Q14028 (CNGB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclic nucleotide-gated cation channel beta-1

Alternative name(s):
Cyclic nucleotide-gated cation channel 4
Short name=CNG channel 4
Short name=CNG-4
Short name=CNG4
Cyclic nucleotide-gated cation channel gamma
Cyclic nucleotide-gated cation channel modulatory subunit
Cyclic nucleotide-gated channel beta-1
Short name=CNG channel beta-1
Glutamic acid-rich protein
Short name=GARP

Gene names

Name:	CNGB1
Synonyms:	CNCG2, CNCG3L, CNCG4, RCNC2

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	1251 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Subunit of cyclic nucleotide-gated (CNG) channels, nonselective cation channels, which play important roles in both visual and olfactory signal transduction. When associated with CNGA1, it is involved in the regulation of ion flow into the rod photoreceptor outer segment (ROS), in response to light-induced alteration of the levels of intracellular cGMP. Ref.4 Ref.8 Isoform GARP2 is a high affinity rod photoreceptor phosphodiesterase (PDE6)-binding protein that modulates its catalytic properties: it is a regulator of spontaneous activation of rod PDE6, thereby serving to lower rod photoreceptor 'dark noise' and allowing these sensory cells to operate at the single photon detection limit. Ref.4 Ref.8
Subunit structure	Tetramer formed of three CNGA1 and one CNGB1 modulatory subunits By similarity.
Subcellular location	Membrane; Multi-pass membrane protein.
Involvement in disease	Retinitis pigmentosa 45 (RP45) [MIM:613767]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11
Sequence similarities	Belongs to the cyclic nucleotide-gated cation channel (TC 1.A.1.5) family. CNGB1 subfamily. [View classification] Contains 1 cyclic nucleotide-binding domain.

Ontologies

Keywords
Biological process	Ion transport Olfaction Sensory transduction Transport Vision
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Retinitis pigmentosa
Domain	Transmembrane Transmembrane helix
Ligand	Nucleotide-binding cAMP cAMP-binding
Molecular function	Ion channel Ligand-gated ion channel
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	photoreceptor cell maintenance Inferred from electronic annotation. Source: Compara phototransduction Inferred from electronic annotation. Source: Compara protein localization to organelle Inferred from electronic annotation. Source: Compara sensory perception of smell Inferred from electronic annotation. Source: UniProtKB-KW visual perception Traceable author statement Ref.1. Source: ProtInc
Cellular_component	intracellular cyclic nucleotide activated cation channel complex Non-traceable author statement. Source: UniProtKB
Molecular_function	cAMP binding Inferred from electronic annotation. Source: UniProtKB-KW intracellular cAMP activated cation channel activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: There is no evidence for an ortholog to bovine GARP1 in the human genome.

Isoform RCNC2B (identifier: Q14028-1)

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 RCNC2A (identifier: Q14028-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-628: Missing.

Isoform GARP2 (identifier: Q14028-3)

Also known as: GARP;

The sequence of this isoform differs from the canonical sequence as follows:
     292-299: ISILPGGQ → RVMGAGGL
     300-1251: Missing.

Note: In the rod cells, the CNGB1 locus encodes the cyclic nucleotide-gated cation channel beta-1 subunit and several glutamic-acid-rich proteins (GARPs).

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1251	1251	Cyclic nucleotide-gated cation channel beta-1		PRO_0000219323
Regions
	Topological domain	343 – 656	314	Cytoplasmic Potential
	Transmembrane	657 – 675	19	Helical; Name=H1; Potential
	Topological domain	676 – 689	14	Extracellular Potential
	Transmembrane	690 – 708	19	Helical; Name=H2; Potential
	Topological domain	709 – 733	25	Cytoplasmic Potential
	Transmembrane	734 – 753	20	Helical; Name=H3; Potential
	Topological domain	754 – 790	37	Extracellular Potential
	Transmembrane	791 – 813	23	Helical; Name=H4; Potential
	Topological domain	814 – 857	44	Cytoplasmic Potential
	Transmembrane	858 – 877	20	Helical; Name=H5; Potential
	Topological domain	878 – 961	84	Extracellular Potential
	Transmembrane	962 – 982	21	Helical; Name=H6; Potential
	Topological domain	983 – 1251	269	Cytoplasmic Potential
	Nucleotide binding	970 – 1109	140	cAMP By similarity
	Motif	568 – 578	11	IQ-like
	Compositional bias	23 – 63	41	Glu-rich
	Compositional bias	171 – 252	82	Pro-rich
	Compositional bias	351 – 371	21	Poly-Glu
Sites
	Binding site	1030	1	cAMP Potential
	Binding site	1042	1	cAMP Potential
Natural variations
	Alternative sequence	1 – 628	628	Missing in isoform RCNC2A.		VSP_001110
	Alternative sequence	292 – 299	8	ISILPGGQ → RVMGAGGL in isoform GARP2.		VSP_037921
	Alternative sequence	300 – 1251	952	Missing in isoform GARP2.		VSP_037922
	Natural variant	100	1	R → H. Ref.2 Ref.3 Ref.4 Corresponds to variant rs13336595 [ dbSNP | Ensembl ].		VAR_058691
	Natural variant	479	1	L → I. Corresponds to variant rs2303783 [ dbSNP | Ensembl ].		VAR_059225
	Natural variant	535	1	V → A. Corresponds to variant rs12927214 [ dbSNP | Ensembl ].		VAR_059226
	Natural variant	731	1	N → K. Corresponds to variant rs376270 [ dbSNP | Ensembl ].		VAR_059227
	Natural variant	745	1	L → I. Corresponds to variant rs10459809 [ dbSNP | Ensembl ].		VAR_059228
	Natural variant	911	1	K → R. Corresponds to variant rs2303785 [ dbSNP | Ensembl ].		VAR_059229
	Natural variant	961	1	A → S. Corresponds to variant rs16942445 [ dbSNP | Ensembl ].		VAR_059230
	Natural variant	993	1	G → V in RP45. Ref.11		VAR_060491
Experimental info
	Mutagenesis	568	1	L → E: Loss of calcium/calmodulin modulation. Ref.7
	Sequence conflict	128	1	I → V in AC010543. Ref.5
	Sequence conflict	189 – 194	6	Missing in AAC04830. Ref.4
	Sequence conflict	1148 – 1149	2	QQ → HE in AAB63387. Ref.2
	Sequence conflict	1148 – 1149	2	QQ → HE in AAA65619. Ref.1
	Sequence conflict	1148 – 1149	2	QQ → HE in AAA65620. Ref.1
	Sequence conflict	1207 – 1208	2	RP → SC in AAB63387. Ref.2
	Sequence conflict	1207 – 1208	2	RP → SC in AAA65619. Ref.1
	Sequence conflict	1207 – 1208	2	RP → SC in AAA65620. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform RCNC2B [UniParc]. Last modified September 1, 2009. Version 2. Checksum: 7A45CB399EB2B20C	FASTA	1,251	139,678
	10 20 30 40 50 60 MLGWVQRVLP QPPGTPRKTK MQEEEEVEPE PEMEAEVEPE PNPEEAETES ESMPPEESFK 70 80 90 100 110 120 EEEVAVADPS PQETKEAALT STISLRAQGA EISEMNSPSR RVLTWLMKGV EKVIPQPVHS 130 140 150 160 170 180 ITEDPAQILG HGSTGDTGCT DEPNEALEAQ DTRPGLRLLL WLEQNLERVL PQPPKSSEVW 190 200 210 220 230 240 RDEPAVATGA ASDPAPPGRP QEMGPKLQAR ETPSLPTPIP LQPKEEPKEA PAPEPQPGSQ 250 260 270 280 290 300 AQTSSLPPTR DPARLVAWVL HRLEMALPQP VLHGKIGEQE PDSPGICDVQ TISILPGGQV 310 320 330 340 350 360 EPDLVLEEVE PPWEDAHQDV STSPQGTEVV PAYEEENKAV EKMPRELSRI EEEKEDEEEE 370 380 390 400 410 420 EEEEEEEEEE EVTEVLLDSC VVSQVGVGQS EEDGTRPQST SDQKLWEEVG EEAKKEAEEK 430 440 450 460 470 480 AKEEAEEVAE EEAEKEPQDW AETKEEPEAE AEAASSGVPA TKQHPEVQVE DTDADSCPLM 490 500 510 520 530 540 AEENPPSTVL PPPSPAKSDT LIVPSSASGT HRKKLPSEDD EAEELKALSP AESPVVAWSD 550 560 570 580 590 600 PTTPKDTDGQ DRAASTASTN SAIINDRLQE LVKLFKERTE KVKEKLIDPD VTSDEESPKP 610 620 630 640 650 660 SPAKKAPEPA PDTKPAEAEP VEEEHYCDML CCKFKHRPWK KYQFPQSIDP LTNLMYVLWL 670 680 690 700 710 720 FFVVMAWNWN CWLIPVRWAF PYQTPDNIHH WLLMDYLCDL IYFLDITVFQ TRLQFVRGGD 730 740 750 760 770 780 IITDKKDMRN NYLKSRRFKM DLLSLLPLDF LYLKVGVNPL LRLPRCLKYM AFFEFNSRLE 790 800 810 820 830 840 SILSKAYVYR VIRTTAYLLY SLHLNSCLYY WASAYQGLGS THWVYDGVGN SYIRCYYFAV 850 860 870 880 890 900 KTLITIGGLP DPKTLFEIVF QLLNYFTGVF AFSVMIGQMR DVVGAATAGQ TYYRSCMDST 910 920 930 940 950 960 VKYMNFYKIP KSVQNRVKTW YEYTWHSQGM LDESELMVQL PDKMRLDLAI DVNYNIVSKV 970 980 990 1000 1010 1020 ALFQGCDRQM IFDMLKRLRS VVYLPNDYVC KKGEIGREMY IIQAGQVQVL GGPDGKSVLV 1030 1040 1050 1060 1070 1080 TLKAGSVFGE ISLLAVGGGN RRTANVVAHG FTNLFILDKK DLNEILVHYP ESQKLLRKKA 1090 1100 1110 1120 1130 1140 RRMLRSNNKP KEEKSVLILP PRAGTPKLFN AALAMTGKMG GKGAKGGKLA HLRARLKELA 1150 1160 1170 1180 1190 1200 ALEAAAKQQE LVEQAKSSQD VKGEEGSAAP DQHTHPKEAA TDPPAPRTPP EPPGSPPSSP 1210 1220 1230 1240 1250 PPASLGRPEG EEEGPAEPEE HSVRICMSPG PEPGEQILSV KMPEEREEKA E
	Isoform RCNC2A [UniParc]. Checksum: 19FD335A37A9BD8A	FASTA	623	70,901
	10 20 30 40 50 60 MLCCKFKHRP WKKYQFPQSI DPLTNLMYVL WLFFVVMAWN WNCWLIPVRW AFPYQTPDNI 70 80 90 100 110 120 HHWLLMDYLC DLIYFLDITV FQTRLQFVRG GDIITDKKDM RNNYLKSRRF KMDLLSLLPL 130 140 150 160 170 180 DFLYLKVGVN PLLRLPRCLK YMAFFEFNSR LESILSKAYV YRVIRTTAYL LYSLHLNSCL 190 200 210 220 230 240 YYWASAYQGL GSTHWVYDGV GNSYIRCYYF AVKTLITIGG LPDPKTLFEI VFQLLNYFTG 250 260 270 280 290 300 VFAFSVMIGQ MRDVVGAATA GQTYYRSCMD STVKYMNFYK IPKSVQNRVK TWYEYTWHSQ 310 320 330 340 350 360 GMLDESELMV QLPDKMRLDL AIDVNYNIVS KVALFQGCDR QMIFDMLKRL RSVVYLPNDY 370 380 390 400 410 420 VCKKGEIGRE MYIIQAGQVQ VLGGPDGKSV LVTLKAGSVF GEISLLAVGG GNRRTANVVA 430 440 450 460 470 480 HGFTNLFILD KKDLNEILVH YPESQKLLRK KARRMLRSNN KPKEEKSVLI LPPRAGTPKL 490 500 510 520 530 540 FNAALAMTGK MGGKGAKGGK LAHLRARLKE LAALEAAAKQ QELVEQAKSS QDVKGEEGSA 550 560 570 580 590 600 APDQHTHPKE AATDPPAPRT PPEPPGSPPS SPPPASLGRP EGEEEGPAEP EEHSVRICMS 610 620 PGPEPGEQIL SVKMPEEREE KAE
	Isoform GARP2 (GARP) [UniParc]. Checksum: 1B07296CA8ECB655	FASTA	299	32,531
	10 20 30 40 50 60 MLGWVQRVLP QPPGTPRKTK MQEEEEVEPE PEMEAEVEPE PNPEEAETES ESMPPEESFK 70 80 90 100 110 120 EEEVAVADPS PQETKEAALT STISLRAQGA EISEMNSPSR RVLTWLMKGV EKVIPQPVHS 130 140 150 160 170 180 ITEDPAQILG HGSTGDTGCT DEPNEALEAQ DTRPGLRLLL WLEQNLERVL PQPPKSSEVW 190 200 210 220 230 240 RDEPAVATGA ASDPAPPGRP QEMGPKLQAR ETPSLPTPIP LQPKEEPKEA PAPEPQPGSQ 250 260 270 280 290 AQTSSLPPTR DPARLVAWVL HRLEMALPQP VLHGKIGEQE PDSPGICDVQ TRVMGAGGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new subunit of the cyclic nucleotide-gated cation channel in retinal rods." Chen T.-Y., Peng Y.-W., Dhallan R.S., Ahamed B., Reed R.R., Yau K.-W. Nature 362:764-767(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS RCNC2A AND RCNC2B). Tissue: Retina.
[2]	"cDNA, gene structure, and chromosomal localization of human GAR1 (CNCG3L), a homolog of the third subunit of bovine photoreceptor cGMP-gated channel." Ardell M.D., Makhija A.K., Oliveira L., Miniou P., Viegas-Pequignot E., Pittler S.J. Genomics 28:32-38(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GARP2), VARIANT HIS-100. Tissue: Retina.
[3]	"The beta subunit of human rod photoreceptor cGMP-gated cation channel is generated from a complex transcription unit." Ardell M.D., Aragon I., Oliveira L., Porche G.E., Burke E., Pittler S.J. FEBS Lett. 389:213-218(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RCNC2B), VARIANT HIS-100. Tissue: Retina.
[4]	"Identification of a domain on the beta-subunit of the rod cGMP-gated cation channel that mediates inhibition by calcium-calmodulin." Grunwald M.E., Yu W.P., Yu H.H., Yau K.W. J. Biol. Chem. 273:9148-9157(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RCNC2B), FUNCTION, VARIANT HIS-100. Tissue: Retina.
[5]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"Genomic organization of the human rod photoreceptor cGMP-gated cation channel beta-subunit gene." Ardell M.D., Bedsole D.L., Schoborg R.V., Pittler S.J. Gene 245:311-318(2000) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING.
[7]	"Calmodulin permanently associates with rat olfactory CNG channels under native conditions." Bradley J., Boenigk W., Yau K.-W., Frings S. Nat. Neurosci. 7:705-710(2004) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF LEU-568.
[8]	"The glutamic acid-rich protein-2 (GARP2) is a high affinity rod photoreceptor phosphodiesterase (PDE6)-binding protein that modulates its catalytic properties." Pentia D.C., Hosier S., Cote R.H. J. Biol. Chem. 281:5500-5505(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORM GARP2), FUNCTION.
[9]	"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded." Batra-Safferling R., Abarca-Heidemann K., Korschen H.G., Tziatzios C., Stoldt M., Budyak I., Willbold D., Schwalbe H., Klein-Seetharaman J., Kaupp U.B. J. Biol. Chem. 281:1449-1460(2006) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF THE GARPS PROTEINS.
[10]	Cote R.H. Unpublished observations (MAY-2009) Cited for: ALTERNATIVE SPLICING (ISOFORM GARP2).
[11]	"Segregation of a mutation in CNGB1 encoding the beta-subunit of the rod cGMP-gated channel in a family with autosomal recessive retinitis pigmentosa." Bareil C., Hamel C.P., Delague V., Arnaud B., Demaille J., Claustres M. Hum. Genet. 108:328-334(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP45 VAL-993.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	L15296 Genomic DNA. Translation: AAA65620.1. L15297 Genomic DNA. Translation: AAA65619.1. U18945 mRNA. Translation: AAA91633.1. U58837 mRNA. Translation: AAB63387.1. AF042498 mRNA. Translation: AAC04830.1. AC010543 Genomic DNA. No translation available.
IPI	IPI00164347. IPI00297656. IPI00646195.
PIR	A57652. S32538. S69275.
RefSeq	NP_001129111.1. NM_001135639.1. NP_001288.3. NM_001297.4.
UniGene	Hs.147062.
3D structure databases
ProteinModelPortal	Q14028.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000251102.
Protein family/group databases
TCDB	1.A.1.5.3. voltage-gated ion channel (VIC) superfamily.
PTM databases
PhosphoSite	Q14028.
Polymorphism databases
DMDM	257051004.
Proteomic databases
PaxDb	Q14028.
PRIDE	Q14028.
Protocols and materials databases
DNASU	1258.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000251102; ENSP00000251102; ENSG00000070729. ENST00000311183; ENSP00000311670; ENSG00000070729.
GeneID	1258.
KEGG	hsa:1258.
UCSC	uc002emt.2. human. uc002emu.2. human.
Organism-specific databases
CTD	1258.
GeneCards	GC16M058001.
H-InvDB	HIX0038536.
HGNC	HGNC:2151. CNGB1.
HPA	HPA039159.
MIM	600724. gene. 613767. phenotype.
neXtProt	NX_Q14028.
Orphanet	791. Retinitis pigmentosa.
PharmGKB	PA26662.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG289446.
HOGENOM	HOG000231425.
HOVERGEN	HBG051038.
InParanoid	Q14028.
KO	K04952.
OMA	DTDADSC.
OrthoDB	EOG4NP72T.
Enzyme and pathway databases
Pathway_Interaction_DB	rhodopsin_pathway. Visual signal transduction: Rods.
Gene expression databases
ArrayExpress	Q14028.
Bgee	Q14028.
CleanEx	HS_CNGB1.
Genevestigator	Q14028.
GermOnline	ENSG00000070729. Homo sapiens.
Family and domain databases
Gene3D	2.60.120.10. 1 hit.
InterPro	IPR018490. cNMP-bd-like. IPR018488. cNMP-bd_CS. IPR000595. cNMP-bd_dom. IPR014710. RmlC-like_jellyroll. [Graphical view]
Pfam	PF00027. cNMP_binding. 1 hit. [Graphical view]
SMART	SM00100. cNMP. 1 hit. [Graphical view]
SUPFAM	SSF51206. cNMP_binding. 1 hit.
PROSITE	PS00888. CNMP_BINDING_1. 1 hit. PS00889. CNMP_BINDING_2. 1 hit. PS50042. CNMP_BINDING_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	1258.
NextBio	5089.
SOURCE	Search...

Entry information

Entry name

CNGB1_HUMAN

Accession

Primary (citable) accession number: Q14028
Secondary accession number(s): O43636 , Q13059, Q14029, Q9UMG2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	September 1, 2009
Last modified:	May 1, 2013
This is version 115 of the entry and version 2 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.