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Q02153

- GCYB1_HUMAN

UniProt

Q02153 - GCYB1_HUMAN

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Protein

Guanylate cyclase soluble subunit beta-1

Gene
GUCY1B3, GUC1B3, GUCSB3, GUCY1B1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Binds 1 or 2 heme groups per heterodimer By similarity.

Enzyme regulationi

Activated by nitric oxide in the presence of magnesium or manganese ions.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi105 – 1051Iron (heme proximal ligand) By similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. guanylate cyclase activity Source: ProtInc
  3. heme binding Source: Ensembl
  4. metal ion binding Source: UniProtKB-KW
  5. receptor activity Source: ProtInc

GO - Biological processi

  1. blood circulation Source: ProtInc
  2. blood coagulation Source: Reactome
  3. nitric oxide mediated signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

cGMP biosynthesis

Keywords - Ligandi

GTP-binding, Heme, Iron, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_23862. Nitric oxide stimulates guanylate cyclase.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylate cyclase soluble subunit beta-1 (EC:4.6.1.2)
Short name:
GCS-beta-1
Alternative name(s):
Guanylate cyclase soluble subunit beta-3
Short name:
GCS-beta-3
Soluble guanylate cyclase small subunit
Gene namesi
Name:GUCY1B3
Synonyms:GUC1B3, GUCSB3, GUCY1B1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:4687. GUCY1B3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. guanylate cyclase complex, soluble Source: ProtInc
  3. intracellular membrane-bounded organelle Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29068.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 619619Guanylate cyclase soluble subunit beta-1PRO_0000074116Add
BLAST

Proteomic databases

MaxQBiQ02153.
PaxDbiQ02153.
PRIDEiQ02153.

PTM databases

PhosphoSiteiQ02153.

Expressioni

Gene expression databases

ArrayExpressiQ02153.
BgeeiQ02153.
CleanExiHS_GUCY1B3.
GenevestigatoriQ02153.

Organism-specific databases

HPAiCAB010890.
HPA020870.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

BioGridi109238. 6 interactions.
IntActiQ02153. 1 interaction.
STRINGi9606.ENSP00000264424.

Structurei

Secondary structure

1
619
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi415 – 42713
Helixi430 – 4367
Helixi443 – 46119
Turni463 – 4653
Beta strandi470 – 4723
Beta strandi479 – 4879
Helixi492 – 50716
Beta strandi519 – 53315
Beta strandi535 – 5373
Beta strandi539 – 5446
Helixi545 – 55511
Beta strandi561 – 5655
Helixi566 – 5716
Turni575 – 5773
Beta strandi582 – 5909
Beta strandi599 – 6079

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WZ1X-ray1.63A/B408-619[»]
3UVJX-ray2.08B/D408-619[»]
4NI2X-ray1.90B408-608[»]
ProteinModelPortaliQ02153.
SMRiQ02153. Positions 1-182, 212-334, 348-408, 412-610.

Miscellaneous databases

EvolutionaryTraceiQ02153.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini421 – 554134Guanylate cyclaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2114.
HOGENOMiHOG000220903.
HOVERGENiHBG051715.
InParanoidiQ02153.
KOiK12319.
OrthoDBiEOG7BS48T.
PhylomeDBiQ02153.
TreeFamiTF351403.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR011645. Haem_no_assoc-bd.
IPR011644. Heme_NO-bd.
IPR024096. NO_sig/Golgi_transp_ligand-bd.
[Graphical view]
PfamiPF00211. Guanylate_cyc. 1 hit.
PF07700. HNOB. 1 hit.
PF07701. HNOBA. 1 hit.
[Graphical view]
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF111126. SSF111126. 1 hit.
SSF55073. SSF55073. 1 hit.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform HSGC-1 (identifier: Q02153-1) [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

MYGFVNHALE LLVIRNYGPE VWEDIKKEAQ LDEEGQFLVR IIYDDSKTYD    50
LVAAASKVLN LNAGEILQMF GKMFFVFCQE SGYDTILRVL GSNVREFLQN 100
LDALHDHLAT IYPGMRAPSF RCTDAEKGKG LILHYYSERE GLQDIVIGII 150
KTVAQQIHGT EIDMKVIQQR NEECDHTQFL IEEKESKEED FYEDLDRFEE 200
NGTQESRISP YTFCKAFPFH IIFDRDLVVT QCGNAIYRVL PQLQPGNCSL 250
LSVFSLVRPH IDISFHGILS HINTVFVLRS KEGLLDVEKL ECEDELTGTE 300
ISCLRLKGQM IYLPEADSIL FLCSPSVMNL DDLTRRGLYL SDIPLHDATR 350
DLVLLGEQFR EEYKLTQELE ILTDRLQLTL RALEDEKKKT DTLLYSVLPP 400
SVANELRHKR PVPAKRYDNV TILFSGIVGF NAFCSKHASG EGAMKIVNLL 450
NDLYTRFDTL TDSRKNPFVY KVETVGDKYM TVSGLPEPCI HHARSICHLA 500
LDMMEIAGQV QVDGESVQIT IGIHTGEVVT GVIGQRMPRY CLFGNTVNLT 550
SRTETTGEKG KINVSEYTYR CLMSPENSDP QFHLEHRGPV SMKGKKEPMQ 600
VWFLSRKNTG TEETKQDDD 619
Length:619
Mass (Da):70,514
Last modified:July 1, 1993 - v1
Checksum:i231E4E660DE02AA1
GO
Isoform HSGC-2 (identifier: Q02153-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     393-425: Missing.

Show »
Length:586
Mass (Da):66,738
Checksum:i59818154086FD4A3
GO
Isoform 3 (identifier: Q02153-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MYGFVNHALELLVIRNYGPEVWEDIK → MLMCFI

Note: No experimental confirmation available.

Show »
Length:599
Mass (Da):68,165
Checksum:i93F6129D51BECB23
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626MYGFV…WEDIK → MLMCFI in isoform 3. VSP_054365Add
BLAST
Alternative sequencei393 – 42533Missing in isoform HSGC-2. VSP_001813Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66533 mRNA. Translation: CAA47144.1.
AF020340 mRNA. Translation: AAB94877.1.
AK296680 mRNA. Translation: BAH12412.1.
AC114761 Genomic DNA. No translation available.
BC047620 mRNA. Translation: AAH47620.2.
CCDSiCCDS47154.1. [Q02153-1]
PIRiS23097.
RefSeqiNP_000848.1. NM_000857.3. [Q02153-1]
UniGeneiHs.77890.

Genome annotation databases

EnsembliENST00000264424; ENSP00000264424; ENSG00000061918. [Q02153-1]
ENST00000503520; ENSP00000420842; ENSG00000061918. [Q02153-2]
ENST00000505764; ENSP00000426319; ENSG00000061918.
GeneIDi2983.
KEGGihsa:2983.
UCSCiuc003ipc.3. human. [Q02153-1]
uc010iqf.3. human. [Q02153-2]

Polymorphism databases

DMDMi399328.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66533 mRNA. Translation: CAA47144.1 .
AF020340 mRNA. Translation: AAB94877.1 .
AK296680 mRNA. Translation: BAH12412.1 .
AC114761 Genomic DNA. No translation available.
BC047620 mRNA. Translation: AAH47620.2 .
CCDSi CCDS47154.1. [Q02153-1 ]
PIRi S23097.
RefSeqi NP_000848.1. NM_000857.3. [Q02153-1 ]
UniGenei Hs.77890.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WZ1 X-ray 1.63 A/B 408-619 [» ]
3UVJ X-ray 2.08 B/D 408-619 [» ]
4NI2 X-ray 1.90 B 408-608 [» ]
ProteinModelPortali Q02153.
SMRi Q02153. Positions 1-182, 212-334, 348-408, 412-610.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109238. 6 interactions.
IntActi Q02153. 1 interaction.
STRINGi 9606.ENSP00000264424.

Chemistry

BindingDBi Q02153.
ChEMBLi CHEMBL2111348.

PTM databases

PhosphoSitei Q02153.

Polymorphism databases

DMDMi 399328.

Proteomic databases

MaxQBi Q02153.
PaxDbi Q02153.
PRIDEi Q02153.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264424 ; ENSP00000264424 ; ENSG00000061918 . [Q02153-1 ]
ENST00000503520 ; ENSP00000420842 ; ENSG00000061918 . [Q02153-2 ]
ENST00000505764 ; ENSP00000426319 ; ENSG00000061918 .
GeneIDi 2983.
KEGGi hsa:2983.
UCSCi uc003ipc.3. human. [Q02153-1 ]
uc010iqf.3. human. [Q02153-2 ]

Organism-specific databases

CTDi 2983.
GeneCardsi GC04P156680.
HGNCi HGNC:4687. GUCY1B3.
HPAi CAB010890.
HPA020870.
MIMi 139397. gene.
neXtProti NX_Q02153.
PharmGKBi PA29068.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2114.
HOGENOMi HOG000220903.
HOVERGENi HBG051715.
InParanoidi Q02153.
KOi K12319.
OrthoDBi EOG7BS48T.
PhylomeDBi Q02153.
TreeFami TF351403.

Enzyme and pathway databases

Reactomei REACT_23862. Nitric oxide stimulates guanylate cyclase.

Miscellaneous databases

EvolutionaryTracei Q02153.
GeneWikii GUCY1B3.
GenomeRNAii 2983.
NextBioi 11832.
PROi Q02153.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q02153.
Bgeei Q02153.
CleanExi HS_GUCY1B3.
Genevestigatori Q02153.

Family and domain databases

Gene3Di 3.30.70.1230. 1 hit.
InterProi IPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR011645. Haem_no_assoc-bd.
IPR011644. Heme_NO-bd.
IPR024096. NO_sig/Golgi_transp_ligand-bd.
[Graphical view ]
Pfami PF00211. Guanylate_cyc. 1 hit.
PF07700. HNOB. 1 hit.
PF07701. HNOBA. 1 hit.
[Graphical view ]
SMARTi SM00044. CYCc. 1 hit.
[Graphical view ]
SUPFAMi SSF111126. SSF111126. 1 hit.
SSF55073. SSF55073. 1 hit.
PROSITEi PS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the cDNAs coding for the two subunits of soluble guanylyl cyclase from human brain."
    Giuili G., Scholl U., Bulle F., Guellaeen G.
    FEBS Lett. 304:83-88(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. Gansemans Y., Brouckaert P., Fiers W.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HSGC-2).
    Tissue: Kidney.
  3. "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 3).
    Tissue: Tongue.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 HSGC-1).
    Tissue: Brain.
  6. "Heterogeneity in human soluble guanylate cyclase due to alternative splicing."
    Chhajilani V., Fraendberg P.-A., Ahlner J., Axelsson K.L., Wikberg J.E.S.
    FEBS Lett. 290:157-158(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 337-545, ALTERNATIVE SPLICING.
    Tissue: Lung.

Entry informationi

Entry nameiGCYB1_HUMAN
AccessioniPrimary (citable) accession number: Q02153
Secondary accession number(s): B7Z426, Q86WY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: September 3, 2014
This is version 141 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

Miscellaneous

There are two types of guanylate cyclases: soluble forms and membrane-associated receptor forms.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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