STEA4_HUMAN - dbPTM
STEA4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STEA4_HUMAN
UniProt AC Q687X5
Protein Name Metalloreductase STEAP4
Gene Name STEAP4
Organism Homo sapiens (Human).
Sequence Length 459
Subcellular Localization Cell membrane
Multi-pass membrane protein . Golgi apparatus membrane
Multi-pass membrane protein . Early endosome membrane
Multi-pass membrane protein .
Protein Description Metalloreductase that has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+) (By similarity). Uses NADP(+) as acceptor (By similarity). Plays a role in systemic metabolic homeostasis, integrating inflammatory and metabolic responses (By similarity). Associated with obesity and insulin-resistance. [PubMed: 18430367]
Protein Sequence MEKTCIDALPLTMNSSEKQETVCIFGTGDFGRSLGLKMLQCGYSVVFGSRNPQKTTLLPSGAEVLSYSEAAKKSGIIIIAIHREHYDFLTELTEVLNGKILVDISNNLKINQYPESNAEYLAHLVPGAHVVKAFNTISAWALQSGALDASRQVFVCGNDSKAKQRVMDIVRNLGLTPMDQGSLMAAKEIEKYPLQLFPMWRFPFYLSAVLCVFLFFYCVIRDVIYPYVYEKKDNTFRMAISIPNRIFPITALTLLALVYLPGVIAAILQLYRGTKYRRFPDWLDHWMLCRKQLGLVALGFAFLHVLYTLVIPIRYYVRWRLGNLTVTQAILKKENPFSTSSAWLSDSYVALGILGFFLFVLLGITSLPSVSNAVNWREFRFVQSKLGYLTLILCTAHTLVYGGKRFLSPSNLRWYLPAAYVLGLIIPCTVLVIKFVLIMPCVDNTLTRIRQGWERNSKH
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
3Ubiquitination-----MEKTCIDALP
-----CCCCHHHEEC
47.6129967540
18UbiquitinationLTMNSSEKQETVCIF
CCCCCCCCCEEEEEE
56.2221963094
33PhosphorylationGTGDFGRSLGLKMLQ
ECCHHHHHHCHHHHC
27.45-
43PhosphorylationLKMLQCGYSVVFGSR
HHHHCCCCEEEECCC
13.1028111955
44PhosphorylationKMLQCGYSVVFGSRN
HHHCCCCEEEECCCC
9.3328111955
49PhosphorylationGYSVVFGSRNPQKTT
CCEEEECCCCCCCCE
19.8828111955
54UbiquitinationFGSRNPQKTTLLPSG
ECCCCCCCCEECCCC
44.7429967540
60PhosphorylationQKTTLLPSGAEVLSY
CCCEECCCCCCEECH
51.0827251275
722-HydroxyisobutyrylationLSYSEAAKKSGIIII
ECHHHHHHHCCEEEE
55.29-
72UbiquitinationLSYSEAAKKSGIIII
ECHHHHHHHCCEEEE
55.2929901268
109UbiquitinationVDISNNLKINQYPES
EECCCCCCCCCCCCC
41.5629967540
161UbiquitinationFVCGNDSKAKQRVMD
EEECCCHHHHHHHHH
63.5721963094
176PhosphorylationIVRNLGLTPMDQGSL
HHHHCCCCCCCHHCH
18.12-
182PhosphorylationLTPMDQGSLMAAKEI
CCCCCHHCHHCHHHH
14.89-
187UbiquitinationQGSLMAAKEIEKYPL
HHCHHCHHHHHHCCC
50.0821963094
187AcetylationQGSLMAAKEIEKYPL
HHCHHCHHHHHHCCC
50.0827452117
225PhosphorylationCVIRDVIYPYVYEKK
HHHHHHHHHHHHCCC
6.59-
323N-linked_GlycosylationYVRWRLGNLTVTQAI
HHHHHHCCEEHHHHH
36.8130337524
332UbiquitinationTVTQAILKKENPFST
EHHHHHHHCCCCCCC
52.5121963094
333UbiquitinationVTQAILKKENPFSTS
HHHHHHHCCCCCCCC
60.3122817900
408PhosphorylationYGGKRFLSPSNLRWY
HCCCCCCCHHHHCCH
24.46-
410PhosphorylationGKRFLSPSNLRWYLP
CCCCCCHHHHCCHHH
45.1622985185

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of STEA4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STEA4_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of STEA4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of STEA4_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STEA4_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323, AND MASSSPECTROMETRY.

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