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Q9ULX7

- CAH14_HUMAN

UniProt

Q9ULX7 - CAH14_HUMAN

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Protein
Carbonic anhydrase 14
Gene
CA14, UNQ690/PRO1335
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 acceptor By similarity
Metal bindingi109 – 1091Zinc; catalytic By similarity
Metal bindingi111 – 1111Zinc; catalytic By similarity
Metal bindingi135 – 1351Zinc; catalytic By similarity
Active sitei144 – 1441 By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. bicarbonate transport Source: Reactome
  2. small molecule metabolic process Source: Reactome
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-RKiQ9ULX7.

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini16 – 290275Extracellular Reviewed prediction
Add
BLAST
Transmembranei291 – 31121Helical; Reviewed prediction
Add
BLAST
Topological domaini312 – 33726Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25988.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515 Reviewed prediction
Add
BLAST
Chaini16 – 337322Carbonic anhydrase 14
PRO_0000004251Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 ↔ 221 By similarity
Glycosylationi213 – 2131N-linked (GlcNAc...) Reviewed prediction
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

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.

Family & Domainsi

Region

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

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti229 – 2291V → A in BAC11191. 1 Publication

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...

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-RKi 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

« 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].

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: September 3, 2014
This is version 131 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

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