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Q92504 (S39A7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SLC39A7
Synonyms:HKE4, RING5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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+. Ref.6 Ref.7 Ref.10

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatuscis-Golgi network membrane Ref.6 Ref.7.

Tissue specificity

Widely expressed. Ref.6 Ref.7

Induction

Down-regulated by Zn(+2). Ref.7

Post-translational modification

Rapidly phosphorylated by CK2 following Zn2+ treatment. This phosphorylation is required for efficient cytosolic Zn2+ release. Ref.10

Sequence similarities

Belongs to the ZIP transporter (TC 2.A.5) family. KE4/Catsup subfamily. [View classification]

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CSNK2A1P684004EBI-1051105,EBI-347804

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 469469Zinc transporter SLC39A7
PRO_0000213688

Regions

Transmembrane10 – 3021Helical; Potential
Transmembrane138 – 15821Helical; Potential
Transmembrane169 – 18921Helical; Potential
Transmembrane214 – 23421Helical; Potential
Transmembrane381 – 40121Helical; Potential
Transmembrane417 – 43620Helical; Potential
Compositional bias30 – 11485His-rich
Compositional bias238 – 26326His-rich

Amino acid modifications

Modified residue2751Phosphoserine; by CK2 Ref.9 Ref.10
Modified residue2761Phosphoserine; by CK2 Ref.9 Ref.10
Cross-link310Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Natural variant871D → N.
Corresponds to variant rs34211188 [ dbSNP | Ensembl ].
VAR_050034
Natural variant1241G → R.
Corresponds to variant rs35690712 [ dbSNP | Ensembl ].
VAR_050035
Natural variant2801E → G. Ref.1 Ref.2
Corresponds to variant rs1048778 [ dbSNP | Ensembl ].
VAR_050036

Experimental info

Mutagenesis2751S → A: Loss of phosphorylation in response to Zn(2+) treatment and of cytosolic Zn(2+) release; when associated with A-276. Ref.10
Mutagenesis2761S → A: Loss of phosphorylation in response to Zn(2+) treatment and of cytosolic Zn(2+) release; when associated with A-275. Ref.10
Sequence conflict71A → G in BAA11528. Ref.1
Sequence conflict71A → G in AAD12305. Ref.2
Sequence conflict3761S → T in BAA11528. Ref.1
Sequence conflict3761S → T in AAD12305. Ref.2
Sequence conflict397 – 46973CALLT…IAHLE → VPFSLKEEQWTVKLQVVQVL AGSCHLLQVALST in BAA11528. Ref.1
Sequence conflict397 – 46973CALLT…IAHLE → VPFSLKEEQWTVKLQVVQVL AGSCHLLQVALST in AAD12305. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q92504 [UniParc].

Last modified January 24, 2001. Version 2.
Checksum: 6504A1EF5AA6A5B9

FASTA46950,118
        10         20         30         40         50         60 
MARGLGAPHW VAVGLLTWAT LGLLVAGLGG HDDLHDDLQE DFHGHSHRHS HEDFHHGHSH 

        70         80         90        100        110        120 
AHGHGHTHES IWHGHTHDHD HGHSHEDLHH GHSHGYSHES LYHRGHGHDH EHSHGGYGES 

       130        140        150        160        170        180 
GAPGIKQDLD AVTLWAYALG ATVLISAAPF FVLFLIPVES NSPRHRSLLQ ILLSFASGGL 

       190        200        210        220        230        240 
LGDAFLHLIP HALEPHSHHT LEQPGHGHSH SGQGPILSVG LWVLSGIVAF LVVEKFVRHV 

       250        260        270        280        290        300 
KGGHGHSHGH GHAHSHTRGS HGHGRQERST KEKQSSEEEE KETRGVQKRR GGSTVPKDGP 

       310        320        330        340        350        360 
VRPQNAEEEK RGLDLRVSGY LNLAADLAHN FTDGLAIGAS FRGGRGLGIL TTMTVLLHEV 

       370        380        390        400        410        420 
PHEVGDFAIL VQSGCSKKQA MRLQLLTAVG ALAGTACALL TEGGAVGSEI AGGAGPGWVL 

       430        440        450        460 
PFTAGGFIYV ATVSVLPELL REASPLQSLL EVLGLLGGVI MMVLIAHLE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS43453.1.
RefSeqNP_001070984.1. NM_001077516.1.
NP_001275706.1. NM_001288777.1.
NP_008910.2. NM_006979.2.
UniGeneHs.631995.

3D structure databases

ProteinModelPortalQ92504.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113652. 10 interactions.
IntActQ92504. 5 interactions.
STRING9606.ENSP00000391735.

Protein family/group databases

TCDB2.A.5.4.3. the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.

PTM databases

PhosphoSiteQ92504.

Polymorphism databases

DMDM12643344.

Proteomic databases

MaxQBQ92504.
PaxDbQ92504.
PRIDEQ92504.

Protocols and materials databases

DNASU7922.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374675; 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.
GeneID7922.
KEGGhsa:7922.
UCSCuc003odf.3. human.

Organism-specific databases

CTD7922.
GeneCardsGC06P033168.
GC06Pj33090.
GC06Pk33146.
GC06Pl33322.
GC06Pm33338.
GC06Pn33097.
HGNCHGNC:4927. SLC39A7.
HPAHPA053999.
MIM601416. gene.
neXtProtNX_Q92504.
PharmGKBPA29305.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0428.
HOGENOMHOG000185308.
HOVERGENHBG001037.
InParanoidQ92504.
KOK14713.
OMAFYISSVP.
PhylomeDBQ92504.
TreeFamTF318470.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ92504.
BgeeQ92504.
CleanExHS_SLC39A7.
GenevestigatorQ92504.

Family and domain databases

InterProIPR003689. ZIP.
[Graphical view]
PfamPF02535. Zip. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLC39A7. human.
GeneWikiSLC39A7.
GenomeRNAi7922.
NextBio30416.
PROQ92504.
SOURCESearch...

Entry information

Entry nameS39A7_HUMAN
AccessionPrimary (citable) accession number: Q92504
Secondary accession number(s): B0UXF6, Q5STP8, Q9UIQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 24, 2001
Last modified: July 9, 2014
This is version 125 of the entry and version 2 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 6

Human chromosome 6: entries, gene names and cross-references to MIM