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Q14028 (CNGB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1251 AA.
Sequence statusComplete.
Protein existenceEvidence 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.9

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.9

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.12

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 processIon transport
Olfaction
Sensory transduction
Transport
Vision
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Retinitis pigmentosa
   DomainTransmembrane
Transmembrane helix
   LigandcAMP
cAMP-binding
Nucleotide-binding
   Molecular functionIon channel
Ligand-gated ion channel
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytosolic calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

phototransduction, visible light

Traceable author statement. Source: Reactome

potassium ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein heterotetramerization

Inferred from electronic annotation. Source: Ensembl

regulation of membrane potential

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of rhodopsin mediated signaling pathway

Traceable author statement. Source: Reactome

rhodopsin mediated signaling pathway

Traceable author statement. Source: Reactome

sensory perception of smell

Inferred from electronic annotation. Source: UniProtKB-KW

transport

Traceable author statement Ref.1. Source: ProtInc

visual perception

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentintegral component of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

intracellular cyclic nucleotide activated cation channel complex

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

terminal bouton

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncAMP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cGMP binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

intracellular cAMP activated cation channel activity

Inferred from electronic annotation. Source: Ensembl

intracellular cGMP activated cation channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

ligand-gated ion channel activity

Traceable author statement Ref.1. Source: ProtInc

voltage-gated potassium channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GRB14Q5ICW42EBI-7959609,EBI-7639273From a different organism.

Alternative products

This entry describes 4 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).
Isoform 4 (identifier: Q14028-4)

The sequence of this isoform differs from the canonical sequence as follows:
     189-194: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12511251Cyclic nucleotide-gated cation channel beta-1
PRO_0000219323

Regions

Topological domain343 – 656314Cytoplasmic Potential
Transmembrane657 – 67519Helical; Name=H1; Potential
Topological domain676 – 68914Extracellular Potential
Transmembrane690 – 70819Helical; Name=H2; Potential
Topological domain709 – 73325Cytoplasmic Potential
Transmembrane734 – 75320Helical; Name=H3; Potential
Topological domain754 – 79037Extracellular Potential
Transmembrane791 – 81323Helical; Name=H4; Potential
Topological domain814 – 85744Cytoplasmic Potential
Transmembrane858 – 87720Helical; Name=H5; Potential
Topological domain878 – 96184Extracellular Potential
Transmembrane962 – 98221Helical; Name=H6; Potential
Topological domain983 – 1251269Cytoplasmic Potential
Nucleotide binding970 – 1109140cAMP By similarity
Motif568 – 57811IQ-like
Compositional bias23 – 6341Glu-rich
Compositional bias171 – 25282Pro-rich
Compositional bias351 – 37121Poly-Glu

Sites

Binding site10301cAMP Potential
Binding site10421cAMP Potential

Natural variations

Alternative sequence1 – 628628Missing in isoform RCNC2A.
VSP_001110
Alternative sequence189 – 1946Missing in isoform 4.
VSP_053421
Alternative sequence292 – 2998ISILPGGQ → RVMGAGGL in isoform GARP2.
VSP_037921
Alternative sequence300 – 1251952Missing in isoform GARP2.
VSP_037922
Natural variant1001R → H. Ref.2 Ref.3 Ref.4
Corresponds to variant rs13336595 [ dbSNP | Ensembl ].
VAR_058691
Natural variant4791L → I.
Corresponds to variant rs2303783 [ dbSNP | Ensembl ].
VAR_059225
Natural variant5351V → A.
Corresponds to variant rs12927214 [ dbSNP | Ensembl ].
VAR_059226
Natural variant7311N → K.
Corresponds to variant rs376270 [ dbSNP | Ensembl ].
VAR_059227
Natural variant7451L → I.
Corresponds to variant rs10459809 [ dbSNP | Ensembl ].
VAR_059228
Natural variant9111K → R.
Corresponds to variant rs2303785 [ dbSNP | Ensembl ].
VAR_059229
Natural variant9611A → S.
Corresponds to variant rs16942445 [ dbSNP | Ensembl ].
VAR_059230
Natural variant9931G → V in RP45. Ref.12
VAR_060491

Experimental info

Mutagenesis5681L → E: Loss of calcium/calmodulin modulation. Ref.8
Sequence conflict1281I → V in AC010543. Ref.5
Sequence conflict1148 – 11492QQ → HE in AAB63387. Ref.2
Sequence conflict1148 – 11492QQ → HE in AAA65619. Ref.1
Sequence conflict1148 – 11492QQ → HE in AAA65620. Ref.1
Sequence conflict1207 – 12082RP → SC in AAB63387. Ref.2
Sequence conflict1207 – 12082RP → SC in AAA65619. Ref.1
Sequence conflict1207 – 12082RP → SC in AAA65620. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform RCNC2B [UniParc].

Last modified September 1, 2009. Version 2.
Checksum: 7A45CB399EB2B20C

FASTA1,251139,678
        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 

« Hide

Isoform RCNC2A [UniParc].

Checksum: 19FD335A37A9BD8A
Show »

FASTA62370,901
Isoform GARP2 (GARP) [UniParc].

Checksum: 1B07296CA8ECB655
Show »

FASTA29932,531
Isoform 4 [UniParc].

Checksum: E99F22376984493D
Show »

FASTA1,245139,179

References

« Hide '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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]Cote R.H.
Unpublished observations (MAY-2009)
Cited for: ALTERNATIVE SPLICING (ISOFORM GARP2).
[12]"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

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.
CH471092 Genomic DNA. Translation: EAW82957.1.
PIRA57652.
S32538.
S69275.
RefSeqNP_001129111.1. NM_001135639.1.
NP_001273059.1. NM_001286130.1.
NP_001288.3. NM_001297.4.
UniGeneHs.147062.

3D structure databases

ProteinModelPortalQ14028.
SMRQ14028. Positions 658-708, 796-883, 893-1070.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107658. 3 interactions.
IntActQ14028. 2 interactions.
MINTMINT-4853474.
STRING9606.ENSP00000251102.

Protein family/group databases

TCDB1.A.1.5.3. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSiteQ14028.

Polymorphism databases

DMDM257051004.

Proteomic databases

PaxDbQ14028.
PRIDEQ14028.

Protocols and materials databases

DNASU1258.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000251102; ENSP00000251102; ENSG00000070729. [Q14028-1]
ENST00000311183; ENSP00000311670; ENSG00000070729. [Q14028-3]
ENST00000564448; ENSP00000454633; ENSG00000070729. [Q14028-4]
GeneID1258.
KEGGhsa:1258.
UCSCuc002emt.2. human. [Q14028-1]
uc002emu.2. human. [Q14028-3]

Organism-specific databases

CTD1258.
GeneCardsGC16M058001.
H-InvDBHIX0038536.
HGNCHGNC:2151. CNGB1.
HPAHPA039159.
MIM600724. gene.
613767. phenotype.
neXtProtNX_Q14028.
Orphanet791. Retinitis pigmentosa.
PharmGKBPA26662.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG289446.
HOGENOMHOG000231425.
HOVERGENHBG051038.
InParanoidQ14028.
KOK04952.
OMADTDADSC.
PhylomeDBQ14028.
TreeFamTF318250.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpressQ14028.
BgeeQ14028.
CleanExHS_CNGB1.
GenevestigatorQ14028.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
InterProIPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamPF00027. cNMP_binding. 1 hit.
[Graphical view]
SMARTSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMSSF51206. SSF51206. 1 hit.
PROSITEPS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCNGB1.
GenomeRNAi1258.
NextBio35525694.
PROQ14028.
SOURCESearch...

Entry information

Entry nameCNGB1_HUMAN
AccessionPrimary (citable) accession number: Q14028
Secondary accession number(s): H3BN09 expand/collapse secondary AC list , O43636, Q13059, Q14029, Q9UMG2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 1, 2009
Last modified: April 16, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM