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Protein
Submitted name:

Copper-transporting ATPase 2

Gene

ATP7B

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cation-transporting ATPase activity Source: InterPro
  3. copper ion binding Source: InterPro

GO - Biological processi

  1. metal ion transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotation

Keywords - Ligandi

ATP-bindingUniRule annotation, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Submitted name:
Copper-transporting ATPase 2Imported
Gene namesi
Name:ATP7BImported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:870. ATP7B.

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Expressioni

Gene expression databases

BgeeiF5H562.
ExpressionAtlasiF5H562. baseline and differential.

Structurei

3D structure databases

ProteinModelPortaliF5H562.
SMRiF5H562. Positions 58-949.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. [View classification]UniRule annotation

Keywords - Domaini

TransmembraneUniRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000063773.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
IPR006122. HMA_Cu_ion-bd.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 4 hits.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SUPFAMiSSF55008. SSF55008. 4 hits.
SSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
TIGR00003. TIGR00003. 4 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 4 hits.
PS50846. HMA_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

F5H562-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEQERQITA REGASRKILS KLSLPTRAWE PAMKKSFAFD NVGYEGGLDG
60 70 80 90 100
LGPSSQVATS TVRILGMTCQ SCVKSIEDRI SNLKGIISMK VSLEQGSATV
110 120 130 140 150
KYVPSVVCLQ QVCHQIGDMG FEASIAEGKA ASWPSRSLPA QEAVVKLRVE
160 170 180 190 200
GMTCQSCVSS IEGKVRKLQG VVRVKVSLSN QEAVITYQPY LIQPEDLRDH
210 220 230 240 250
VNDMGFEAAI KSKVAPLSLG PIDIERLQST NPKRPLSSAN QNFNNSETLG
260 270 280 290 300
HQGSHVVTLQ LRIDGMHCKS CVLNIEENIG QLLGVQSIQV SLENKTAQVK
310 320 330 340 350
YDPSCTSPVA LQRAIEALPP GNFKVSLPDG AEGSGTDHRS SSSHSPGSPP
360 370 380 390 400
RNQVQGTCST TLIAIAGMTC ASCVHSIEGM ISQLEGVQQI SVSLAEGTAT
410 420 430 440 450
VLYNPSVISP EELRAAIEDM GFEASVVSGE AMPVTKKPGS TVIAGSINAH
460 470 480 490 500
GSVLIKATHV GNDTTLAQIV KLVEEAQMSK APIQQLADRF SGYFVPFIII
510 520 530 540 550
MSTLTLVVWI VIGFIDFGVV QRYFPNPNKH ISQTEVIIRF AFQTSITVLC
560 570 580 590 600
IACPCSLGLA TPTAVMVGTG VAAQNGILIK GGKPLEMAHK IKTVMFDKTG
610 620 630 640 650
TITHGVPRVM RVLLLGDVAT LPLRKVLAVV GTAEASSEHP LGVAVTKYCK
660 670 680 690 700
EELGTETLGY CTDFQAVPGC GIGCKVSNVE GILAHSERPL SAPASHLNEA
710 720 730 740 750
GSLPAEKDAV PQTFSVLIGN REWLRRNGLT ISSDVSDAMT DHEMKGQTAI
760 770 780 790 800
LVAIDGVLCG MIAIADAVKQ EAALAVHTLQ SMGVDVVLIT GDNRKTARAI
810 820 830 840 850
ATQVGINKVF AEVLPSHKVA KVQELQNKGK KVAMVGDGVN DSPALAQADM
860 870 880 890 900
GVAIGTGTDV AIEAADVVLI RNDLLDVVAS IHLSKRTVRR IRINLVLALI
910 920 930 940 950
YNLVGIPIAA GVFMPIGIVL QPWMGSAAMA ASSVSVVLSS LQLKCYKKPD
960 970 980 990 1000
LERYEAQAHG HMKPLTASQV SVHIGMDDRW RDSPRATPWD QVSYVSQVSL
1010 1020 1030
SSLTSDKPSR HSAAADDDGD KWSLLLNGRD EEQYI
Length:1,035
Mass (Da):110,319
Last modified:June 28, 2011 - v1
Checksum:i4DAD27FA0ECB37E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL138821 Genomic DNA. No translation available.
AL139082 Genomic DNA. No translation available.
AL162377 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000400370; ENSP00000383221; ENSG00000123191.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL138821 Genomic DNA. No translation available.
AL139082 Genomic DNA. No translation available.
AL162377 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortaliF5H562.
SMRiF5H562. Positions 58-949.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000400370; ENSP00000383221; ENSG00000123191.

Organism-specific databases

HGNCiHGNC:870. ATP7B.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00530000063773.

Miscellaneous databases

NextBioi35508930.

Gene expression databases

BgeeiF5H562.
ExpressionAtlasiF5H562. baseline and differential.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
IPR006122. HMA_Cu_ion-bd.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 4 hits.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SUPFAMiSSF55008. SSF55008. 4 hits.
SSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
TIGR00003. TIGR00003. 4 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 4 hits.
PS50846. HMA_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiF5H562_HUMAN
AccessioniPrimary (citable) accession number: F5H562
Entry historyi
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: March 4, 2015
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationMaxQB annotation, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.