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Q92504

- S39A7_HUMAN

UniProt

Q92504 - S39A7_HUMAN

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Protein

Zinc transporter SLC39A7

Gene

SLC39A7

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

Functioni

Zinc transporter, that transports Zn2+ from the endoplasmic reticulum/Golgi apparatus to the cytosol. Transport is stimulated by growth factors, such as EGF, and Ca2+, as well as by exogenous Zn2+.3 Publications

GO - Molecular functioni

  1. metal ion transmembrane transporter activity Source: InterPro

GO - Biological processi

  1. transmembrane transport Source: Reactome
  2. zinc ion transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Ion transport, Transport, Zinc transport

Keywords - Ligandi

Zinc

Enzyme and pathway databases

ReactomeiREACT_20603. Zinc influx into cells by the SLC39 gene family.

Protein family/group databases

TCDBi2.A.5.4.3. the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc transporter SLC39A7
Alternative name(s):
Histidine-rich membrane protein Ke4
Really interesting new gene 5 protein
Solute carrier family 39 member 7
Zrt-, Irt-like protein 7
Short name:
ZIP7
Gene namesi
Name:SLC39A7
Synonyms:HKE4, RING5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:4927. SLC39A7.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. Golgi apparatus Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi275 – 2751S → A: Loss of phosphorylation in response to Zn(2+) treatment and of cytosolic Zn(2+) release; when associated with A-276. 1 Publication
Mutagenesisi276 – 2761S → A: Loss of phosphorylation in response to Zn(2+) treatment and of cytosolic Zn(2+) release; when associated with A-275. 1 Publication

Organism-specific databases

PharmGKBiPA29305.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469Zinc transporter SLC39A7PRO_0000213688Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei275 – 2751Phosphoserine; by CK22 Publications
Modified residuei276 – 2761Phosphoserine; by CK22 Publications
Cross-linki310 – 310Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Rapidly phosphorylated by CK2 following Zn2+ treatment. This phosphorylation is required for efficient cytosolic Zn2+ release.2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ92504.
PaxDbiQ92504.
PRIDEiQ92504.

PTM databases

PhosphoSiteiQ92504.

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Inductioni

Down-regulated by Zn(+2).1 Publication

Gene expression databases

BgeeiQ92504.
CleanExiHS_SLC39A7.
ExpressionAtlasiQ92504. baseline and differential.
GenevestigatoriQ92504.

Organism-specific databases

HPAiHPA053999.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CSNK2A1P684004EBI-1051105,EBI-347804

Protein-protein interaction databases

BioGridi113652. 8 interactions.
IntActiQ92504. 5 interactions.
STRINGi9606.ENSP00000391735.

Structurei

3D structure databases

ProteinModelPortaliQ92504.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei10 – 3021HelicalSequence AnalysisAdd
BLAST
Transmembranei138 – 15821HelicalSequence AnalysisAdd
BLAST
Transmembranei169 – 18921HelicalSequence AnalysisAdd
BLAST
Transmembranei214 – 23421HelicalSequence AnalysisAdd
BLAST
Transmembranei381 – 40121HelicalSequence AnalysisAdd
BLAST
Transmembranei417 – 43620HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi30 – 11485His-richAdd
BLAST
Compositional biasi238 – 26326His-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0428.
GeneTreeiENSGT00760000119115.
HOGENOMiHOG000185308.
HOVERGENiHBG001037.
InParanoidiQ92504.
KOiK14713.
OMAiFYISSVP.
PhylomeDBiQ92504.
TreeFamiTF318470.

Family and domain databases

InterProiIPR003689. ZIP.
[Graphical view]
PfamiPF02535. Zip. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92504-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARGLGAPHW VAVGLLTWAT LGLLVAGLGG HDDLHDDLQE DFHGHSHRHS
60 70 80 90 100
HEDFHHGHSH AHGHGHTHES IWHGHTHDHD HGHSHEDLHH GHSHGYSHES
110 120 130 140 150
LYHRGHGHDH EHSHGGYGES GAPGIKQDLD AVTLWAYALG ATVLISAAPF
160 170 180 190 200
FVLFLIPVES NSPRHRSLLQ ILLSFASGGL LGDAFLHLIP HALEPHSHHT
210 220 230 240 250
LEQPGHGHSH SGQGPILSVG LWVLSGIVAF LVVEKFVRHV KGGHGHSHGH
260 270 280 290 300
GHAHSHTRGS HGHGRQERST KEKQSSEEEE KETRGVQKRR GGSTVPKDGP
310 320 330 340 350
VRPQNAEEEK RGLDLRVSGY LNLAADLAHN FTDGLAIGAS FRGGRGLGIL
360 370 380 390 400
TTMTVLLHEV PHEVGDFAIL VQSGCSKKQA MRLQLLTAVG ALAGTACALL
410 420 430 440 450
TEGGAVGSEI AGGAGPGWVL PFTAGGFIYV ATVSVLPELL REASPLQSLL
460
EVLGLLGGVI MMVLIAHLE
Length:469
Mass (Da):50,118
Last modified:January 24, 2001 - v2
Checksum:i6504A1EF5AA6A5B9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71A → G in BAA11528. (PubMed:8812499)Curated
Sequence conflicti7 – 71A → G in AAD12305. 1 PublicationCurated
Sequence conflicti376 – 3761S → T in BAA11528. (PubMed:8812499)Curated
Sequence conflicti376 – 3761S → T in AAD12305. 1 PublicationCurated
Sequence conflicti397 – 46973CALLT…IAHLE → VPFSLKEEQWTVKLQVVQVL AGSCHLLQVALST in BAA11528. (PubMed:8812499)CuratedAdd
BLAST
Sequence conflicti397 – 46973CALLT…IAHLE → VPFSLKEEQWTVKLQVVQVL AGSCHLLQVALST in AAD12305. 1 PublicationCuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti87 – 871D → N.
Corresponds to variant rs34211188 [ dbSNP | Ensembl ].
VAR_050034
Natural varianti124 – 1241G → R.
Corresponds to variant rs35690712 [ dbSNP | Ensembl ].
VAR_050035
Natural varianti280 – 2801E → G.2 Publications
Corresponds to variant rs1048778 [ dbSNP | Ensembl ].
VAR_050036

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D82060 mRNA. Translation: BAA11528.1.
AF117221 Genomic DNA. Translation: AAD12305.1.
AL031228 Genomic DNA. Translation: CAA20238.1.
AL645940 Genomic DNA. Translation: CAI18067.1.
AL662824 Genomic DNA. Translation: CAI17615.1.
AL844527 Genomic DNA. Translation: CAI41839.1.
CR759786, CR936877 Genomic DNA. Translation: CAQ08249.1.
CR936877, CR759786 Genomic DNA. Translation: CAQ09067.1.
CR759733 Genomic DNA. Translation: CAQ10301.1.
CR354565 Genomic DNA. Translation: CAQ11085.1.
CH471081 Genomic DNA. Translation: EAX03680.1.
BC000645 mRNA. Translation: AAH00645.1.
CCDSiCCDS43453.1.
RefSeqiNP_001070984.1. NM_001077516.1.
NP_001275706.1. NM_001288777.1.
NP_008910.2. NM_006979.2.
UniGeneiHs.631995.

Genome annotation databases

EnsembliENST00000374675; ENSP00000363807; ENSG00000112473.
ENST00000374677; ENSP00000363809; ENSG00000112473.
ENST00000383213; ENSP00000372700; ENSG00000206288.
ENST00000383214; ENSP00000372701; ENSG00000206288.
ENST00000416369; ENSP00000403583; ENSG00000229802.
ENST00000418477; ENSP00000416439; ENSG00000226614.
ENST00000423043; ENSP00000389623; ENSG00000226614.
ENST00000431735; ENSP00000410656; ENSG00000224399.
ENST00000441854; ENSP00000391735; ENSG00000229802.
ENST00000441953; ENSP00000413027; ENSG00000224399.
ENST00000443773; ENSP00000407093; ENSG00000227402.
ENST00000456261; ENSP00000414145; ENSG00000227402.
GeneIDi7922.
KEGGihsa:7922.
UCSCiuc003odf.3. human.

Polymorphism databases

DMDMi12643344.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D82060 mRNA. Translation: BAA11528.1 .
AF117221 Genomic DNA. Translation: AAD12305.1 .
AL031228 Genomic DNA. Translation: CAA20238.1 .
AL645940 Genomic DNA. Translation: CAI18067.1 .
AL662824 Genomic DNA. Translation: CAI17615.1 .
AL844527 Genomic DNA. Translation: CAI41839.1 .
CR759786 , CR936877 Genomic DNA. Translation: CAQ08249.1 .
CR936877 , CR759786 Genomic DNA. Translation: CAQ09067.1 .
CR759733 Genomic DNA. Translation: CAQ10301.1 .
CR354565 Genomic DNA. Translation: CAQ11085.1 .
CH471081 Genomic DNA. Translation: EAX03680.1 .
BC000645 mRNA. Translation: AAH00645.1 .
CCDSi CCDS43453.1.
RefSeqi NP_001070984.1. NM_001077516.1.
NP_001275706.1. NM_001288777.1.
NP_008910.2. NM_006979.2.
UniGenei Hs.631995.

3D structure databases

ProteinModelPortali Q92504.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113652. 8 interactions.
IntActi Q92504. 5 interactions.
STRINGi 9606.ENSP00000391735.

Protein family/group databases

TCDBi 2.A.5.4.3. the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.

PTM databases

PhosphoSitei Q92504.

Polymorphism databases

DMDMi 12643344.

Proteomic databases

MaxQBi Q92504.
PaxDbi Q92504.
PRIDEi Q92504.

Protocols and materials databases

DNASUi 7922.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374675 ; ENSP00000363807 ; ENSG00000112473 .
ENST00000374677 ; ENSP00000363809 ; ENSG00000112473 .
ENST00000383213 ; ENSP00000372700 ; ENSG00000206288 .
ENST00000383214 ; ENSP00000372701 ; ENSG00000206288 .
ENST00000416369 ; ENSP00000403583 ; ENSG00000229802 .
ENST00000418477 ; ENSP00000416439 ; ENSG00000226614 .
ENST00000423043 ; ENSP00000389623 ; ENSG00000226614 .
ENST00000431735 ; ENSP00000410656 ; ENSG00000224399 .
ENST00000441854 ; ENSP00000391735 ; ENSG00000229802 .
ENST00000441953 ; ENSP00000413027 ; ENSG00000224399 .
ENST00000443773 ; ENSP00000407093 ; ENSG00000227402 .
ENST00000456261 ; ENSP00000414145 ; ENSG00000227402 .
GeneIDi 7922.
KEGGi hsa:7922.
UCSCi uc003odf.3. human.

Organism-specific databases

CTDi 7922.
GeneCardsi GC06P033168.
GC06Pj33090.
GC06Pk33146.
GC06Pl33322.
GC06Pm33338.
GC06Pn33097.
HGNCi HGNC:4927. SLC39A7.
HPAi HPA053999.
MIMi 601416. gene.
neXtProti NX_Q92504.
PharmGKBi PA29305.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0428.
GeneTreei ENSGT00760000119115.
HOGENOMi HOG000185308.
HOVERGENi HBG001037.
InParanoidi Q92504.
KOi K14713.
OMAi FYISSVP.
PhylomeDBi Q92504.
TreeFami TF318470.

Enzyme and pathway databases

Reactomei REACT_20603. Zinc influx into cells by the SLC39 gene family.

Miscellaneous databases

ChiTaRSi SLC39A7. human.
GeneWikii SLC39A7.
GenomeRNAii 7922.
NextBioi 30416.
PROi Q92504.
SOURCEi Search...

Gene expression databases

Bgeei Q92504.
CleanExi HS_SLC39A7.
ExpressionAtlasi Q92504. baseline and differential.
Genevestigatori Q92504.

Family and domain databases

InterProi IPR003689. ZIP.
[Graphical view ]
Pfami PF02535. Zip. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of the human homologues of the mouse Ke4 and Ke6 genes at the centromeric end of the human MHC region."
    Ando A., Kikuti Y.Y., Shigenari A., Kawata H., Okamoto N., Shiina T., Chen L., Ikemura T., Abe K., Kimura M., Inoko H.
    Genomics 35:600-602(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-280.
    Tissue: Kidney.
  2. "Molecular cloning and characterization of the human KE4 gene and 5' flanking region."
    Vergara A., Lana I., Corella A., de Miguel C., Migliaccio M., Encio I.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-280.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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].
    Tissue: Skin.
  6. "Structure-function analysis of HKE4, a member of the new LIV-1 subfamily of zinc transporters."
    Taylor K.M., Morgan H.E., Johnson A., Nicholson R.I.
    Biochem. J. 377:131-139(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "The ZIP7 gene (Slc39a7) encodes a zinc transporter involved in zinc homeostasis of the Golgi apparatus."
    Huang L., Kirschke C.P., Zhang Y., Yu Y.Y.
    J. Biol. Chem. 280:15456-15463(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND SER-276, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Protein kinase CK2 triggers cytosolic zinc signaling pathways by phosphorylation of zinc channel ZIP7."
    Taylor K.M., Hiscox S., Nicholson R.I., Hogstrand C., Kille P.
    Sci. Signal. 5:RA11-RA11(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-275 AND SER-276, MUTAGENESIS OF SER-275 AND SER-276.

Entry informationi

Entry nameiS39A7_HUMAN
AccessioniPrimary (citable) accession number: Q92504
Secondary accession number(s): B0UXF6, Q5STP8, Q9UIQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 24, 2001
Last modified: October 29, 2014
This is version 128 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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