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Protein

Carbonic anhydrase 14

Gene

CA14

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

Functioni

Reversible hydration of carbon dioxide.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+By similarity

Enzyme regulationi

Activated by histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. Inhibited by coumarins, saccharin, sulfonamide derivatives such as acetazolamide (AZA) and Foscarnet (phosphonoformate trisodium salt).8 Publications

Kineticsi

  1. KM=7.9 mM for CO21 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei84 – 841Proton acceptorBy similarity
    Metal bindingi109 – 1091Zinc; catalytic1 Publication
    Metal bindingi111 – 1111Zinc; catalytic1 Publication
    Metal bindingi135 – 1351Zinc; catalytic1 Publication
    Active sitei144 – 1441By similarity

    GO - Molecular functioni

    • carbonate dehydratase activity Source: ProtInc
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi4.2.1.1. 2681.
    ReactomeiREACT_121123. Reversible hydration of carbon dioxide.
    SABIO-RKQ9ULX7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonic anhydrase 14 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase XIV
    Carbonic anhydrase XIV
    Short name:
    CA-XIV
    Gene namesi
    Name:CA14
    ORF Names:UNQ690/PRO1335
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1372. CA14.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini16 – 290275ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei291 – 31121HelicalSequence AnalysisAdd
    BLAST
    Topological domaini312 – 33726CytoplasmicSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    • integral component of membrane Source: ProtInc
    • plasma membrane Source: Reactome
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25988.

    Chemistry

    DrugBankiDB00819. Acetazolamide.
    DB00909. Zonisamide.

    Polymorphism and mutation databases

    BioMutaiCA14.
    DMDMi8928036.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1515Sequence AnalysisAdd
    BLAST
    Chaini16 – 337322Carbonic anhydrase 14PRO_0000004251Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi40 ↔ 2211 Publication
    Glycosylationi213 – 2131N-linked (GlcNAc...)1 Publication
    Modified residuei325 – 3251Phosphoserine1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ9ULX7.
    PRIDEiQ9ULX7.

    PTM databases

    PhosphoSiteiQ9ULX7.

    Expressioni

    Tissue specificityi

    High expression in all parts of the central nervous system and lower expression in adult liver, heart, small intestine, colon, kidney, urinary bladder and skeletal muscle.

    Gene expression databases

    BgeeiQ9ULX7.
    CleanExiHS_CA14.
    ExpressionAtlasiQ9ULX7. baseline and differential.
    GenevisibleiQ9ULX7. HS.

    Organism-specific databases

    HPAiHPA008482.

    Interactioni

    Protein-protein interaction databases

    BioGridi117162. 41 interactions.
    IntActiQ9ULX7. 1 interaction.
    STRINGi9606.ENSP00000358107.

    Structurei

    Secondary structure

    1
    337
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 263Combined sources
    Helixi30 – 323Combined sources
    Helixi33 – 364Combined sources
    Helixi38 – 414Combined sources
    Beta strandi42 – 443Combined sources
    Helixi52 – 543Combined sources
    Beta strandi66 – 683Combined sources
    Beta strandi77 – 815Combined sources
    Beta strandi86 – 894Combined sources
    Beta strandi95 – 1017Combined sources
    Beta strandi103 – 11210Combined sources
    Beta strandi122 – 1254Combined sources
    Beta strandi131 – 14010Combined sources
    Turni141 – 1433Combined sources
    Helixi147 – 1504Combined sources
    Beta strandi157 – 16913Combined sources
    Helixi172 – 1787Combined sources
    Helixi179 – 1835Combined sources
    Beta strandi190 – 1934Combined sources
    Helixi198 – 2014Combined sources
    Beta strandi209 – 2146Combined sources
    Beta strandi225 – 2328Combined sources
    Beta strandi234 – 2374Combined sources
    Helixi238 – 2469Combined sources
    Beta strandi249 – 2557Combined sources
    Beta strandi275 – 2773Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4LU3X-ray2.00A16-290[»]
    ProteinModelPortaliQ9ULX7.
    SMRiQ9ULX7. Positions 21-286.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni217 – 2182Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3338.
    GeneTreeiENSGT00760000118915.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiQ9ULX7.
    KOiK01672.
    OMAiSYPECGS.
    OrthoDBiEOG7WMCK7.
    PhylomeDBiQ9ULX7.
    TreeFamiTF316425.

    Family and domain databases

    Gene3Di3.10.200.10. 1 hit.
    InterProiIPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018431. Carbonic_anhydrase_CA14.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF84. PTHR18952:SF84. 1 hit.
    PfamiPF00194. Carb_anhydrase. 1 hit.
    [Graphical view]
    SMARTiSM01057. Carb_anhydrase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51069. SSF51069. 1 hit.
    PROSITEiPS51144. ALPHA_CA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9ULX7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLFSALLLEV IWILAADGGQ HWTYEGPHGQ DHWPASYPEC GNNAQSPIDI
    60 70 80 90 100
    QTDSVTFDPD LPALQPHGYD QPGTEPLDLH NNGHTVQLSL PSTLYLGGLP
    110 120 130 140 150
    RKYVAAQLHL HWGQKGSPGG SEHQINSEAT FAELHIVHYD SDSYDSLSEA
    160 170 180 190 200
    AERPQGLAVL GILIEVGETK NIAYEHILSH LHEVRHKDQK TSVPPFNLRE
    210 220 230 240 250
    LLPKQLGQYF RYNGSLTTPP CYQSVLWTVF YRRSQISMEQ LEKLQGTLFS
    260 270 280 290 300
    TEEEPSKLLV QNYRALQPLN QRMVFASFIQ AGSSYTTGEM LSLGVGILVG
    310 320 330
    CLCLLLAVYF IARKIRKKRL ENRKSVVFTS AQATTEA
    Length:337
    Mass (Da):37,668
    Last modified:May 1, 2000 - v1
    Checksum:i6E101C44EA70A700
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti229 – 2291V → A in BAC11191 (PubMed:14702039).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB025904 mRNA. Translation: BAA85002.1.
    AY358689 mRNA. Translation: AAQ89052.1.
    AK074765 mRNA. Translation: BAC11191.1.
    BT020054 mRNA. Translation: AAV38857.1.
    AL138795 Genomic DNA. Translation: CAI22810.1.
    BC034412 mRNA. Translation: AAH34412.1.
    CCDSiCCDS947.1.
    RefSeqiNP_036245.1. NM_012113.2.
    UniGeneiHs.528988.

    Genome annotation databases

    EnsembliENST00000369111; ENSP00000358107; ENSG00000118298.
    GeneIDi23632.
    KEGGihsa:23632.
    UCSCiuc001etx.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB025904 mRNA. Translation: BAA85002.1.
    AY358689 mRNA. Translation: AAQ89052.1.
    AK074765 mRNA. Translation: BAC11191.1.
    BT020054 mRNA. Translation: AAV38857.1.
    AL138795 Genomic DNA. Translation: CAI22810.1.
    BC034412 mRNA. Translation: AAH34412.1.
    CCDSiCCDS947.1.
    RefSeqiNP_036245.1. NM_012113.2.
    UniGeneiHs.528988.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4LU3X-ray2.00A16-290[»]
    ProteinModelPortaliQ9ULX7.
    SMRiQ9ULX7. Positions 21-286.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi117162. 41 interactions.
    IntActiQ9ULX7. 1 interaction.
    STRINGi9606.ENSP00000358107.

    Chemistry

    BindingDBiQ9ULX7.
    ChEMBLiCHEMBL2095180.
    DrugBankiDB00819. Acetazolamide.
    DB00909. Zonisamide.
    GuidetoPHARMACOLOGYi2598.

    PTM databases

    PhosphoSiteiQ9ULX7.

    Polymorphism and mutation databases

    BioMutaiCA14.
    DMDMi8928036.

    Proteomic databases

    PaxDbiQ9ULX7.
    PRIDEiQ9ULX7.

    Protocols and materials databases

    DNASUi23632.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000369111; ENSP00000358107; ENSG00000118298.
    GeneIDi23632.
    KEGGihsa:23632.
    UCSCiuc001etx.3. human.

    Organism-specific databases

    CTDi23632.
    GeneCardsiGC01P150230.
    HGNCiHGNC:1372. CA14.
    HPAiHPA008482.
    MIMi604832. gene.
    neXtProtiNX_Q9ULX7.
    PharmGKBiPA25988.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG3338.
    GeneTreeiENSGT00760000118915.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiQ9ULX7.
    KOiK01672.
    OMAiSYPECGS.
    OrthoDBiEOG7WMCK7.
    PhylomeDBiQ9ULX7.
    TreeFamiTF316425.

    Enzyme and pathway databases

    BRENDAi4.2.1.1. 2681.
    ReactomeiREACT_121123. Reversible hydration of carbon dioxide.
    SABIO-RKQ9ULX7.

    Miscellaneous databases

    ChiTaRSiCA14. human.
    GeneWikiiCA14.
    GenomeRNAii23632.
    NextBioi46407.
    PROiQ9ULX7.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9ULX7.
    CleanExiHS_CA14.
    ExpressionAtlasiQ9ULX7. baseline and differential.
    GenevisibleiQ9ULX7. HS.

    Family and domain databases

    Gene3Di3.10.200.10. 1 hit.
    InterProiIPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018431. Carbonic_anhydrase_CA14.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF84. PTHR18952:SF84. 1 hit.
    PfamiPF00194. Carb_anhydrase. 1 hit.
    [Graphical view]
    SMARTiSM01057. Carb_anhydrase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51069. SSF51069. 1 hit.
    PROSITEiPS51144. ALPHA_CA_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Human carbonic anhydrase XIV (CA14): cDNA cloning, mRNA expression, and mapping to chromosome 1."
      Fujikawa-Adachi K., Nishimori I., Taguchi T., Onishi S.
      Genomics 61:74-81(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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].
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Brain, Lung and Testis.
    7. "Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and crystallographic analysis of their adducts with isoform II: engineering proton-transfer processes within the active site of an enzyme."
      Temperini C., Scozzafava A., Vullo D., Supuran C.T.
      Chemistry 12:7057-7066(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    8. "Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII, and XIV with L- and D-phenylalanine and crystallographic analysis of their adducts with isozyme II: stereospecific recognition within the active site of an enzyme and its consequences for the drug design."
      Temperini C., Scozzafava A., Vullo D., Supuran C.T.
      J. Med. Chem. 49:3019-3027(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    9. "Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste."
      Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A., Supuran C.T., Klebe G.
      Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    10. "Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV."
      Temperini C., Innocenti A., Scozzafava A., Mastrolorenzo A., Supuran C.T.
      Bioorg. Med. Chem. Lett. 17:628-635(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    11. "Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I."
      Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S., Supuran C.T.
      Bioorg. Med. Chem. Lett. 17:2210-2215(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    12. "A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases."
      Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A., Muehlschlegel F.A., Supuran C.T.
      Bioorg. Med. Chem. Lett. 19:1371-1375(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    13. "Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors."
      Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A., Quinn R.J., Supuran C.T.
      J. Am. Chem. Soc. 131:3057-3062(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    14. "Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide."
      Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A., Pedone C., Scozzafava A., Supuran C.T., De Simone G.
      Proteins 74:164-175(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    17. "The structural comparison between membrane-associated human carbonic anhydrases provides insights into drug design of selective inhibitors."
      Alterio V., Pan P., Parkkila S., Buonanno M., Supuran C.T., Monti S.M., De Simone G.
      Biopolymers 101:769-778(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 16-290, ZINC-BINDING SITES, GLYCOSYLATION AT ASN-213, DISULFIDE BOND.

    Entry informationi

    Entry nameiCAH14_HUMAN
    AccessioniPrimary (citable) accession number: Q9ULX7
    Secondary accession number(s): Q5TB24, Q8NCF4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: July 22, 2015
    This is version 140 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.