SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9BQS7

- HEPH_HUMAN

UniProt

Q9BQS7 - HEPH_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Hephaestin
Gene
HEPH, KIAA0698, UNQ2562/PRO6242
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

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 2 By similarity
Metal bindingi128 – 1281Copper 2; type 3 By similarity
Metal bindingi186 – 1861Copper 2; type 3 By similarity
Metal bindingi188 – 1881Copper 3; type 3 By similarity
Metal bindingi304 – 3041Copper 4; type 1 By similarity
Metal bindingi347 – 3471Copper 4; type 1 By similarity
Metal bindingi352 – 3521Copper 4; type 1 By similarity
Metal bindingi656 – 6561Copper 5; type 1 By similarity
Metal bindingi699 – 6991Copper 5; type 1 By similarity
Metal bindingi704 – 7041Copper 5; type 1 By similarity
Metal bindingi709 – 7091Copper 5; type 1 By similarity
Metal bindingi1000 – 10001Copper 6; type 1 By similarity
Metal bindingi1003 – 10031Copper 1; type 2 By similarity
Metal bindingi1005 – 10051Copper 3; type 3 By similarity
Metal bindingi1045 – 10451Copper 3; type 3 By similarity
Metal bindingi1046 – 10461Copper 6; type 1 By similarity
Metal bindingi1047 – 10471Copper 2; type 3 By similarity
Metal bindingi1051 – 10511Copper 6; type 1 By similarity
Metal bindingi1056 – 10561Copper 6; type 1 By 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 11101087Extracellular Reviewed prediction
Add
BLAST
Transmembranei1111 – 113121Helical; Reviewed prediction
Add
BLAST
Topological domaini1132 – 115827Cytoplasmic Reviewed prediction
Add
BLAST

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
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29241.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed prediction
Add
BLAST
Chaini24 – 11581135Hephaestin
PRO_0000002915Add
BLAST

Amino acid modifications

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

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.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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.

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.
VSP_047332Add
BLAST
Alternative sequencei1 – 11M → MTQTLPYHLSLLNVLFPGPC SRHFKFRRGKCAQPAWRKVS APSQDLLITKVMWAM in isoform 3.
VSP_047331
Alternative sequencei1082 – 10821Missing in isoform 2.
VSP_011627

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 562DI → QR in BAA31673. 1 Publication
Sequence conflicti222 – 2221V → T in CAC35365. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 122 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

Similar proteinsi