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Q02153

- GCYB1_HUMAN

UniProt

Q02153 - GCYB1_HUMAN

Protein

Guanylate cyclase soluble subunit beta-1

Gene

GUCY1B3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    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

    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ02153.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini421 – 554134Guanylate cyclasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    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. 1 PublicationVSP_054365Add
    BLAST
    Alternative sequencei393 – 42533Missing in isoform HSGC-2. 1 PublicationVSP_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. [Q02153-3]
    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 . [Q02153-3 ]
    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

    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: October 1, 2014
    This is version 142 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