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Q9BQS7 (HEPH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hephaestin

EC=1.-.-.-
Gene names
Name:HEPH
Synonyms:KIAA0698
ORF Names:UNQ2562/PRO6242
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1158 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Cofactor

Binds 6 copper ions per monomer By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

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

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 6 plastocyanin-like domains.

Sequence caution

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.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BQS7-1)

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.
Isoform 2 (identifier: Q9BQS7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1082-1082: Missing.
Isoform 3 (identifier: Q9BQS7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTQTLPYHLSLLNVLFPGPCSRHFKFRRGKCAQPAWRKVSAPSQDLLITKVMWAM
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9BQS7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-267: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 11581135Hephaestin
PRO_0000002915

Regions

Topological domain24 – 11101087Extracellular Potential
Transmembrane1111 – 113121Helical; Potential
Topological domain1132 – 115827Cytoplasmic Potential
Domain24 – 206183Plastocyanin-like 1
Domain218 – 366149Plastocyanin-like 2
Domain379 – 560182Plastocyanin-like 3
Domain570 – 718149Plastocyanin-like 4
Domain731 – 903173Plastocyanin-like 5
Domain911 – 1087177Plastocyanin-like 6

Sites

Metal binding1261Copper 1; type 2 By similarity
Metal binding1281Copper 2; type 3 By similarity
Metal binding1861Copper 2; type 3 By similarity
Metal binding1881Copper 3; type 3 By similarity
Metal binding3041Copper 4; type 1 By similarity
Metal binding3471Copper 4; type 1 By similarity
Metal binding3521Copper 4; type 1 By similarity
Metal binding6561Copper 5; type 1 By similarity
Metal binding6991Copper 5; type 1 By similarity
Metal binding7041Copper 5; type 1 By similarity
Metal binding7091Copper 5; type 1 By similarity
Metal binding10001Copper 6; type 1 By similarity
Metal binding10031Copper 1; type 2 By similarity
Metal binding10051Copper 3; type 3 By similarity
Metal binding10451Copper 3; type 3 By similarity
Metal binding10461Copper 6; type 1 By similarity
Metal binding10471Copper 2; type 3 By similarity
Metal binding10511Copper 6; type 1 By similarity
Metal binding10561Copper 6; type 1 By similarity

Amino acid modifications

Glycosylation1641N-linked (GlcNAc...) Potential
Glycosylation2361N-linked (GlcNAc...) Potential
Glycosylation5881N-linked (GlcNAc...) Potential
Glycosylation7141N-linked (GlcNAc...) Potential
Glycosylation7581N-linked (GlcNAc...) Potential
Glycosylation8291N-linked (GlcNAc...) Potential
Glycosylation8731N-linked (GlcNAc...) Potential
Glycosylation9311N-linked (GlcNAc...) Potential
Disulfide bond180 ↔ 206 Potential
Disulfide bond285 ↔ 366 Potential
Disulfide bond534 ↔ 560 Potential
Disulfide bond637 ↔ 718 Potential
Disulfide bond877 ↔ 903 Potential

Natural variations

Alternative sequence1 – 267267Missing in isoform 4.
VSP_047332
Alternative sequence11M → MTQTLPYHLSLLNVLFPGPC SRHFKFRRGKCAQPAWRKVS APSQDLLITKVMWAM in isoform 3.
VSP_047331
Alternative sequence10821Missing in isoform 2.
VSP_011627
Natural variant5951A → T.
Corresponds to variant rs17216603 [ dbSNP | Ensembl ].
VAR_024379

Experimental info

Sequence conflict55 – 562DI → QR in BAA31673. Ref.7
Sequence conflict2221V → T in CAC35365. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 27, 2004. Version 3.
Checksum: CD032199E2E2868D

FASTA1,158130,449
        10         20         30         40         50         60 
MESGHLLWAL LFMQSLWPQL TDGATRVYYL GIRDVQWNYA PKGRNVITNQ PLDSDIVASS 

        70         80         90        100        110        120 
FLKSDKNRIG GTYKKTIYKE YKDDSYTDEV AQPAWLGFLG PVLQAEVGDV ILIHLKNFAT 

       130        140        150        160        170        180 
RPYTIHPHGV FYEKDSEGSL YPDGSSGPLK ADDSVPPGGS HIYNWTIPEG HAPTDADPAC 

       190        200        210        220        230        240 
LTWIYHSHVD APRDIATGLI GPLITCKRGA LDGNSPPQRQ DVDHDFFLLF SVVDENLSWH 

       250        260        270        280        290        300 
LNENIATYCS DPASVDKEDE TFQESNRMHA INGFVFGNLP ELNMCAQKRV AWHLFGMGNE 

       310        320        330        340        350        360 
IDVHTAFFHG QMLTTRGHHT DVANIFPATF VTAEMVPWEP GTWLISCQVN SHFRDGMQAL 

       370        380        390        400        410        420 
YKVKSCSMAP PVDLLTGKVR QYFIEAHEIQ WDYGPMGHDG STGKNLREPG SISDKFFQKS 

       430        440        450        460        470        480 
SSRIGGTYWK VRYEAFQDET FQEKMHLEED RHLGILGPVI RAEVGDTIQV VFYNRASQPF 

       490        500        510        520        530        540 
SMQPHGVFYE KDYEGTVYND GSSYPGLVAK PFEKVTYRWT VPPHAGPTAQ DPACLTWMYF 

       550        560        570        580        590        600 
SAADPIRDTN SGLVGPLLVC RAGALGADGK QKGVDKEFFL LFTVLDENKS WYSNANQAAA 

       610        620        630        640        650        660 
MLDFRLLSED IEGFQDSNRM HAINGFLFSN LPRLDMCKGD TVAWHLLGLG TETDVHGVMF 

       670        680        690        700        710        720 
QGNTVQLQGM RKGAAMLFPH TFVMAIMQPD NLGTFEIYCQ AGSHREAGMR AIYNVSQCPG 

       730        740        750        760        770        780 
HQATPRQRYQ AARIYYIMAE EVEWDYCPDR SWEREWHNQS EKDSYGYIFL SNKDGLLGSR 

       790        800        810        820        830        840 
YKKAVFREYT DGTFRIPRPR TGPEEHLGIL GPLIKGEVGD ILTVVFKNNA SRPYSVHAHG 

       850        860        870        880        890        900 
VLESTTVWPL AAEPGEVVTY QWNIPERSGP GPNDSACVSW IYYSAVDPIK DMYSGLVGPL 

       910        920        930        940        950        960 
AICQKGILEP HGGRSDMDRE FALLFLIFDE NKSWYLEENV ATHGSQDPGS INLQDETFLE 

       970        980        990       1000       1010       1020 
SNKMHAINGK LYANLRGLTM YQGERVAWYM LAMGQDVDLH TIHFHAESFL YRNGENYRAD 

      1030       1040       1050       1060       1070       1080 
VVDLFPGTFE VVEMVASNPG TWLMHCHVTD HVHAGMETLF TVFSRTEHLS PLTVITKETE 

      1090       1100       1110       1120       1130       1140 
KAVPPRDIEE GNVKMLGMQI PIKNVEMLAS VLVAISVTLL LVVLALGGVV WYQHRQRKLR 

      1150 
RNRRSILDDS FKLLSFKQ 

« Hide

Isoform 2 [UniParc].

Checksum: 3DCFE053093BFA7D
Show »

FASTA1,157130,378
Isoform 3 [UniParc].

Checksum: 9C03D79DAE69BA8C
Show »

FASTA1,212136,658
Isoform 4 [UniParc].

Checksum: AB70D0436109C5B2
Show »

FASTA891100,624

References

« Hide 'large scale' references
[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]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Web resources

Wikipedia

Hephaestin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14384.3. [Q9BQS7-3]
CCDS14385.1. [Q9BQS7-4]
RefSeqNP_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.
UniGeneHs.31720.

3D structure databases

ProteinModelPortalQ9BQS7.
SMRQ9BQS7. Positions 28-1065.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115179. 1 interaction.
STRING9606.ENSP00000403834.

PTM databases

PhosphoSiteQ9BQS7.

Polymorphism databases

DMDM52782976.

Proteomic databases

MaxQBQ9BQS7.
PaxDbQ9BQS7.
PRIDEQ9BQS7.

Protocols and materials databases

DNASU9843.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336279; ENSP00000337418; ENSG00000089472. [Q9BQS7-4]
ENST00000343002; ENSP00000343939; ENSG00000089472. [Q9BQS7-1]
ENST00000441993; ENSP00000411687; ENSG00000089472.
ENST00000519389; ENSP00000430620; ENSG00000089472. [Q9BQS7-3]
GeneID9843.
KEGGhsa:9843.
UCSCuc004dwn.3. human. [Q9BQS7-2]
uc004dwo.3. human. [Q9BQS7-1]

Organism-specific databases

CTD9843.
GeneCardsGC0XP065299.
H-InvDBHIX0016844.
HGNCHGNC:4866. HEPH.
HPAHPA005824.
MIM300167. gene.
neXtProtNX_Q9BQS7.
PharmGKBPA29241.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG276067.
HOGENOMHOG000231499.
HOVERGENHBG003674.
InParanoidQ9BQS7.
KOK14735.
OMALIHLKNF.
OrthoDBEOG7V49XN.
PhylomeDBQ9BQS7.
TreeFamTF329807.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ9BQS7.
BgeeQ9BQS7.
CleanExHS_HEPH.
GenevestigatorQ9BQS7.

Family and domain databases

Gene3D2.60.40.420. 6 hits.
InterProIPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
IPR027154. HEPH.
[Graphical view]
PANTHERPTHR10127:SF317. PTHR10127:SF317. 1 hit.
PfamPF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 2 hits.
[Graphical view]
SUPFAMSSF49503. SSF49503. 6 hits.
PROSITEPS00079. MULTICOPPER_OXIDASE1. 3 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi9843.
NextBio37092.
PROQ9BQS7.
SOURCESearch...

Entry information

Entry nameHEPH_HUMAN
AccessionPrimary (citable) accession number: Q9BQS7
Secondary accession number(s): B1AJX8 expand/collapse secondary AC list , D3DVT7, E9PHN8, O75180, Q6UW45, Q9C058
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: July 9, 2014
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM