CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014671
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Metalloreductase STEAP3 
Protein Synonyms/Alias
 Dudulin-2; Six-transmembrane epithelial antigen of prostate 3; Tumor suppressor-activated pathway protein 6; hTSAP6; pHyde; hpHyde 
Gene Name
 STEAP3 
Gene Synonyms/Alias
 TSAP6 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
339DLVNLAVKQVLANKSubiquitination[1]
472WERESTIKFTLPTDHubiquitination[1, 2]
484TDHALAEKTSHV***ubiquitination[2, 3, 4, 5, 6]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572
Functional Description
 Endosomal ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Participates in erythroid iron homeostasis by reducing Fe(3+) to Fe(2+). Can also reduce of Cu(2+) to Cu(1+), 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. 
Sequence Annotation
 DOMAIN 259 407 Ferric oxidoreductase.
 METAL 316 316 Iron (heme axial ligand) (Probable).
 METAL 409 409 Iron (heme axial ligand) (Probable).
 BINDING 36 36 NADP.
 BINDING 38 38 NADP; via amide nitrogen.
 BINDING 39 39 NADP; via amide nitrogen.
 BINDING 58 58 NADP.
 BINDING 59 59 NADP.
 BINDING 91 91 NADP; via carbonyl oxygen.
 BINDING 116 116 NADP; via amide nitrogen.
 BINDING 151 151 NADP; via amide nitrogen.
 MOD_RES 17 17 Phosphoserine (By similarity).
 MOD_RES 20 20 Phosphoserine (By similarity).
 CARBOHYD 256 256 N-linked (GlcNAc...) (Probable).
 CARBOHYD 344 344 N-linked (GlcNAc...) (Probable).  
Keyword
 3D-structure; Alternative splicing; Apoptosis; Cell cycle; Complete proteome; Copper; Endosome; FAD; Flavoprotein; Glycoprotein; Ion transport; Iron; Iron transport; Membrane; Metal-binding; NADP; Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 488 AA 
Protein Sequence
MPEEMDKPLI SLHLVDSDSS LAKVPDEAPK VGILGSGDFA RSLATRLVGS GFKVVVGSRN 60
PKRTARLFPS AAQVTFQEEA VSSPEVIFVA VFREHYSSLC SLSDQLAGKI LVDVSNPTEQ 120
EHLQHRESNA EYLASLFPTC TVVKAFNVIS AWTLQAGPRD GNRQVPICGD QPEAKRAVSE 180
MALAMGFMPV DMGSLASAWE VEAMPLRLLP AWKVPTLLAL GLFVCFYAYN FVRDVLQPYV 240
QESQNKFFKL PVSVVNTTLP CVAYVLLSLV YLPGVLAAAL QLRRGTKYQR FPDWLDHWLQ 300
HRKQIGLLSF FCAALHALYS FCLPLRRAHR YDLVNLAVKQ VLANKSHLWV EEEVWRMEIY 360
LSLGVLALGT LSLLAVTSLP SIANSLNWRE FSFVQSSLGF VALVLSTLHT LTYGWTRAFE 420
ESRYKFYLPP TFTLTLLVPC VVILAKALFL LPCISRRLAR IRRGWEREST IKFTLPTDHA 480
LAEKTSHV 488 
Gene Ontology
 GO:0010008; C:endosome membrane; TAS:Reactome.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005771; C:multivesicular body; IDA:MGI.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0000293; F:ferric-chelate reductase activity; IEA:Compara.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
 GO:0006917; P:induction of apoptosis; IEA:Compara.
 GO:0009306; P:protein secretion; IMP:UniProtKB.
 GO:0033572; P:transferrin transport; TAS:Reactome.
 GO:0055085; P:transmembrane transport; TAS:Reactome. 
Interpro
 IPR013130; Fe3_Rdtase_TM_dom.
 IPR016040; NAD(P)-bd_dom.
 IPR004455; NADP_OxRdtase_F420. 
Pfam
 PF03807; F420_oxidored
 PF01794; Ferric_reduct 
SMART
  
PROSITE
  
PRINTS