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Q9ULX7

- CAH14_HUMAN

UniProt

Q9ULX7 - CAH14_HUMAN

Protein

Carbonic anhydrase 14

Gene

CA14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Reversible hydration of carbon dioxide.

    Catalytic activityi

    H2CO3 = CO2 + H2O.

    Cofactori

    Zinc.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; catalyticBy similarity
    Metal bindingi111 – 1111Zinc; catalyticBy similarity
    Metal bindingi135 – 1351Zinc; catalyticBy similarity
    Active sitei144 – 1441By similarity

    GO - Molecular functioni

    1. carbonate dehydratase activity Source: ProtInc
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. bicarbonate transport Source: Reactome
    2. small molecule metabolic process Source: Reactome

    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: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1372. CA14.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: ProtInc
    2. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25988.

    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 ↔ 221By similarity
    Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
    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

    ArrayExpressiQ9ULX7.
    BgeeiQ9ULX7.
    CleanExiHS_CA14.
    GenevestigatoriQ9ULX7.

    Organism-specific databases

    HPAiHPA008482.

    Interactioni

    Protein-protein interaction databases

    BioGridi117162. 1 interaction.
    IntActiQ9ULX7. 1 interaction.
    STRINGi9606.ENSP00000358107.

    Structurei

    Secondary structure

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

    3D structure databases

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

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei291 – 31121HelicalSequence AnalysisAdd
    BLAST

    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.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiQ9ULX7.
    KOiK01672.
    OMAiHWPASYP.
    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

    MLFSALLLEV IWILAADGGQ HWTYEGPHGQ DHWPASYPEC GNNAQSPIDI    50
    QTDSVTFDPD LPALQPHGYD QPGTEPLDLH NNGHTVQLSL PSTLYLGGLP 100
    RKYVAAQLHL HWGQKGSPGG SEHQINSEAT FAELHIVHYD SDSYDSLSEA 150
    AERPQGLAVL GILIEVGETK NIAYEHILSH LHEVRHKDQK TSVPPFNLRE 200
    LLPKQLGQYF RYNGSLTTPP CYQSVLWTVF YRRSQISMEQ LEKLQGTLFS 250
    TEEEPSKLLV QNYRALQPLN QRMVFASFIQ AGSSYTTGEM LSLGVGILVG 300
    CLCLLLAVYF IARKIRKKRL ENRKSVVFTS AQATTEA 337
    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:
    EMBL
    GenBank
    DDBJ
    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_012113.1.
    UniGeneiHs.528988.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi8928036.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS947.1.
    RefSeqi NP_036245.1. NM_012113.1.
    UniGenei Hs.528988.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4LU3 X-ray 2.00 A 16-290 [» ]
    ProteinModelPortali Q9ULX7.
    SMRi Q9ULX7. Positions 21-286.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117162. 1 interaction.
    IntActi Q9ULX7. 1 interaction.
    STRINGi 9606.ENSP00000358107.

    Chemistry

    BindingDBi Q9ULX7.
    ChEMBLi CHEMBL3510.
    GuidetoPHARMACOLOGYi 2598.

    PTM databases

    PhosphoSitei Q9ULX7.

    Polymorphism databases

    DMDMi 8928036.

    Proteomic databases

    PaxDbi Q9ULX7.
    PRIDEi Q9ULX7.

    Protocols and materials databases

    DNASUi 23632.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369111 ; ENSP00000358107 ; ENSG00000118298 .
    GeneIDi 23632.
    KEGGi hsa:23632.
    UCSCi uc001etx.3. human.

    Organism-specific databases

    CTDi 23632.
    GeneCardsi GC01P150230.
    HGNCi HGNC:1372. CA14.
    HPAi HPA008482.
    MIMi 604832. gene.
    neXtProti NX_Q9ULX7.
    PharmGKBi PA25988.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3338.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi Q9ULX7.
    KOi K01672.
    OMAi HWPASYP.
    OrthoDBi EOG7WMCK7.
    PhylomeDBi Q9ULX7.
    TreeFami TF316425.

    Enzyme and pathway databases

    BRENDAi 4.2.1.1. 2681.
    Reactomei REACT_121123. Reversible hydration of carbon dioxide.
    SABIO-RK Q9ULX7.

    Miscellaneous databases

    ChiTaRSi CA14. human.
    GeneWikii CA14.
    GenomeRNAii 23632.
    NextBioi 46407.
    PROi Q9ULX7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ULX7.
    Bgeei Q9ULX7.
    CleanExi HS_CA14.
    Genevestigatori Q9ULX7.

    Family and domain databases

    Gene3Di 3.10.200.10. 1 hit.
    InterProi IPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018431. Carbonic_anhydrase_CA14.
    [Graphical view ]
    PANTHERi PTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF84. PTHR18952:SF84. 1 hit.
    Pfami PF00194. Carb_anhydrase. 1 hit.
    [Graphical view ]
    SMARTi SM01057. Carb_anhydrase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51069. SSF51069. 1 hit.
    PROSITEi PS51144. ALPHA_CA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].

    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: October 1, 2014
    This is version 132 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