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P13674

- P4HA1_HUMAN

UniProt

P13674 - P4HA1_HUMAN

Protein

Prolyl 4-hydroxylase subunit alpha-1

Gene

P4HA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.

    Catalytic activityi

    L-proline-[procollagen] + 2-oxoglutarate + O2 = trans-4-hydroxy-L-proline-[procollagen] + succinate + CO2.

    Cofactori

    Binds 1 Fe2+ ion per subunit.
    Ascorbate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi429 – 4291IronPROSITE-ProRule annotation
    Metal bindingi431 – 4311IronPROSITE-ProRule annotation
    Metal bindingi500 – 5001IronPROSITE-ProRule annotation
    Binding sitei510 – 51012-oxoglutaratePROSITE-ProRule annotation

    GO - Molecular functioni

    1. iron ion binding Source: InterPro
    2. L-ascorbic acid binding Source: UniProtKB-KW
    3. oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Source: InterPro
    4. procollagen-proline 4-dioxygenase activity Source: ProtInc
    5. protein binding Source: IntAct

    GO - Biological processi

    1. collagen fibril organization Source: Ensembl
    2. peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: Ensembl

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Iron, Metal-binding, Vitamin C

    Enzyme and pathway databases

    BRENDAi1.14.11.2. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prolyl 4-hydroxylase subunit alpha-1 (EC:1.14.11.2)
    Short name:
    4-PH alpha-1
    Alternative name(s):
    Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1
    Gene namesi
    Name:P4HA1
    Synonyms:P4HA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:8546. P4HA1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: HPA
    2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    3. intracellular membrane-bounded organelle Source: HPA
    4. membrane Source: UniProtKB
    5. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi210 – 2101Y → A: Strongly reduced affinity for peptide substrate. 1 Publication
    Mutagenesisi213 – 2131Y → A: Strongly reduced affinity for peptide substrate. 1 Publication
    Mutagenesisi247 – 2471Y → A: Strongly reduced affinity for peptide substrate. 1 Publication

    Organism-specific databases

    PharmGKBiPA32874.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Add
    BLAST
    Chaini18 – 534517Prolyl 4-hydroxylase subunit alpha-1PRO_0000022723Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi113 – 1131N-linked (GlcNAc...)1 Publication
    Glycosylationi259 – 2591N-linked (GlcNAc...)

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiP13674.
    PaxDbiP13674.
    PRIDEiP13674.

    PTM databases

    PhosphoSiteiP13674.

    Expressioni

    Gene expression databases

    ArrayExpressiP13674.
    BgeeiP13674.
    CleanExiHS_P4HA1.
    GenevestigatoriP13674.

    Organism-specific databases

    HPAiHPA007599.
    HPA026593.

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha-1 chains and two beta chains (the beta chain is the multi-functional PDI).1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HTTP428585EBI-1237386,EBI-466029

    Protein-protein interaction databases

    BioGridi111072. 13 interactions.
    DIPiDIP-38180N.
    IntActiP13674. 7 interactions.
    MINTiMINT-4657265.
    STRINGi9606.ENSP00000263556.

    Structurei

    Secondary structure

    1
    534
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 7151
    Helixi74 – 796
    Helixi81 – 9212
    Helixi94 – 10310
    Helixi108 – 11811
    Helixi124 – 14118
    Helixi145 – 1495
    Beta strandi153 – 1564
    Helixi164 – 17613
    Helixi180 – 19516
    Helixi204 – 21714
    Helixi221 – 23414
    Helixi239 – 25214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TJCX-ray2.30A/B161-261[»]
    2V5FX-ray2.03A161-263[»]
    2YQ8X-ray2.99A/B18-255[»]
    4BT8X-ray2.20A/B18-255[»]
    4BT9X-ray1.90A/B18-255[»]
    4BTAX-ray2.95A/B18-261[»]
    4BTBX-ray1.90A18-255[»]
    ProteinModelPortaliP13674.
    SMRiP13674. Positions 18-254, 335-518.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13674.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati205 – 23834TPRAdd
    BLAST
    Domaini411 – 519109Fe2OG dioxygenasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the P4HA family.Curated
    Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation
    Contains 1 TPR repeat.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, TPR repeat

    Phylogenomic databases

    eggNOGiNOG78926.
    HOGENOMiHOG000230465.
    HOVERGENiHBG006834.
    InParanoidiP13674.
    KOiK00472.
    OMAiNDEDQIG.
    OrthoDBiEOG7W6WKC.
    PhylomeDBiP13674.
    TreeFamiTF313393.

    Family and domain databases

    Gene3Di1.25.40.10. 2 hits.
    InterProiIPR005123. Oxoglu/Fe-dep_dioxygenase.
    IPR006620. Pro_4_hyd_alph.
    IPR013547. Pro_4_hyd_alph_N.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR019734. TPR_repeat.
    [Graphical view]
    PfamiPF03171. 2OG-FeII_Oxy. 1 hit.
    PF08336. P4Ha_N. 1 hit.
    [Graphical view]
    SMARTiSM00702. P4Hc. 1 hit.
    [Graphical view]
    PROSITEiPS51471. FE2OG_OXY. 1 hit.
    PS50005. TPR. 1 hit.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P13674-1) [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

    MIWYILIIGI LLPQSLAHPG FFTSIGQMTD LIHTEKDLVT SLKDYIKAEE    50
    DKLEQIKKWA EKLDRLTSTA TKDPEGFVGH PVNAFKLMKR LNTEWSELEN 100
    LVLKDMSDGF ISNLTIQRQY FPNDEDQVGA AKALLRLQDT YNLDTDTISK 150
    GNLPGVKHKS FLTAEDCFEL GKVAYTEADY YHTELWMEQA LRQLDEGEIS 200
    TIDKVSVLDY LSYAVYQQGD LDKALLLTKK LLELDPEHQR ANGNLKYFEY 250
    IMAKEKDVNK SASDDQSDQK TTPKKKGVAV DYLPERQKYE MLCRGEGIKM 300
    TPRRQKKLFC RYHDGNRNPK FILAPAKQED EWDKPRIIRF HDIISDAEIE 350
    IVKDLAKPRL RRATISNPIT GDLETVHYRI SKSAWLSGYE NPVVSRINMR 400
    IQDLTGLDVS TAEELQVANY GVGGQYEPHF DFARKDEPDA FKELGTGNRI 450
    ATWLFYMSDV SAGGATVFPE VGASVWPKKG TAVFWYNLFA SGEGDYSTRH 500
    AACPVLVGNK WVSNKWLHER GQEFRRPCTL SELE 534
    Length:534
    Mass (Da):61,049
    Last modified:November 1, 1997 - v2
    Checksum:iEBAFA8CCF09A1DDB
    GO
    Isoform 2 (identifier: P13674-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         361-380: RRATISNPITGDLETVHYRI → SRATVHDPETGKLTTAQYRV

    Show »
    Length:534
    Mass (Da):60,967
    Checksum:i5FE1B10A8AC5E792
    GO
    Isoform 3 (identifier: P13674-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         361-380: RRATISNPITGDLETVHYRI → SRATVHDPETGKLTTAQYRV
         417-434: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:516
    Mass (Da):58,958
    Checksum:iED30BECCFB48CD7E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti119 – 1224QYFP → PVLS in AAA36534. (PubMed:2543975)Curated
    Sequence conflicti119 – 1224QYFP → PVLS in AAA36535. (PubMed:2543975)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei361 – 38020RRATI…VHYRI → SRATVHDPETGKLTTAQYRV in isoform 2 and isoform 3. 2 PublicationsVSP_004504Add
    BLAST
    Alternative sequencei417 – 43418Missing in isoform 3. 1 PublicationVSP_044578Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24486 mRNA. Translation: AAA36534.1.
    M24487 mRNA. Translation: AAA36535.1.
    U14620
    , U14607, U14605, U14608, U14609, U14611, U14610, U14612, U14614, U14615, U14616, U14617, U14618, U14619 Genomic DNA. Translation: AAA59068.1.
    U14620
    , U14607, U14605, U14608, U14609, U14611, U14610, U14612, U14613, U14615, U14616, U14617, U14618, U14619 Genomic DNA. Translation: AAA59069.1.
    CD013929 Genomic DNA. No translation available.
    AL731563 Genomic DNA. Translation: CAH72754.1.
    BC034998 mRNA. Translation: AAH34998.1.
    CCDSiCCDS41537.1. [P13674-1]
    CCDS44432.1. [P13674-3]
    CCDS7320.1. [P13674-2]
    PIRiA33919. DAHUA1.
    I37173. DAHUA2.
    RefSeqiNP_000908.2. NM_000917.3. [P13674-2]
    NP_001017962.1. NM_001017962.2. [P13674-1]
    NP_001136067.1. NM_001142595.1. [P13674-1]
    NP_001136068.1. NM_001142596.1. [P13674-3]
    UniGeneiHs.500047.
    Hs.593005.

    Genome annotation databases

    EnsembliENST00000263556; ENSP00000263556; ENSG00000122884. [P13674-2]
    ENST00000307116; ENSP00000307318; ENSG00000122884. [P13674-1]
    ENST00000373008; ENSP00000362099; ENSG00000122884. [P13674-2]
    ENST00000394890; ENSP00000378353; ENSG00000122884. [P13674-1]
    ENST00000440381; ENSP00000414464; ENSG00000122884. [P13674-3]
    GeneIDi5033.
    KEGGihsa:5033.
    UCSCiuc001jtg.3. human. [P13674-1]

    Polymorphism databases

    DMDMi2507090.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24486 mRNA. Translation: AAA36534.1 .
    M24487 mRNA. Translation: AAA36535.1 .
    U14620
    , U14607 , U14605 , U14608 , U14609 , U14611 , U14610 , U14612 , U14614 , U14615 , U14616 , U14617 , U14618 , U14619 Genomic DNA. Translation: AAA59068.1 .
    U14620
    , U14607 , U14605 , U14608 , U14609 , U14611 , U14610 , U14612 , U14613 , U14615 , U14616 , U14617 , U14618 , U14619 Genomic DNA. Translation: AAA59069.1 .
    CD013929 Genomic DNA. No translation available.
    AL731563 Genomic DNA. Translation: CAH72754.1 .
    BC034998 mRNA. Translation: AAH34998.1 .
    CCDSi CCDS41537.1. [P13674-1 ]
    CCDS44432.1. [P13674-3 ]
    CCDS7320.1. [P13674-2 ]
    PIRi A33919. DAHUA1.
    I37173. DAHUA2.
    RefSeqi NP_000908.2. NM_000917.3. [P13674-2 ]
    NP_001017962.1. NM_001017962.2. [P13674-1 ]
    NP_001136067.1. NM_001142595.1. [P13674-1 ]
    NP_001136068.1. NM_001142596.1. [P13674-3 ]
    UniGenei Hs.500047.
    Hs.593005.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TJC X-ray 2.30 A/B 161-261 [» ]
    2V5F X-ray 2.03 A 161-263 [» ]
    2YQ8 X-ray 2.99 A/B 18-255 [» ]
    4BT8 X-ray 2.20 A/B 18-255 [» ]
    4BT9 X-ray 1.90 A/B 18-255 [» ]
    4BTA X-ray 2.95 A/B 18-261 [» ]
    4BTB X-ray 1.90 A 18-255 [» ]
    ProteinModelPortali P13674.
    SMRi P13674. Positions 18-254, 335-518.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111072. 13 interactions.
    DIPi DIP-38180N.
    IntActi P13674. 7 interactions.
    MINTi MINT-4657265.
    STRINGi 9606.ENSP00000263556.

    Chemistry

    ChEMBLi CHEMBL1250350.
    DrugBanki DB01275. Hydralazine.
    DB00172. L-Proline.
    DB00139. Succinic acid.
    DB00126. Vitamin C.

    PTM databases

    PhosphoSitei P13674.

    Polymorphism databases

    DMDMi 2507090.

    Proteomic databases

    MaxQBi P13674.
    PaxDbi P13674.
    PRIDEi P13674.

    Protocols and materials databases

    DNASUi 5033.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263556 ; ENSP00000263556 ; ENSG00000122884 . [P13674-2 ]
    ENST00000307116 ; ENSP00000307318 ; ENSG00000122884 . [P13674-1 ]
    ENST00000373008 ; ENSP00000362099 ; ENSG00000122884 . [P13674-2 ]
    ENST00000394890 ; ENSP00000378353 ; ENSG00000122884 . [P13674-1 ]
    ENST00000440381 ; ENSP00000414464 ; ENSG00000122884 . [P13674-3 ]
    GeneIDi 5033.
    KEGGi hsa:5033.
    UCSCi uc001jtg.3. human. [P13674-1 ]

    Organism-specific databases

    CTDi 5033.
    GeneCardsi GC10M074767.
    HGNCi HGNC:8546. P4HA1.
    HPAi HPA007599.
    HPA026593.
    MIMi 176710. gene.
    neXtProti NX_P13674.
    PharmGKBi PA32874.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG78926.
    HOGENOMi HOG000230465.
    HOVERGENi HBG006834.
    InParanoidi P13674.
    KOi K00472.
    OMAi NDEDQIG.
    OrthoDBi EOG7W6WKC.
    PhylomeDBi P13674.
    TreeFami TF313393.

    Enzyme and pathway databases

    BRENDAi 1.14.11.2. 2681.

    Miscellaneous databases

    EvolutionaryTracei P13674.
    GeneWikii P4HA1.
    GenomeRNAii 5033.
    NextBioi 19392.
    PROi P13674.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13674.
    Bgeei P13674.
    CleanExi HS_P4HA1.
    Genevestigatori P13674.

    Family and domain databases

    Gene3Di 1.25.40.10. 2 hits.
    InterProi IPR005123. Oxoglu/Fe-dep_dioxygenase.
    IPR006620. Pro_4_hyd_alph.
    IPR013547. Pro_4_hyd_alph_N.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF03171. 2OG-FeII_Oxy. 1 hit.
    PF08336. P4Ha_N. 1 hit.
    [Graphical view ]
    SMARTi SM00702. P4Hc. 1 hit.
    [Graphical view ]
    PROSITEi PS51471. FE2OG_OXY. 1 hit.
    PS50005. TPR. 1 hit.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts."
      Helaakoski T., Vuori K., Myllylae R., Kivirikko K.I., Pihlajaniemi T.
      Proc. Natl. Acad. Sci. U.S.A. 86:4392-4396(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    2. "Structure and expression of the human gene for the alpha subunit of prolyl 4-hydroxylase. The two alternatively spliced types of mRNA correspond to two homologous exons the sequences of which are expressed in a variety of tissues."
      Helaakoski T., Veijola J., Vuori K., Rehn M., Chow L.T., Taillon-Miller P., Kivirikko K.I., Pihlajaniemi T.
      J. Biol. Chem. 269:27847-27854(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    3. "PCR isolation and cloning of novel splice variant mRNAs from known drug target genes."
      Jin P., Fu G.K., Wilson A.D., Yang J., Chien D., Hawkins P.R., Au-Young J., Stuve L.L.
      Genomics 83:566-571(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    4. "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].
    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 1).
      Tissue: Brain.
    6. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-113.
      Tissue: Liver.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residues."
      Pekkala M., Hieta R., Bergmann U., Kivirikko K.I., Wierenga R.K., Myllyharju J.
      J. Biol. Chem. 279:52255-52261(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 161-261, SUBUNIT, MUTAGENESIS OF TYR-210; TYR-213 AND TYR-247.

    Entry informationi

    Entry nameiP4HA1_HUMAN
    AccessioniPrimary (citable) accession number: P13674
    Secondary accession number(s): C9JL12
    , Q15082, Q15083, Q5VSQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 167 of the entry and version 2 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. 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