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P04053

- TDT_HUMAN

UniProt

P04053 - TDT_HUMAN

Protein

DNA nucleotidylexotransferase

Gene

DNTT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 3 (02 Nov 2010)
      Previous versions | rss
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    Functioni

    Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells.

    Catalytic activityi

    Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

    Cofactori

    Magnesium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi253 – 2531Sodium; via carbonyl oxygenBy similarity
    Metal bindingi255 – 2551Sodium; via carbonyl oxygenBy similarity
    Metal bindingi343 – 3431MagnesiumBy similarity
    Metal bindingi345 – 3451MagnesiumBy similarity
    Metal bindingi433 – 4331MagnesiumBy similarity

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. DNA-directed DNA polymerase activity Source: InterPro
    3. DNA nucleotidylexotransferase activity Source: ProtInc
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. DNA modification Source: UniProtKB-KW

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Terminal addition

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    SABIO-RKP04053.
    SignaLinkiP04053.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA nucleotidylexotransferase (EC:2.7.7.31)
    Alternative name(s):
    Terminal addition enzyme
    Terminal deoxynucleotidyltransferase
    Short name:
    Terminal transferase
    Gene namesi
    Name:DNTT
    Synonyms:TDT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:2983. DNTT.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27449.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 509509DNA nucleotidylexotransferasePRO_0000218791Add
    BLAST

    Proteomic databases

    MaxQBiP04053.
    PaxDbiP04053.
    PRIDEiP04053.

    PTM databases

    PhosphoSiteiP04053.

    Expressioni

    Gene expression databases

    BgeeiP04053.
    CleanExiHS_DNTT.
    GenevestigatoriP04053.

    Organism-specific databases

    HPAiHPA044194.

    Interactioni

    Subunit structurei

    Interacts with PRP19 and DNTTIP1. Forms a ternary complex with DNTTIP2 and core histone. Released from this complex by PCNA.3 Publications

    Protein-protein interaction databases

    BioGridi108127. 9 interactions.
    IntActiP04053. 1 interaction.
    STRINGi9606.ENSP00000360216.

    Structurei

    Secondary structure

    1
    509
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 253
    Beta strandi36 – 405
    Turni42 – 443
    Helixi46 – 5813
    Beta strandi73 – 786
    Helixi81 – 9010
    Beta strandi100 – 1034
    Helixi104 – 1129
    Beta strandi120 – 1245

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2COENMR-A19-125[»]
    ProteinModelPortaliP04053.
    SMRiP04053. Positions 21-125, 149-509.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04053.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 12498BRCTPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni151 – 509359Mediates interaction with DNTTIP2Add
    BLAST
    Regioni336 – 34510Involved in ssDNA bindingBy similarity

    Sequence similaritiesi

    Belongs to the DNA polymerase type-X family.Curated
    Contains 1 BRCT domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1796.
    HOGENOMiHOG000263600.
    HOVERGENiHBG003670.
    InParanoidiP04053.
    KOiK00977.
    OMAiRRTTLNN.
    OrthoDBiEOG7BS4BH.
    PhylomeDBiP04053.
    TreeFamiTF103012.

    Family and domain databases

    Gene3Di1.10.150.110. 1 hit.
    3.30.210.10. 1 hit.
    3.40.50.10190. 1 hit.
    InterProiIPR001357. BRCT_dom.
    IPR002054. DNA-dir_DNA_pol_X.
    IPR019843. DNA_pol-X_BS.
    IPR010996. DNA_pol_b-like_N.
    IPR018944. DNA_pol_lambd_fingers_domain.
    IPR022312. DNA_pol_X.
    IPR027421. DNA_pol_X_lyase_dom.
    IPR002934. Nucleotidyltransferase.
    IPR029398. PolB_thumb.
    IPR027292. TdT.
    IPR001726. TdT/Mu.
    [Graphical view]
    PfamiPF00533. BRCT. 1 hit.
    PF14791. DNA_pol_B_thumb. 1 hit.
    PF10391. DNA_pol_lambd_f. 1 hit.
    PF01909. NTP_transf_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000817. DNA_NT. 1 hit.
    PIRSF501175. TDT. 1 hit.
    PRINTSiPR00869. DNAPOLX.
    PR00871. DNAPOLXTDT.
    SMARTiSM00292. BRCT. 1 hit.
    SM00483. POLXc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47802. SSF47802. 1 hit.
    SSF52113. SSF52113. 1 hit.
    PROSITEiPS50172. BRCT. 1 hit.
    PS00522. DNA_POLYMERASE_X. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P04053-1) [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

    MDPPRASHLS PRKKRPRQTG ALMASSPQDI KFQDLVVFIL EKKMGTTRRA    50
    FLMELARRKG FRVENELSDS VTHIVAENNS GSDVLEWLQA QKVQVSSQPE 100
    LLDVSWLIEC IRAGKPVEMT GKHQLVVRRD YSDSTNPGPP KTPPIAVQKI 150
    SQYACQRRTT LNNCNQIFTD AFDILAENCE FRENEDSCVT FMRAASVLKS 200
    LPFTIISMKD TEGIPCLGSK VKGIIEEIIE DGESSEVKAV LNDERYQSFK 250
    LFTSVFGVGL KTSEKWFRMG FRTLSKVRSD KSLKFTRMQK AGFLYYEDLV 300
    SCVTRAEAEA VSVLVKEAVW AFLPDAFVTM TGGFRRGKKM GHDVDFLITS 350
    PGSTEDEEQL LQKVMNLWEK KGLLLYYDLV ESTFEKLRLP SRKVDALDHF 400
    QKCFLIFKLP RQRVDSDQSS WQEGKTWKAI RVDLVLCPYE RRAFALLGWT 450
    GSRQFERDLR RYATHERKMI LDNHALYDKT KRIFLKAESE EEIFAHLGLD 500
    YIEPWERNA 509
    Length:509
    Mass (Da):58,536
    Last modified:November 2, 2010 - v3
    Checksum:i0EC01E380FA7E5A2
    GO
    Isoform 2 (identifier: P04053-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         454-454: Missing.

    Show »
    Length:508
    Mass (Da):58,408
    Checksum:iC72DABE3ACAEADD1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 511F → L in BAD97037. 1 PublicationCurated
    Sequence conflicti299 – 2991L → P in BAD97037. 1 PublicationCurated
    Sequence conflicti329 – 3291T → A in BAD97037. 1 PublicationCurated
    Sequence conflicti383 – 3831T → A in BAD97037. 1 PublicationCurated
    Sequence conflicti389 – 3891L → M in BAD97037. 1 PublicationCurated
    Sequence conflicti452 – 4521S → SP in AAA53100. (PubMed:2833741)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti112 – 1121R → G.5 Publications
    Corresponds to variant rs6584066 [ dbSNP | Ensembl ].
    VAR_058200

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei454 – 4541Missing in isoform 2. 2 PublicationsVSP_038397

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11722 mRNA. Translation: AAA36726.1.
    M20703
    , M22968, M20694, M20695, M20696, M20697, M20698, M20699, M20700, M20701, M20702 mRNA. Translation: AAA53100.1.
    AB046378 mRNA. Translation: BAB72001.1.
    AK223317 mRNA. Translation: BAD97037.1.
    AL136181 Genomic DNA. Translation: CAH72984.1.
    BC012920 mRNA. Translation: AAH12920.1.
    M21195 Genomic DNA. Translation: AAA61137.1.
    K01919 mRNA. Translation: AAA61136.1.
    CCDSiCCDS44465.1. [P04053-2]
    CCDS7447.1. [P04053-1]
    PIRiA23924. WXHU.
    RefSeqiNP_001017520.1. NM_001017520.1. [P04053-2]
    NP_004079.3. NM_004088.3. [P04053-1]
    UniGeneiHs.534206.

    Genome annotation databases

    EnsembliENST00000371174; ENSP00000360216; ENSG00000107447. [P04053-1]
    GeneIDi1791.
    KEGGihsa:1791.
    UCSCiuc001kmf.3. human. [P04053-1]
    uc001kmg.3. human. [P04053-2]

    Polymorphism databases

    DMDMi311033533.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11722 mRNA. Translation: AAA36726.1 .
    M20703
    , M22968 , M20694 , M20695 , M20696 , M20697 , M20698 , M20699 , M20700 , M20701 , M20702 mRNA. Translation: AAA53100.1 .
    AB046378 mRNA. Translation: BAB72001.1 .
    AK223317 mRNA. Translation: BAD97037.1 .
    AL136181 Genomic DNA. Translation: CAH72984.1 .
    BC012920 mRNA. Translation: AAH12920.1 .
    M21195 Genomic DNA. Translation: AAA61137.1 .
    K01919 mRNA. Translation: AAA61136.1 .
    CCDSi CCDS44465.1. [P04053-2 ]
    CCDS7447.1. [P04053-1 ]
    PIRi A23924. WXHU.
    RefSeqi NP_001017520.1. NM_001017520.1. [P04053-2 ]
    NP_004079.3. NM_004088.3. [P04053-1 ]
    UniGenei Hs.534206.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2COE NMR - A 19-125 [» ]
    ProteinModelPortali P04053.
    SMRi P04053. Positions 21-125, 149-509.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108127. 9 interactions.
    IntActi P04053. 1 interaction.
    STRINGi 9606.ENSP00000360216.

    Chemistry

    BindingDBi P04053.
    ChEMBLi CHEMBL4810.

    PTM databases

    PhosphoSitei P04053.

    Polymorphism databases

    DMDMi 311033533.

    Proteomic databases

    MaxQBi P04053.
    PaxDbi P04053.
    PRIDEi P04053.

    Protocols and materials databases

    DNASUi 1791.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371174 ; ENSP00000360216 ; ENSG00000107447 . [P04053-1 ]
    GeneIDi 1791.
    KEGGi hsa:1791.
    UCSCi uc001kmf.3. human. [P04053-1 ]
    uc001kmg.3. human. [P04053-2 ]

    Organism-specific databases

    CTDi 1791.
    GeneCardsi GC10P098054.
    H-InvDB HIX0009072.
    HGNCi HGNC:2983. DNTT.
    HPAi HPA044194.
    MIMi 187410. gene.
    neXtProti NX_P04053.
    PharmGKBi PA27449.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1796.
    HOGENOMi HOG000263600.
    HOVERGENi HBG003670.
    InParanoidi P04053.
    KOi K00977.
    OMAi RRTTLNN.
    OrthoDBi EOG7BS4BH.
    PhylomeDBi P04053.
    TreeFami TF103012.

    Enzyme and pathway databases

    SABIO-RK P04053.
    SignaLinki P04053.

    Miscellaneous databases

    EvolutionaryTracei P04053.
    GeneWikii Terminal_deoxynucleotidyl_transferase.
    GenomeRNAii 1791.
    NextBioi 7299.
    PROi P04053.
    SOURCEi Search...

    Gene expression databases

    Bgeei P04053.
    CleanExi HS_DNTT.
    Genevestigatori P04053.

    Family and domain databases

    Gene3Di 1.10.150.110. 1 hit.
    3.30.210.10. 1 hit.
    3.40.50.10190. 1 hit.
    InterProi IPR001357. BRCT_dom.
    IPR002054. DNA-dir_DNA_pol_X.
    IPR019843. DNA_pol-X_BS.
    IPR010996. DNA_pol_b-like_N.
    IPR018944. DNA_pol_lambd_fingers_domain.
    IPR022312. DNA_pol_X.
    IPR027421. DNA_pol_X_lyase_dom.
    IPR002934. Nucleotidyltransferase.
    IPR029398. PolB_thumb.
    IPR027292. TdT.
    IPR001726. TdT/Mu.
    [Graphical view ]
    Pfami PF00533. BRCT. 1 hit.
    PF14791. DNA_pol_B_thumb. 1 hit.
    PF10391. DNA_pol_lambd_f. 1 hit.
    PF01909. NTP_transf_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000817. DNA_NT. 1 hit.
    PIRSF501175. TDT. 1 hit.
    PRINTSi PR00869. DNAPOLX.
    PR00871. DNAPOLXTDT.
    SMARTi SM00292. BRCT. 1 hit.
    SM00483. POLXc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47802. SSF47802. 1 hit.
    SSF52113. SSF52113. 1 hit.
    PROSITEi PS50172. BRCT. 1 hit.
    PS00522. DNA_POLYMERASE_X. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression of human terminal deoxynucleotidyl transferase in Escherichia coli."
      Peterson R.C., Cheung L.C., Mattaliano R.J., White S.T., Chang L.M.S., Bollum F.J.
      J. Biol. Chem. 260:10495-10502(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT GLY-112.
    2. "Human terminal deoxyribonucleotidyltransferase: molecular cloning and structural analysis of the gene and 5' flanking region."
      Riley L.K., Morrow J.K., Danton M.J., Coleman M.S.
      Proc. Natl. Acad. Sci. U.S.A. 85:2489-2493(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-112.
    3. "Terminal deoxynucleotidyltransferase is negatively regulated by direct interaction with proliferating cell nuclear antigen."
      Ibe S., Fujita K., Toyomoto T., Shimazaki N., Kaneko R., Tanabe A., Takebe I., Kuroda S., Kobayashi T., Toji S., Tamai K., Yamamoto H., Koiwai O.
      Genes Cells 6:815-824(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-112.
    4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLY-112.
      Tissue: Thymus.
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [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] (ISOFORM 1), VARIANT GLY-112.
      Tissue: Testis.
    7. "Isolation of putative promoter region for human terminal deoxynucleotidyltransferase gene."
      Koiwai O., Morita A.
      Biochem. Biophys. Res. Commun. 154:91-100(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
    8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 271-508 (ISOFORM 2).
    9. "Terminal deoxynucleotidyltransferase directly interacts with a novel nuclear protein that is homologous to p65."
      Yamashita N., Shimazaki N., Ibe S., Kaneko R., Tanabe A., Toyomoto T., Fujita K., Hasegawa T., Toji S., Tamai K., Yamamoto H., Koiwai O.
      Genes Cells 6:641-652(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TDIF1.
      Tissue: Thymus.
    10. "Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone."
      Fujita K., Shimazaki N., Ohta Y., Kubota T., Ibe S., Toji S., Tamai K., Fujisaki S., Hayano T., Koiwai O.
      Genes Cells 8:559-571(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNTTIP2 AND CORE HISTONE.
    11. "Role of human Pso4 in mammalian DNA repair and association with terminal deoxynucleotidyl transferase."
      Mahajan K.N., Mitchell B.S.
      Proc. Natl. Acad. Sci. U.S.A. 100:10746-10751(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRP19.
    12. "Mutational analysis of residues in the nucleotide binding domain of human terminal deoxynucleotidyl transferase."
      Yang B., Gathy K.N., Coleman M.S.
      J. Biol. Chem. 269:11859-11868(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    13. "Solution structure of BRCT domain of terminal deoxynucleotidyltransferase."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 19-125.

    Entry informationi

    Entry nameiTDT_HUMAN
    AccessioniPrimary (citable) accession number: P04053
    Secondary accession number(s): Q53FH1, Q5W103, Q96E50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1986
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 162 of the entry and version 3 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 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3