RNRVIQPMGM SPRGHLTSLQ DAMCETMEQQ LSSDPDSDPD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." 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. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Uterus.
[2]	"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] (ISOFORM 1). Tissue: Teratocarcinoma.
[3]	The European IMAGE consortium Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"The full-ORF clone resource of the German cDNA consortium." 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. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Uterine endothelium.
[5]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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 4). Tissue: Lymph and Uterus.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[8]	"Ric-8A potentiates Gq-mediated signal transduction by acting downstream of G protein-coupled receptor in intact cells." Nishimura A., Okamoto M., Sugawara Y., Mizuno N., Yamauchi J., Itoh H. Genes Cells 11:487-498(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[10]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436; THR-441; SER-523; SER-524 AND SER-528, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Liver.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436 AND THR-441, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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-436; THR-441 AND SER-502, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL136935 mRNA. Translation: CAB66869.1. AK022870 mRNA. Translation: BAB14282.1. Sequence problems. AK027090 mRNA. Translation: BAB15653.1. Different initiation. AK027461 mRNA. Translation: BAB55126.1. Frameshift. AL390088 mRNA. Translation: CAB98211.1. BX538115 mRNA. Translation: CAD98025.1. AC069287 Genomic DNA. No translation available. BC011821 mRNA. Translation: AAH11821.2. BC111499 mRNA. Translation: AAI11500.1. BC121807 mRNA. Translation: AAI21808.1. BC121808 mRNA. Translation: AAI21809.1.
IPI	IPI00100106. IPI00746360. IPI00749304. IPI00970851.
RefSeq	NP_068751.4. NM_021932.4.
UniGene	Hs.592292.
3D structure databases
ProteinModelPortal	Q9NPQ8.
SMR	Q9NPQ8. Positions 373-407.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NPQ8. 10 interactions.
MINT	MINT-1422193.
PTM databases
PhosphoSite	Q9NPQ8.
Polymorphism databases
DMDM	308153562.
Proteomic databases
PaxDb	Q9NPQ8.
PRIDE	Q9NPQ8.
Protocols and materials databases
DNASU	60626.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000325207; ENSP00000325941; ENSG00000177963. ENST00000526104; ENSP00000432008; ENSG00000177963. ENST00000527696; ENSP00000434833; ENSG00000177963.
GeneID	60626.
KEGG	hsa:60626.
UCSC	uc001lof.3. human. uc001log.3. human. uc001loh.3. human.
Organism-specific databases
CTD	60626.
GeneCards	GC11P000200.
HGNC	HGNC:29550. RIC8A.
HPA	CAB046012. HPA041491.
MIM	609146. gene.
neXtProt	NX_Q9NPQ8.
PharmGKB	PA142671067.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG322219.
HOVERGEN	HBG054867.
InParanoid	Q9NPQ8.
OMA	LHQTHRL.
OrthoDB	EOG40CHGV.
Gene expression databases
ArrayExpress	Q9NPQ8.
Bgee	Q9NPQ8.
Genevestigator	Q9NPQ8.
GermOnline	ENSG00000177963. Homo sapiens.
Family and domain databases
Gene3D	1.25.10.10. 2 hits.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR019318. Gua_nucleotide_exch_fac_Ric8. IPR008376. Synembryn. [Graphical view]
Pfam	PF10165. Ric8. 1 hit. [Graphical view]
PRINTS	PR01802. SYNEMBRYN.
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	RIC8A. human.
GenomeRNAi	60626.
NextBio	65465.
SOURCE	Search...

Entry information

Entry name

RIC8A_HUMAN

Accession

Primary (citable) accession number: Q9NPQ8
Secondary accession number(s): Q0P508 , Q2T9J1, Q7Z352, Q96EZ1, Q96SZ2, Q9H064, Q9H5H3, Q9H9E7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	October 5, 2010
Last modified:	May 1, 2013
This is version 82 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.