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Q658P3 (STEA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Metalloreductase STEAP3

EC=1.16.1.-
Alternative name(s):
Dudulin-2
Six-transmembrane epithelial antigen of prostate 3
Tumor suppressor-activated pathway protein 6
Short name=hTSAP6
pHyde
Short name=hpHyde
Gene names
Name:STEAP3
Synonyms:TSAP6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endosomal ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Participates in erythroid iron homeostasis by reducing Fe3+ to Fe2+. Can also reduce of Cu2+ to Cu1+, suggesting that it participates in copper homeostasis. Uses NADP+ as acceptor. May play a role downstream of p53/TP53 to interface apoptosis and cell cycle progression. Indirectly involved in exosome secretion by facilitating the secretion of proteins such as TCTP. Ref.11 Ref.12 Ref.15

Cofactor

FAD By similarity. Ref.18

NADP. Ref.18

Subunit structure

Homodimer. Interacts with BNIP3L, MYT1, RHBDL4/RHBDD1 and TCTP. Ref.1 Ref.12 Ref.17 Ref.18

Subcellular location

Endosome membrane; Multi-pass membrane protein By similarity. Note: Localizes to vesicular-like structures at the plasma membrane and around the nucleus.

Tissue specificity

Expressed in adult bone marrow, placenta, liver, skeletal muscle and pancreas. Down-regulated in hepatocellular carcinoma. Ref.1 Ref.13 Ref.14

Induction

By p53/TP53. Ref.1

Post-translational modification

Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced cleavage occurs at multiple sites in a glycosylation-independent manner. Ref.17

Glycosylated. Ref.17

Involvement in disease

Anemia, hypochromic microcytic, with iron overload 2 (AHMIO2) [MIM:615234]: A hematologic disease characterized by abnormal hemoglobin content in the erythrocytes which are reduced in size, severe anemia, erythropoietic hyperplasia of bone marrow, massive hepatic iron deposition, and hepatosplenomegaly.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Sequence similarities

Belongs to the STEAP family.

Contains 1 ferric oxidoreductase domain.

Caution

Was initially thought to have tumor suppressor function in prostate cancer. However, it was shown that it is probably not the case (Ref.11).

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
Ion transport
Iron transport
Transport
   Cellular componentEndosome
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   LigandCopper
FAD
Flavoprotein
Iron
Metal-binding
NADP
   Molecular functionOxidoreductase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cellular iron ion homeostasis

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

protein secretion

Inferred from mutant phenotype Ref.17. Source: UniProtKB

transferrin transport

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentendosome membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

multivesicular body

Inferred from direct assay Ref.12. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionferric-chelate reductase activity

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.17. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q658P3-1)

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: Q658P3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSHQPAVATKM
Isoform 3 (identifier: Q658P3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     351-351: Missing.
Isoform 4 (identifier: Q658P3-4)

Also known as: pHyde II;

The sequence of this isoform differs from the canonical sequence as follows:
     351-351: Missing.
     396-488: SSLGFVALVL...HALAEKTSHV → CVATSSAGNT...GHQEDLSWTR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Metalloreductase STEAP3
PRO_0000285171

Regions

Topological domain1 – 207207Cytoplasmic Potential
Transmembrane208 – 22821Helical; Potential
Topological domain229 – 25830Vesicular Potential
Transmembrane259 – 27921Helical; Potential
Topological domain280 – 30425Cytoplasmic Potential
Transmembrane305 – 32521Helical; Potential
Topological domain326 – 35833Vesicular Potential
Transmembrane359 – 37921Helical; Potential
Topological domain380 – 39011Cytoplasmic Potential
Transmembrane391 – 41121Helical; Potential
Topological domain412 – 43322Vesicular Potential
Transmembrane434 – 45421Helical; Potential
Topological domain455 – 48834Cytoplasmic Potential
Domain259 – 407149Ferric oxidoreductase

Sites

Metal binding3161Iron (heme axial ligand) Probable
Metal binding4091Iron (heme axial ligand) Probable
Binding site361NADP
Binding site381NADP; via amide nitrogen
Binding site391NADP; via amide nitrogen
Binding site581NADP
Binding site591NADP
Binding site911NADP; via carbonyl oxygen
Binding site1161NADP; via amide nitrogen
Binding site1511NADP; via amide nitrogen
Site325 – 3262Cleavage; by RHBDL4/RHBDD1 Probable

Amino acid modifications

Modified residue171Phosphoserine By similarity
Modified residue201Phosphoserine By similarity
Glycosylation2561N-linked (GlcNAc...) Probable
Glycosylation3441N-linked (GlcNAc...) Probable

Natural variations

Alternative sequence11M → MSHQPAVATKM in isoform 2.
VSP_024829
Alternative sequence3511Missing in isoform 3 and isoform 4.
VSP_024830
Alternative sequence396 – 48893SSLGF…KTSHV → CVATSSAGNTGSGTRRPESQ SQDPHLPAPHHQTSFLGPRS FCCSLVPVSTPYGHQEDLSW TR in isoform 4.
VSP_024831
Natural variant1841A → T.
Corresponds to variant rs17013371 [ dbSNP | Ensembl ].
VAR_031975

Experimental info

Mutagenesis2561N → I: Inhibits glycosylation and does not inhibit RHBDL4/RHBDD1-induced cleavage; when associated with A-344. Ref.17
Mutagenesis3251L → F: Strongly inhibits RHBDL4/RHBDD1-induced cleavage. Ref.17
Mutagenesis3441N → I: Inhibits glycosylation and does not inhibit RHBDL4/RHBDD1-induced cleavage; when associated with A-256. Ref.17
Sequence conflict321G → S in AAL78206. Ref.3
Sequence conflict321G → S in AAM08128. Ref.3
Sequence conflict321G → S in AAM45136. Ref.6
Sequence conflict681F → Y in AAK50538. Ref.4
Sequence conflict681F → Y in BAA91839. Ref.7
Sequence conflict1631R → G in AAL78206. Ref.3
Sequence conflict1631R → G in AAM08128. Ref.3
Sequence conflict4781D → G in CAD97986. Ref.8

Secondary structure

..................................... 488
Helix Strand Turn

Details...

Sequences

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

Last modified May 1, 2007. Version 2.
Checksum: C89EB0D0430F9BFB

FASTA48854,601
        10         20         30         40         50         60 
MPEEMDKPLI SLHLVDSDSS LAKVPDEAPK VGILGSGDFA RSLATRLVGS GFKVVVGSRN 

        70         80         90        100        110        120 
PKRTARLFPS AAQVTFQEEA VSSPEVIFVA VFREHYSSLC SLSDQLAGKI LVDVSNPTEQ 

       130        140        150        160        170        180 
EHLQHRESNA EYLASLFPTC TVVKAFNVIS AWTLQAGPRD GNRQVPICGD QPEAKRAVSE 

       190        200        210        220        230        240 
MALAMGFMPV DMGSLASAWE VEAMPLRLLP AWKVPTLLAL GLFVCFYAYN FVRDVLQPYV 

       250        260        270        280        290        300 
QESQNKFFKL PVSVVNTTLP CVAYVLLSLV YLPGVLAAAL QLRRGTKYQR FPDWLDHWLQ 

       310        320        330        340        350        360 
HRKQIGLLSF FCAALHALYS FCLPLRRAHR YDLVNLAVKQ VLANKSHLWV EEEVWRMEIY 

       370        380        390        400        410        420 
LSLGVLALGT LSLLAVTSLP SIANSLNWRE FSFVQSSLGF VALVLSTLHT LTYGWTRAFE 

       430        440        450        460        470        480 
ESRYKFYLPP TFTLTLLVPC VVILAKALFL LPCISRRLAR IRRGWEREST IKFTLPTDHA 


LAEKTSHV 

« Hide

Isoform 2 [UniParc].

Checksum: 69DD201AA00C2D6B
Show »

FASTA49855,652
Isoform 3 [UniParc].

Checksum: 4A279EE7C8964412
Show »

FASTA48754,472
Isoform 4 (pHyde II) [UniParc].

Checksum: 2ECEEB9C1515A9B7
Show »

FASTA45650,499

References

« Hide 'large scale' references
[1]"The p53-inducible TSAP6 gene product regulates apoptosis and the cell cycle and interacts with Nix and the Myt1 kinase."
Passer B.J., Nancy-Portebois V., Amzallag N., Prieur S., Cans C., Roborel de Climens A., Fiucci G., Bouvard V., Tuynder M., Susini L., Morchoisne S., Crible V., Lespagnol A., Dausset J., Oren M., Amson R., Telerman A.
Proc. Natl. Acad. Sci. U.S.A. 100:2284-2289(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH BNIP3L AND MYT1.
[2]"Molecular cloning and characterization of STAMP2, an androgen-regulated six transmembrane protein that is overexpressed in prostate cancer."
Korkmaz C.G., Korkmaz K.S., Kurys P., Elbi C., Wang L., Klokk T.I., Hammarstrom C., Troen G., Svindland A., Hager G.L., Saatcioglu F.
Oncogene 24:4934-4945(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Growth inhibition of prostate cancer by an adenovirus expressing a novel tumor suppressor gene, pHyde."
Steiner M.S., Zhang X., Wang Y., Lu Y.
Cancer Res. 60:4419-4425(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
[4]"Dudulin 2, a new tumor antigen expressed in various human tumors."
Serru V., Manivet P., Lenoir C., Eschwege P., Lamblin D., Vaubourdolle M., Kellermann O., Loric S.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"Characterization of a novel apoptosis-inducing gene, hpHyde, that inhibits prostate cancer cell growth."
Lu Y., Beheshti B., Squire J.A., Yang X.J.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Placenta.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Colon endothelium and Endometrial adenocarcinoma.
[8]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]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].
[10]"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: Kidney.
[11]"Human pHyde is not a classical tumor suppressor gene in prostate cancer."
Porkka K.P., Nupponen N.N., Tammela T.L., Vessella R.L., Visakorpi T.
Int. J. Cancer 106:729-735(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LACK OF TUMOR SUPPRESSOR FUNCTION.
[12]"TSAP6 facilitates the secretion of translationally controlled tumor protein/histamine-releasing factor via a nonclassical pathway."
Amzallag N., Passer B.J., Allanic D., Segura E., Thery C., Goud B., Amson R., Telerman A.
J. Biol. Chem. 279:46104-46112(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TCTP.
[13]"Global gene repression in hepatocellular carcinoma and fetal liver, and suppression of dudulin-2 mRNA as a possible marker for the cirrhosis-to-tumor transition."
Coulouarn C., Derambure C., Lefebvre G., Daveau R., Hiron M., Scotte M., Francois A., Daveau M., Salier J.-P.
J. Hepatol. 42:860-869(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[14]"Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells."
Ohgami R.S., Campagna D.R., Greer E.L., Antiochos B., McDonald A., Chen J., Sharp J.J., Fujiwara Y., Barker J.E., Fleming M.D.
Nat. Genet. 37:1264-1269(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[15]"The regulation of exosome secretion: a novel function of the p53 protein."
Yu X., Harris S.L., Levine A.J.
Cancer Res. 66:4795-4801(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"A novel type of congenital hypochromic anemia associated with a nonsense mutation in the STEAP3/TSAP6 gene."
Grandchamp B., Hetet G., Kannengiesser C., Oudin C., Beaumont C., Rodrigues-Ferreira S., Amson R., Telerman A., Nielsen P., Kohne E., Balser C., Heimpel H.
Blood 118:6660-6666(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN AHMIO2.
[17]"Exosome-related multi-pass transmembrane protein TSAP6 is a target of rhomboid protease RHBDD1-induced proteolysis."
Wan C., Fu J., Wang Y., Miao S., Song W., Wang L.
PLoS ONE 7:E37452-E37452(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY RHBDD1, INTERACTION WITH RHBDD1, GLYCOSYLATION AT ASN-256 AND ASN-344, MUTAGENESIS OF ASN-256; LEU-325 AND ASN-344.
[18]"Structure of the membrane proximal oxidoreductase domain of human Steap3, the dominant ferrireductase of the erythroid transferrin cycle."
Sendamarai A.K., Ohgami R.S., Fleming M.D., Lawrence C.M.
Proc. Natl. Acad. Sci. U.S.A. 105:7410-7415(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-215 ALONE AND IN COMPLEX WITH NADPH, COFACTOR, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY214461 mRNA. Translation: AAO38238.1.
AF423424 mRNA. Translation: AAQ04065.1.
AF238864 mRNA. Translation: AAL78206.1.
AF262322 mRNA. Translation: AAM08128.1.
AY029585 mRNA. Translation: AAK50538.1.
AY082673 mRNA. Translation: AAM45136.1.
AK001691 mRNA. Translation: BAA91839.1.
AK291608 mRNA. Translation: BAF84297.1.
AL833624 mRNA. Translation: CAH56204.1.
BX538047 mRNA. Translation: CAD97986.1.
AC016673 Genomic DNA. Translation: AAX88963.1.
AC016736 Genomic DNA. Translation: AAY14872.1.
CH471103 Genomic DNA. Translation: EAW95209.1.
BC042150 mRNA. Translation: AAH42150.1.
BC095421 mRNA. Translation: AAH95421.2.
CCDSCCDS2125.1. [Q658P3-1]
CCDS42738.1. [Q658P3-2]
RefSeqNP_001008410.1. NM_001008410.1. [Q658P3-1]
NP_060704.2. NM_018234.2. [Q658P3-1]
NP_878919.2. NM_182915.2. [Q658P3-2]
XP_006712676.1. XM_006712613.1. [Q658P3-1]
XP_006712677.1. XM_006712614.1. [Q658P3-1]
XP_006712678.1. XM_006712615.1. [Q658P3-1]
UniGeneHs.647822.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VNSX-ray2.00A/B1-215[»]
2VQ3X-ray2.00A/B1-215[»]
ProteinModelPortalQ658P3.
SMRQ658P3. Positions 29-209.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120533. 5 interactions.
IntActQ658P3. 2 interactions.

Protein family/group databases

TCDB9.B.66.1.1. the animal nonclassical protein secretion (nps) family.

PTM databases

PhosphoSiteQ658P3.

Polymorphism databases

DMDM146325737.

Proteomic databases

MaxQBQ658P3.
PaxDbQ658P3.
PRIDEQ658P3.

Protocols and materials databases

DNASU55240.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354888; ENSP00000346961; ENSG00000115107. [Q658P3-1]
ENST00000393106; ENSP00000376818; ENSG00000115107. [Q658P3-1]
ENST00000393107; ENSP00000376819; ENSG00000115107. [Q658P3-1]
ENST00000393108; ENSP00000376820; ENSG00000115107. [Q658P3-1]
ENST00000393110; ENSP00000376822; ENSG00000115107. [Q658P3-2]
ENST00000425223; ENSP00000396214; ENSG00000115107. [Q658P3-1]
GeneID55240.
KEGGhsa:55240.
UCSCuc002tlp.3. human. [Q658P3-1]
uc002tlq.3. human. [Q658P3-2]

Organism-specific databases

CTD55240.
GeneCardsGC02P119981.
HGNCHGNC:24592. STEAP3.
HPAHPA050510.
MIM609671. gene.
615234. phenotype.
neXtProtNX_Q658P3.
Orphanet300298. Severe congenital hypochromic anemia with ringed sideroblasts.
PharmGKBPA142670863.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2085.
HOVERGENHBG054379.
InParanoidQ658P3.
KOK10142.
OMAGWKVPAL.
OrthoDBEOG7Z0JWH.
PhylomeDBQ658P3.
TreeFamTF332031.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ658P3.
BgeeQ658P3.
GenevestigatorQ658P3.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR013130. Fe3_Rdtase_TM_dom.
IPR016040. NAD(P)-bd_dom.
IPR028939. ProC_N.
[Graphical view]
PfamPF03807. F420_oxidored. 1 hit.
PF01794. Ferric_reduct. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTEAP3. human.
EvolutionaryTraceQ658P3.
GeneWikiSTEAP3.
GenomeRNAi55240.
NextBio59270.
PROQ658P3.
SOURCESearch...

Entry information

Entry nameSTEA3_HUMAN
AccessionPrimary (citable) accession number: Q658P3
Secondary accession number(s): A8K6E3 expand/collapse secondary AC list , Q4VBR2, Q4ZG36, Q53SQ8, Q7Z389, Q86SF6, Q8NEW6, Q8TDP3, Q8TF03, Q9NVB5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: July 9, 2014
This is version 99 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 2

Human chromosome 2: entries, gene names and cross-references to MIM