STEA3_HUMAN - dbPTM
STEA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STEA3_HUMAN
UniProt AC Q658P3
Protein Name Metalloreductase STEAP3
Gene Name STEAP3
Organism Homo sapiens (Human).
Sequence Length 488
Subcellular Localization Endosome membrane
Multi-pass membrane protein. Localizes to vesicular-like structures at the plasma membrane and around the nucleus.
Protein 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..
Protein Sequence MPEEMDKPLISLHLVDSDSSLAKVPDEAPKVGILGSGDFARSLATRLVGSGFKVVVGSRNPKRTARLFPSAAQVTFQEEAVSSPEVIFVAVFREHYSSLCSLSDQLAGKILVDVSNPTEQEHLQHRESNAEYLASLFPTCTVVKAFNVISAWTLQAGPRDGNRQVPICGDQPEAKRAVSEMALAMGFMPVDMGSLASAWEVEAMPLRLLPAWKVPTLLALGLFVCFYAYNFVRDVLQPYVQESQNKFFKLPVSVVNTTLPCVAYVLLSLVYLPGVLAAALQLRRGTKYQRFPDWLDHWLQHRKQIGLLSFFCAALHALYSFCLPLRRAHRYDLVNLAVKQVLANKSHLWVEEEVWRMEIYLSLGVLALGTLSLLAVTSLPSIANSLNWREFSFVQSSLGFVALVLSTLHTLTYGWTRAFEESRYKFYLPPTFTLTLLVPCVVILAKALFLLPCISRRLARIRRGWERESTIKFTLPTDHALAEKTSHV
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
7Ubiquitination-MPEEMDKPLISLHL
-CCHHHCCCEEEEEE		40.17-
11PhosphorylationEMDKPLISLHLVDSD
HHCCCEEEEEEECCC		19.8828450419
17PhosphorylationISLHLVDSDSSLAKV
EEEEEECCCCCCCCC		31.7325159151
17 (in isoform 2)Ubiquitination-31.73-
19PhosphorylationLHLVDSDSSLAKVPD
EEEECCCCCCCCCCC		31.0725159151
20PhosphorylationHLVDSDSSLAKVPDE
EEECCCCCCCCCCCC		37.0225159151
23UbiquitinationDSDSSLAKVPDEAPK
CCCCCCCCCCCCCCC		60.64-
27 (in isoform 2)Phosphorylation-61.8827251275
29 (in isoform 2)Phosphorylation-29.8027251275
30 (in isoform 2)Phosphorylation-61.2127251275
30UbiquitinationKVPDEAPKVGILGSG
CCCCCCCCCEEECCH		61.21-
33 (in isoform 2)Ubiquitination-4.39-
42PhosphorylationGSGDFARSLATRLVG
CCHHHHHHHHHHHHC		20.9421406692
45PhosphorylationDFARSLATRLVGSGF
HHHHHHHHHHHCCCC		29.8121406692
97PhosphorylationAVFREHYSSLCSLSD
EHHHHHHHHHHHHHH		20.8123898821
98PhosphorylationVFREHYSSLCSLSDQ
HHHHHHHHHHHHHHH		26.6524275569
141PhosphorylationASLFPTCTVVKAFNV
HHHCCCCHHHHHHCE		30.71-
227PhosphorylationLGLFVCFYAYNFVRD
HHHHHHHHHHHHHHH		11.7518083107
239PhosphorylationVRDVLQPYVQESQNK
HHHHHHHHHHHHCCC		11.2120068231
243PhosphorylationLQPYVQESQNKFFKL
HHHHHHHHCCCCCCC		23.2020068231
253PhosphorylationKFFKLPVSVVNTTLP
CCCCCCHHHHCCHHH		20.5720068231
256N-linked_GlycosylationKLPVSVVNTTLPCVA
CCCHHHHCCHHHHHH		25.7822624035
288PhosphorylationQLRRGTKYQRFPDWL
HHHCCCCCHHCCHHH		12.54-
331PhosphorylationPLRRAHRYDLVNLAV
HHHHHHHHHHHHHHH		12.0818083107
339 (in isoform 4)Ubiquitination-29.1421890473
339 (in isoform 3)Ubiquitination-29.1421890473
339 (in isoform 1)Ubiquitination-29.1421890473
339UbiquitinationDLVNLAVKQVLANKS
HHHHHHHHHHHCCCC		29.1421890473
344N-linked_GlycosylationAVKQVLANKSHLWVE
HHHHHHCCCCCEEEE		42.0522624035
349 (in isoform 2)Ubiquitination-7.0521890473
453S-palmitoylationKALFLLPCISRRLAR
HHHHHHHHHHHHHHH		4.4429575903
469PhosphorylationRRGWERESTIKFTLP
HCCCCCCCEEEEECC		41.4730266825
470PhosphorylationRGWERESTIKFTLPT
CCCCCCCEEEEECCC		24.3530266825
471 (in isoform 3)Ubiquitination-4.8721890473
472UbiquitinationWERESTIKFTLPTDH
CCCCCEEEEECCCCH		32.172189047
472 (in isoform 1)Ubiquitination-32.1721890473
474PhosphorylationRESTIKFTLPTDHAL
CCCEEEEECCCCHHH		27.1626699800
477PhosphorylationTIKFTLPTDHALAEK
EEEEECCCCHHHHHH		43.4630108239
479 (in isoform 2)Phosphorylation-25.7224719451
482 (in isoform 2)Ubiquitination-19.6121890473
483 (in isoform 3)Ubiquitination-58.6921890473
484UbiquitinationTDHALAEKTSHV---
CCHHHHHHCCCC---		50.1221139048
484 (in isoform 1)Ubiquitination-50.1221890473
485PhosphorylationDHALAEKTSHV----
CHHHHHHCCCC----		18.6430266825
486PhosphorylationHALAEKTSHV-----
HHHHHHCCCC-----		33.0630266825
487 (in isoform 2)Phosphorylation-34.2427251275
494 (in isoform 2)Ubiquitination-21890473
495 (in isoform 2)Phosphorylation-24719451
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 STEA3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STEA3_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 STEA3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BNI3L_HUMANBNIP3Lphysical
12606722
PMYT1_HUMANPKMYT1physical
12606722
TT21A_HUMANTTC21Aphysical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615234Anemia, hypochromic microcytic, with iron overload 2 (AHMIO2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STEA3_HUMAN

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Related Literatures of Post-Translational Modification

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