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P51841

- GUC2F_HUMAN

UniProt

P51841 - GUC2F_HUMAN

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Protein

Retinal guanylyl cyclase 2

Gene

GUCY2F

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

Functioni

Probably plays a specific functional role in the rods and/or cones of photoreceptors. It may be the enzyme involved in the resynthesis of cGMP required for recovery of the dark state after phototransduction.

Catalytic activityi

GTP = 3',5'-cyclic GMP + diphosphate.

Enzyme regulationi

Activated by GCAP-1; inhibited by calcium.

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. guanylate cyclase activity Source: ProtInc
  4. protein kinase activity Source: InterPro
  5. receptor activity Source: ProtInc

GO - Biological processi

  1. intracellular signal transduction Source: InterPro
  2. phototransduction, visible light Source: Reactome
  3. receptor guanylyl cyclase signaling pathway Source: ProtInc
  4. regulation of rhodopsin mediated signaling pathway Source: Reactome
  5. rhodopsin mediated signaling pathway Source: Reactome
  6. visual perception Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

cGMP biosynthesis, Sensory transduction, Vision

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinal guanylyl cyclase 2 (EC:4.6.1.2)
Short name:
RETGC-2
Alternative name(s):
Guanylate cyclase 2F, retinal
Guanylate cyclase F
Short name:
GC-F
Rod outer segment membrane guanylate cyclase 2
Short name:
ROS-GC2
Gene namesi
Name:GUCY2F
Synonyms:GUC2F, RETGC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:4691. GUCY2F.

Subcellular locationi

GO - Cellular componenti

  1. integral component of plasma membrane Source: ProtInc
  2. nuclear outer membrane Source: ProtInc
  3. photoreceptor disc membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29071.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5050Sequence AnalysisAdd
BLAST
Chaini51 – 11081058Retinal guanylyl cyclase 2PRO_0000012386Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi104 ↔ 132By similarity
Disulfide bondi452 – 452InterchainBy similarity
Disulfide bondi460 – 460InterchainBy similarity

Post-translational modificationi

There are 9 conserved cysteine residues in sensory guanylate cyclases, 6 in the extracellular domain, which may be involved in intra- or interchain disulfide bonds.

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP51841.
PRIDEiP51841.

PTM databases

PhosphoSiteiP51841.

Expressioni

Tissue specificityi

Retina. Localized exclusively in the outer nuclear layer and inner segments of the rod and cone photoreceptor cells.

Gene expression databases

BgeeiP51841.
CleanExiHS_GUCY2F.
GenevestigatoriP51841.

Organism-specific databases

HPAiHPA000734.
HPA027473.

Interactioni

Protein-protein interaction databases

BioGridi109241. 3 interactions.
IntActiP51841. 2 interactions.
MINTiMINT-7970335.
STRINGi9606.ENSP00000218006.

Structurei

3D structure databases

ProteinModelPortaliP51841.
SMRiP51841. Positions 584-820, 883-1083.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini51 – 467417ExtracellularSequence AnalysisAdd
BLAST
Topological domaini491 – 1108618CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei468 – 49023HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini532 – 812281Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini884 – 1014131Guanylate cyclasePROSITE-ProRule annotationAdd
BLAST

Domaini

The protein kinase domain is predicted to be catalytically inactive.

Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation
Contains 1 guanylate cyclase domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000293307.
HOVERGENiHBG098487.
InParanoidiP51841.
KOiK12321.
OMAiNSIYFIA.
OrthoDBiEOG7QVM1V.
PhylomeDBiP51841.
TreeFamiTF106338.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR011645. Haem_no_assoc-bd.
IPR011009. Kinase-like_dom.
IPR029787. Nucleotide_cyclase.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07701. HNOBA. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P51841-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFLGLGRFSR LVLWFAAFRK LLGHHGLASA KFLWCLCLLS VMSLPQQVWT
60 70 80 90 100
LPYKIGVVGP WACDSLFSKA LPEVAARLAI ERINRDPSFD LSYSFEYVIL
110 120 130 140 150
NEDCQTSRAL SSFISHHQMA SGFIGPTNPG YCEAASLLGN SWDKGIFSWA
160 170 180 190 200
CVNYELDNKI SYPTFSRTLP SPIRVLVTVM KYFQWAHAGV ISSDEDIWVH
210 220 230 240 250
TANRVASALR SHGLPVGVVL TTGQDSQSMR KALQRIHQAD RIRIIIMCMH
260 270 280 290 300
SALIGGETQM HLLECAHDLK MTDGTYVFVP YDALLYSLPY KHTPYRVLRN
310 320 330 340 350
NPKLREAYDA VLTITVESQE KTFYQAFTEA AARGEIPEKL EFDQVSPLFG
360 370 380 390 400
TIYNSIYFIA QAMNNAMKEN GQAGAASLVQ HSRNMQFHGF NQLMRTDSNG
410 420 430 440 450
NGISEYVILD TNLKEWELHS TYTVDMEMEL LRFGGTPIHF PGGRPPRADA
460 470 480 490 500
KCWFAEGKIC HGGIDPAFAM MVCLTLLIAL LSINGFAYFI RRRINKIQLI
510 520 530 540 550
KGPNRILLTL EDVTFINPHF GSKRGSRASV SFQITSEVQS GRSPRLSFSS
560 570 580 590 600
GSLTPATYEN SNIAIYEGDW VWLKKFSLGD FGDLKSIKSR ASDVFEMMKD
610 620 630 640 650
LRHENINPLL GFFYDSGMFA IVTEFCSRGS LEDILTNQDV KLDWMFKSSL
660 670 680 690 700
LLDLIKGMKY LHHREFVHGR LKSRNCVVDG RFVLKVTDYG FNDILEMLRL
710 720 730 740 750
SEEESSMEEL LWTAPELLRA PRGSRLGSFA GDVYSFAIIM QEVMVRGTPF
760 770 780 790 800
CMMDLPAQEI INRLKKPPPV YRPVVPPEHA PPECLQLMKQ CWAEAAEQRP
810 820 830 840 850
TFDEIFNQFK TFNKGKKTNI IDSMLRMLEQ YSSNLEDLIR ERTEELEIEK
860 870 880 890 900
QKTEKLLTQM LPPSVAESLK KGCTVEPEGF DLVTLYFSDI VGFTTISAMS
910 920 930 940 950
EPIEVVDLLN DLYTLFDAII GSHDVYKVET IGDAYMVASG LPKRNGSRHA
960 970 980 990 1000
AEIANMSLDI LSSVGTFKMR HMPEVPVRIR IGLHSGPVVA GVVGLTMPRY
1010 1020 1030 1040 1050
CLFGDTVNTA SRMESTGLPY RIHVSLSTVT ILQNLSEGYE VELRGRTELK
1060 1070 1080 1090 1100
GKGTEETFWL IGKKGFMKPL PVPPPVDKDG QVGHGLQPVE IAAFQRRKAE

RQLVRNKP
Length:1,108
Mass (Da):124,850
Last modified:November 2, 2010 - v2
Checksum:iB047BBF1A3C009F9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti10 – 101R → P in a breast cancer sample; somatic mutation. 1 Publication
VAR_036419
Natural varianti40 – 401S → C.1 Publication
Corresponds to variant rs34228145 [ dbSNP | Ensembl ].
VAR_042233
Natural varianti160 – 1601I → N.1 Publication
Corresponds to variant rs33971675 [ dbSNP | Ensembl ].
VAR_042234
Natural varianti230 – 2301R → W.1 Publication
Corresponds to variant rs33973457 [ dbSNP | Ensembl ].
VAR_042235
Natural varianti284 – 2841L → P.1 Publication
Corresponds to variant rs12008095 [ dbSNP | Ensembl ].
VAR_009136
Natural varianti296 – 2961R → Q.1 Publication
Corresponds to variant rs502209 [ dbSNP | Ensembl ].
VAR_009137
Natural varianti305 – 3051R → Q.1 Publication
Corresponds to variant rs55966326 [ dbSNP | Ensembl ].
VAR_042236
Natural varianti308 – 3081Y → C.1 Publication
Corresponds to variant rs16985750 [ dbSNP | Ensembl ].
VAR_030633
Natural varianti380 – 3801Q → H.1 Publication
Corresponds to variant rs2272925 [ dbSNP | Ensembl ].
VAR_030634
Natural varianti434 – 4341G → R.1 Publication
Corresponds to variant rs56293008 [ dbSNP | Ensembl ].
VAR_042237
Natural varianti568 – 5681G → D in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_042238
Natural varianti628 – 6281R → Q.1 Publication
Corresponds to variant rs7883913 [ dbSNP | Ensembl ].
VAR_030635
Natural varianti677 – 6771V → L.1 Publication
Corresponds to variant rs35474112 [ dbSNP | Ensembl ].
VAR_042239
Natural varianti794 – 7941E → K.1 Publication
Corresponds to variant rs35726803 [ dbSNP | Ensembl ].
VAR_042240
Natural varianti872 – 8721G → D.1 Publication
VAR_069424
Natural varianti1010 – 10101A → V.1 Publication
Corresponds to variant rs55735218 [ dbSNP | Ensembl ].
VAR_042241
Natural varianti1052 – 10521K → R in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042242
Natural varianti1055 – 10551E → D in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication
VAR_042243

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L37378 mRNA. Translation: AAA74451.1.
AL031387 Genomic DNA. Translation: CAB41303.1.
CCDSiCCDS14545.1.
PIRiI59385.
RefSeqiNP_001513.2. NM_001522.2.
UniGeneiHs.123074.

Genome annotation databases

EnsembliENST00000218006; ENSP00000218006; ENSG00000101890.
GeneIDi2986.
KEGGihsa:2986.
UCSCiuc004eod.4. human.

Polymorphism databases

DMDMi311033391.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Mutations of the GUCY2F gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L37378 mRNA. Translation: AAA74451.1 .
AL031387 Genomic DNA. Translation: CAB41303.1 .
CCDSi CCDS14545.1.
PIRi I59385.
RefSeqi NP_001513.2. NM_001522.2.
UniGenei Hs.123074.

3D structure databases

ProteinModelPortali P51841.
SMRi P51841. Positions 584-820, 883-1083.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109241. 3 interactions.
IntActi P51841. 2 interactions.
MINTi MINT-7970335.
STRINGi 9606.ENSP00000218006.

PTM databases

PhosphoSitei P51841.

Polymorphism databases

DMDMi 311033391.

Proteomic databases

PaxDbi P51841.
PRIDEi P51841.

Protocols and materials databases

DNASUi 2986.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000218006 ; ENSP00000218006 ; ENSG00000101890 .
GeneIDi 2986.
KEGGi hsa:2986.
UCSCi uc004eod.4. human.

Organism-specific databases

CTDi 2986.
GeneCardsi GC0XM108616.
H-InvDB HIX0056276.
HGNCi HGNC:4691. GUCY2F.
HPAi HPA000734.
HPA027473.
MIMi 300041. gene.
neXtProti NX_P51841.
PharmGKBi PA29071.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118959.
HOGENOMi HOG000293307.
HOVERGENi HBG098487.
InParanoidi P51841.
KOi K12321.
OMAi NSIYFIA.
OrthoDBi EOG7QVM1V.
PhylomeDBi P51841.
TreeFami TF106338.

Enzyme and pathway databases

Reactomei REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.

Miscellaneous databases

GenomeRNAii 2986.
NextBioi 11840.
PROi P51841.
SOURCEi Search...

Gene expression databases

Bgeei P51841.
CleanExi HS_GUCY2F.
Genevestigatori P51841.

Family and domain databases

Gene3Di 3.30.70.1230. 1 hit.
InterProi IPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR011645. Haem_no_assoc-bd.
IPR011009. Kinase-like_dom.
IPR029787. Nucleotide_cyclase.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view ]
Pfami PF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07701. HNOBA. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PRINTSi PR00109. TYRKINASE.
SMARTi SM00044. CYCc. 1 hit.
[Graphical view ]
SUPFAMi SSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a second photoreceptor-specific membrane retina guanylyl cyclase (RetGC), RetGC-2."
    Lowe D.G., Dizhoor A.M., Liu K., Gu Q., Spencer M., Laura R., Lu L., Hurley J.B.
    Proc. Natl. Acad. Sci. U.S.A. 92:5535-5539(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-296.
    Tissue: Retina.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-10.
  4. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-40; ASN-160; TRP-230; PRO-284; GLN-305; CYS-308; HIS-380; ARG-434; ASP-568; GLN-628; LEU-677; LYS-794; VAL-1010; ARG-1052 AND ASP-1055.
  5. Cited for: VARIANT ASP-872.

Entry informationi

Entry nameiGUC2F_HUMAN
AccessioniPrimary (citable) accession number: P51841
Secondary accession number(s): Q9UJF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 2, 2010
Last modified: October 29, 2014
This is version 145 of the entry and version 2 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 X
    Human chromosome X: 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

External Data

Dasty 3