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Q9BQS7

- HEPH_HUMAN

UniProt

Q9BQS7 - HEPH_HUMAN

Protein

Hephaestin

Gene

HEPH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 3 (27 Sep 2004)
      Previous versions | rss
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    Functioni

    May function as a ferroxidase for ferrous (II) to ferric ion (III) conversion and may be involved in copper transport and homeostasis. Implicated in iron homeostasis and may mediate iron efflux associated to ferroportin 1.

    Cofactori

    Binds 6 copper ions per monomer.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi126 – 1261Copper 1; type 2By similarity
    Metal bindingi128 – 1281Copper 2; type 3By similarity
    Metal bindingi186 – 1861Copper 2; type 3By similarity
    Metal bindingi188 – 1881Copper 3; type 3By similarity
    Metal bindingi304 – 3041Copper 4; type 1By similarity
    Metal bindingi347 – 3471Copper 4; type 1By similarity
    Metal bindingi352 – 3521Copper 4; type 1By similarity
    Metal bindingi656 – 6561Copper 5; type 1By similarity
    Metal bindingi699 – 6991Copper 5; type 1By similarity
    Metal bindingi704 – 7041Copper 5; type 1By similarity
    Metal bindingi709 – 7091Copper 5; type 1By similarity
    Metal bindingi1000 – 10001Copper 6; type 1By similarity
    Metal bindingi1003 – 10031Copper 1; type 2By similarity
    Metal bindingi1005 – 10051Copper 3; type 3By similarity
    Metal bindingi1045 – 10451Copper 3; type 3By similarity
    Metal bindingi1046 – 10461Copper 6; type 1By similarity
    Metal bindingi1047 – 10471Copper 2; type 3By similarity
    Metal bindingi1051 – 10511Copper 6; type 1By similarity
    Metal bindingi1056 – 10561Copper 6; type 1By similarity

    GO - Molecular functioni

    1. copper ion binding Source: UniProt
    2. ferrous iron binding Source: UniProt
    3. ferroxidase activity Source: UniProt

    GO - Biological processi

    1. cellular iron ion homeostasis Source: Reactome
    2. copper ion transport Source: UniProtKB-KW
    3. iron ion transport Source: UniProt
    4. transmembrane transport Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Copper transport, Ion transport, Iron transport, Transport

    Keywords - Ligandi

    Copper, Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_20547. Metal ion SLC transporters.
    REACT_25060. Iron uptake and transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hephaestin (EC:1.-.-.-)
    Gene namesi
    Name:HEPH
    Synonyms:KIAA0698
    ORF Names:UNQ2562/PRO6242
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:4866. HEPH.

    Subcellular locationi

    GO - Cellular componenti

    1. basolateral plasma membrane Source: UniProt
    2. integral component of membrane Source: UniProtKB-KW
    3. intracellular Source: UniProt
    4. perinuclear region of cytoplasm Source: Ensembl
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29241.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 11581135HephaestinPRO_0000002915Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi180 ↔ 206Sequence Analysis
    Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi285 ↔ 366Sequence Analysis
    Disulfide bondi534 ↔ 560Sequence Analysis
    Glycosylationi588 – 5881N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi637 ↔ 718Sequence Analysis
    Glycosylationi714 – 7141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi758 – 7581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi829 – 8291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi873 – 8731N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi877 ↔ 903Sequence Analysis
    Glycosylationi931 – 9311N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ9BQS7.
    PaxDbiQ9BQS7.
    PRIDEiQ9BQS7.

    PTM databases

    PhosphoSiteiQ9BQS7.

    Expressioni

    Tissue specificityi

    Detected in breast, colon, bone trabecular cells and fibroblasts.

    Gene expression databases

    ArrayExpressiQ9BQS7.
    BgeeiQ9BQS7.
    CleanExiHS_HEPH.
    GenevestigatoriQ9BQS7.

    Organism-specific databases

    HPAiHPA005824.

    Interactioni

    Protein-protein interaction databases

    BioGridi115179. 1 interaction.
    STRINGi9606.ENSP00000403834.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BQS7.
    SMRiQ9BQS7. Positions 28-1065.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 11101087ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1132 – 115827CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1111 – 113121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 206183Plastocyanin-like 1Add
    BLAST
    Domaini218 – 366149Plastocyanin-like 2Add
    BLAST
    Domaini379 – 560182Plastocyanin-like 3Add
    BLAST
    Domaini570 – 718149Plastocyanin-like 4Add
    BLAST
    Domaini731 – 903173Plastocyanin-like 5Add
    BLAST
    Domaini911 – 1087177Plastocyanin-like 6Add
    BLAST

    Sequence similaritiesi

    Belongs to the multicopper oxidase family.Curated
    Contains 6 plastocyanin-like domains.Curated

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG276067.
    HOGENOMiHOG000231499.
    HOVERGENiHBG003674.
    InParanoidiQ9BQS7.
    KOiK14735.
    OMAiLIHLKNF.
    OrthoDBiEOG7V49XN.
    PhylomeDBiQ9BQS7.
    TreeFamiTF329807.

    Family and domain databases

    Gene3Di2.60.40.420. 6 hits.
    InterProiIPR011706. Cu-oxidase_2.
    IPR011707. Cu-oxidase_3.
    IPR002355. Cu_oxidase_Cu_BS.
    IPR008972. Cupredoxin.
    IPR027154. HEPH.
    [Graphical view]
    PANTHERiPTHR10127:SF317. PTHR10127:SF317. 1 hit.
    PfamiPF07731. Cu-oxidase_2. 1 hit.
    PF07732. Cu-oxidase_3. 2 hits.
    [Graphical view]
    SUPFAMiSSF49503. SSF49503. 6 hits.
    PROSITEiPS00079. MULTICOPPER_OXIDASE1. 3 hits.
    PS00080. MULTICOPPER_OXIDASE2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BQS7-1) [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

    MESGHLLWAL LFMQSLWPQL TDGATRVYYL GIRDVQWNYA PKGRNVITNQ     50
    PLDSDIVASS FLKSDKNRIG GTYKKTIYKE YKDDSYTDEV AQPAWLGFLG 100
    PVLQAEVGDV ILIHLKNFAT RPYTIHPHGV FYEKDSEGSL YPDGSSGPLK 150
    ADDSVPPGGS HIYNWTIPEG HAPTDADPAC LTWIYHSHVD APRDIATGLI 200
    GPLITCKRGA LDGNSPPQRQ DVDHDFFLLF SVVDENLSWH LNENIATYCS 250
    DPASVDKEDE TFQESNRMHA INGFVFGNLP ELNMCAQKRV AWHLFGMGNE 300
    IDVHTAFFHG QMLTTRGHHT DVANIFPATF VTAEMVPWEP GTWLISCQVN 350
    SHFRDGMQAL YKVKSCSMAP PVDLLTGKVR QYFIEAHEIQ WDYGPMGHDG 400
    STGKNLREPG SISDKFFQKS SSRIGGTYWK VRYEAFQDET FQEKMHLEED 450
    RHLGILGPVI RAEVGDTIQV VFYNRASQPF SMQPHGVFYE KDYEGTVYND 500
    GSSYPGLVAK PFEKVTYRWT VPPHAGPTAQ DPACLTWMYF SAADPIRDTN 550
    SGLVGPLLVC RAGALGADGK QKGVDKEFFL LFTVLDENKS WYSNANQAAA 600
    MLDFRLLSED IEGFQDSNRM HAINGFLFSN LPRLDMCKGD TVAWHLLGLG 650
    TETDVHGVMF QGNTVQLQGM RKGAAMLFPH TFVMAIMQPD NLGTFEIYCQ 700
    AGSHREAGMR AIYNVSQCPG HQATPRQRYQ AARIYYIMAE EVEWDYCPDR 750
    SWEREWHNQS EKDSYGYIFL SNKDGLLGSR YKKAVFREYT DGTFRIPRPR 800
    TGPEEHLGIL GPLIKGEVGD ILTVVFKNNA SRPYSVHAHG VLESTTVWPL 850
    AAEPGEVVTY QWNIPERSGP GPNDSACVSW IYYSAVDPIK DMYSGLVGPL 900
    AICQKGILEP HGGRSDMDRE FALLFLIFDE NKSWYLEENV ATHGSQDPGS 950
    INLQDETFLE SNKMHAINGK LYANLRGLTM YQGERVAWYM LAMGQDVDLH 1000
    TIHFHAESFL YRNGENYRAD VVDLFPGTFE VVEMVASNPG TWLMHCHVTD 1050
    HVHAGMETLF TVFSRTEHLS PLTVITKETE KAVPPRDIEE GNVKMLGMQI 1100
    PIKNVEMLAS VLVAISVTLL LVVLALGGVV WYQHRQRKLR RNRRSILDDS 1150
    FKLLSFKQ 1158
    Length:1,158
    Mass (Da):130,449
    Last modified:September 27, 2004 - v3
    Checksum:iCD032199E2E2868D
    GO
    Isoform 2 (identifier: Q9BQS7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1082-1082: Missing.

    Show »
    Length:1,157
    Mass (Da):130,378
    Checksum:i3DCFE053093BFA7D
    GO
    Isoform 3 (identifier: Q9BQS7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MTQTLPYHLSLLNVLFPGPCSRHFKFRRGKCAQPAWRKVSAPSQDLLITKVMWAM

    Note: No experimental confirmation available.

    Show »
    Length:1,212
    Mass (Da):136,658
    Checksum:i9C03D79DAE69BA8C
    GO
    Isoform 4 (identifier: Q9BQS7-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-267: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:891
    Mass (Da):100,624
    Checksum:iAB70D0436109C5B2
    GO

    Sequence cautioni

    The sequence AAQ89349.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence EAX05385.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence EAX05388.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 562DI → QR in BAA31673. (PubMed:9734811)Curated
    Sequence conflicti222 – 2221V → T in CAC35365. (PubMed:11932491)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti595 – 5951A → T.
    Corresponds to variant rs17216603 [ dbSNP | Ensembl ].
    VAR_024379

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 267267Missing in isoform 4. CuratedVSP_047332Add
    BLAST
    Alternative sequencei1 – 11M → MTQTLPYHLSLLNVLFPGPC SRHFKFRRGKCAQPAWRKVS APSQDLLITKVMWAM in isoform 3. CuratedVSP_047331
    Alternative sequencei1082 – 10821Missing in isoform 2. 1 PublicationVSP_011627

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ296162 mRNA. Translation: CAC35365.2.
    AF148860 mRNA. Translation: AAK08131.1.
    AY358990 mRNA. Translation: AAQ89349.1. Different initiation.
    AL030998 Genomic DNA. No translation available.
    AL157698 Genomic DNA. No translation available.
    CH471132 Genomic DNA. Translation: EAX05384.1.
    CH471132 Genomic DNA. Translation: EAX05385.1. Different initiation.
    CH471132 Genomic DNA. Translation: EAX05386.1.
    CH471132 Genomic DNA. Translation: EAX05388.1. Different initiation.
    BC011561 mRNA. Translation: AAH11561.1.
    AB014598 mRNA. Translation: BAA31673.2.
    CCDSiCCDS14384.3. [Q9BQS7-3]
    CCDS14385.1. [Q9BQS7-4]
    RefSeqiNP_001124332.1. NM_001130860.3.
    NP_001269070.1. NM_001282141.1.
    NP_055614.1. NM_014799.3. [Q9BQS7-4]
    NP_620074.3. NM_138737.4. [Q9BQS7-3]
    XP_006724785.1. XM_006724722.1.
    UniGeneiHs.31720.

    Genome annotation databases

    EnsembliENST00000336279; ENSP00000337418; ENSG00000089472. [Q9BQS7-4]
    ENST00000343002; ENSP00000343939; ENSG00000089472. [Q9BQS7-1]
    ENST00000441993; ENSP00000411687; ENSG00000089472.
    ENST00000519389; ENSP00000430620; ENSG00000089472. [Q9BQS7-3]
    GeneIDi9843.
    KEGGihsa:9843.
    UCSCiuc004dwn.3. human. [Q9BQS7-2]
    uc004dwo.3. human. [Q9BQS7-1]

    Polymorphism databases

    DMDMi52782976.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Hephaestin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ296162 mRNA. Translation: CAC35365.2 .
    AF148860 mRNA. Translation: AAK08131.1 .
    AY358990 mRNA. Translation: AAQ89349.1 . Different initiation.
    AL030998 Genomic DNA. No translation available.
    AL157698 Genomic DNA. No translation available.
    CH471132 Genomic DNA. Translation: EAX05384.1 .
    CH471132 Genomic DNA. Translation: EAX05385.1 . Different initiation.
    CH471132 Genomic DNA. Translation: EAX05386.1 .
    CH471132 Genomic DNA. Translation: EAX05388.1 . Different initiation.
    BC011561 mRNA. Translation: AAH11561.1 .
    AB014598 mRNA. Translation: BAA31673.2 .
    CCDSi CCDS14384.3. [Q9BQS7-3 ]
    CCDS14385.1. [Q9BQS7-4 ]
    RefSeqi NP_001124332.1. NM_001130860.3.
    NP_001269070.1. NM_001282141.1.
    NP_055614.1. NM_014799.3. [Q9BQS7-4 ]
    NP_620074.3. NM_138737.4. [Q9BQS7-3 ]
    XP_006724785.1. XM_006724722.1.
    UniGenei Hs.31720.

    3D structure databases

    ProteinModelPortali Q9BQS7.
    SMRi Q9BQS7. Positions 28-1065.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115179. 1 interaction.
    STRINGi 9606.ENSP00000403834.

    PTM databases

    PhosphoSitei Q9BQS7.

    Polymorphism databases

    DMDMi 52782976.

    Proteomic databases

    MaxQBi Q9BQS7.
    PaxDbi Q9BQS7.
    PRIDEi Q9BQS7.

    Protocols and materials databases

    DNASUi 9843.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336279 ; ENSP00000337418 ; ENSG00000089472 . [Q9BQS7-4 ]
    ENST00000343002 ; ENSP00000343939 ; ENSG00000089472 . [Q9BQS7-1 ]
    ENST00000441993 ; ENSP00000411687 ; ENSG00000089472 .
    ENST00000519389 ; ENSP00000430620 ; ENSG00000089472 . [Q9BQS7-3 ]
    GeneIDi 9843.
    KEGGi hsa:9843.
    UCSCi uc004dwn.3. human. [Q9BQS7-2 ]
    uc004dwo.3. human. [Q9BQS7-1 ]

    Organism-specific databases

    CTDi 9843.
    GeneCardsi GC0XP065299.
    H-InvDB HIX0016844.
    HGNCi HGNC:4866. HEPH.
    HPAi HPA005824.
    MIMi 300167. gene.
    neXtProti NX_Q9BQS7.
    PharmGKBi PA29241.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG276067.
    HOGENOMi HOG000231499.
    HOVERGENi HBG003674.
    InParanoidi Q9BQS7.
    KOi K14735.
    OMAi LIHLKNF.
    OrthoDBi EOG7V49XN.
    PhylomeDBi Q9BQS7.
    TreeFami TF329807.

    Enzyme and pathway databases

    Reactomei REACT_20547. Metal ion SLC transporters.
    REACT_25060. Iron uptake and transport.

    Miscellaneous databases

    GenomeRNAii 9843.
    NextBioi 37092.
    PROi Q9BQS7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BQS7.
    Bgeei Q9BQS7.
    CleanExi HS_HEPH.
    Genevestigatori Q9BQS7.

    Family and domain databases

    Gene3Di 2.60.40.420. 6 hits.
    InterProi IPR011706. Cu-oxidase_2.
    IPR011707. Cu-oxidase_3.
    IPR002355. Cu_oxidase_Cu_BS.
    IPR008972. Cupredoxin.
    IPR027154. HEPH.
    [Graphical view ]
    PANTHERi PTHR10127:SF317. PTHR10127:SF317. 1 hit.
    Pfami PF07731. Cu-oxidase_2. 1 hit.
    PF07732. Cu-oxidase_3. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49503. SSF49503. 6 hits.
    PROSITEi PS00079. MULTICOPPER_OXIDASE1. 3 hits.
    PS00080. MULTICOPPER_OXIDASE2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of the human hephaestin gene and protein: comparative modelling of the N-terminus ecto-domain based upon ceruloplasmin."
      Syed B.A., Beaumont N.J., Patel A., Naylor C.E., Bayele H.K., Joannou C.L., Rowe P.S.N., Evans R.W., Srai S.K.S.
      Protein Eng. 15:205-214(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Zhao K.W.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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).
      Tissue: Colon.
    7. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-1158 (ISOFORM 1).
      Tissue: Brain.
    8. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.

    Entry informationi

    Entry nameiHEPH_HUMAN
    AccessioniPrimary (citable) accession number: Q9BQS7
    Secondary accession number(s): B1AJX8
    , D3DVT7, E9PHN8, O75180, Q6UW45, Q9C058
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: September 27, 2004
    Last modified: October 1, 2014
    This is version 123 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3