STR3N_HUMAN - dbPTM
STR3N_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STR3N_HUMAN
UniProt AC O95772
Protein Name STARD3 N-terminal-like protein {ECO:0000303|PubMed:24105263}
Gene Name STARD3NL {ECO:0000303|PubMed:24105263, ECO:0000312|HGNC:HGNC:19169}
Organism Homo sapiens (Human).
Sequence Length 234
Subcellular Localization Late endosome membrane
Multi-pass membrane protein . Localizes to contact sites between the endoplasmic reticulum and late endosomes: associates with the endoplasmic reticulum membrane via interaction with VAPA and VAPB.
Protein Description Tethering protein that creates contact site between the endoplasmic reticulum and late endosomes: localizes to late endosome membranes and contacts the endoplasmic reticulum via interaction with VAPA and VAPB. [PubMed: 24105263]
Protein Sequence MNHLPEDMENALTGSQSSHASLRNIHSINPTQLMARIESYEGREKKGISDVRRTFCLFVTFDLLFVTLLWIIELNVNGGIENTLEKEVMQYDYYSSYFDIFLLAVFRFKVLILAYAVCRLRHWWAIALTTAVTSAFLLAKVILSKLFSQGAFGYVLPIISFILAWIETWFLDFKVLPQEAEEENRLLIVQDASERAALIPGGLSDGQFYSPPESEAGSEEAEEKQDSEKPLLEL
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
1Acetylation-------MNHLPEDM
-------CCCCCHHH
20068231
10 (in isoform 2)Phosphorylation-22210691
11 (in isoform 2)Phosphorylation-22210691
13PhosphorylationEDMENALTGSQSSHA
HHHHHHHHCCCCCCH
29255136
14 (in isoform 2)Phosphorylation-27135362
15PhosphorylationMENALTGSQSSHASL
HHHHHHCCCCCCHHH
29255136
17PhosphorylationNALTGSQSSHASLRN
HHHHCCCCCCHHHCC
29255136
18PhosphorylationALTGSQSSHASLRNI
HHHCCCCCCHHHCCH
29255136
21PhosphorylationGSQSSHASLRNIHSI
CCCCCCHHHCCHHHC
29255136
27PhosphorylationASLRNIHSINPTQLM
HHHCCHHHCCHHHHH
30266825
31PhosphorylationNIHSINPTQLMARIE
CHHHCCHHHHHHHHH
23090842
39PhosphorylationQLMARIESYEGREKK
HHHHHHHHHCCCHHC
23401153
40PhosphorylationLMARIESYEGREKKG
HHHHHHHHCCCHHCC
23403867
46AcetylationSYEGREKKGISDVRR
HHCCCHHCCCCHHHH
7825013
193PhosphorylationLLIVQDASERAALIP
EEEEECHHHHHHCCC
19664994
204PhosphorylationALIPGGLSDGQFYSP
HCCCCCCCCCCCCCC
25159151
209PhosphorylationGLSDGQFYSPPESEA
CCCCCCCCCCCCCCC
22115753
210PhosphorylationLSDGQFYSPPESEAG
CCCCCCCCCCCCCCC
26503892
214PhosphorylationQFYSPPESEAGSEEA
CCCCCCCCCCCCHHH
26503892
218PhosphorylationPPESEAGSEEAEEKQ
CCCCCCCCHHHHHHH
26503892
222 (in isoform 2)Ubiquitination-21906983
227PhosphorylationEAEEKQDSEKPLLEL
HHHHHHHCCCCCCCC
25850435
229UbiquitinationEEKQDSEKPLLEL--
HHHHHCCCCCCCC--
-
229UbiquitinationEEKQDSEKPLLEL--
HHHHHCCCCCCCC--
21906983
229 (in isoform 1)Ubiquitination-21906983

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 STR3N_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STR3N_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 STR3N_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STOM_HUMANSTOMphysical
27173435

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STR3N_HUMAN

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Related Literatures of Post-Translational Modification

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