ITM2C_HUMAN - dbPTM
ITM2C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITM2C_HUMAN
UniProt AC Q9NQX7
Protein Name Integral membrane protein 2C
Gene Name ITM2C
Organism Homo sapiens (Human).
Sequence Length 267
Subcellular Localization Lysosome membrane
Single-pass type II membrane protein. Cell membrane
Single-pass type II membrane protein .
Protein Description Negative regulator of amyloid-beta peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation (By similarity)..
Protein Sequence MVKISFQPAVAGIKGDKADKASASAPAPASATEILLTPAREEQPPQHRSKRGGSVGGVCYLSMGMVVLLMGLVFASVYIYRYFFLAQLARDNFFRCGVLYEDSLSSQVRTQMELEEDVKIYLDENYERINVPVPQFGGGDPADIIHDFQRGLTAYHDISLDKCYVIELNTTIVLPPRNFWELLMNVKRGTYLPQTYIIQEEMVVTEHVSDKEALGSFIYHLCNGKDTYRLRRRATRRRINKRGAKNCNAIRHFENTFVVETLICGVV
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-----MVKISFQPAV
-----CCEEEECCCC
31.1921139048
5Phosphorylation---MVKISFQPAVAG
---CCEEEECCCCCC
16.47-
14UbiquitinationQPAVAGIKGDKADKA
CCCCCCCCCCCCCCC
61.2021890473
14 (in isoform 3)Ubiquitination-61.2021890473
14 (in isoform 2)Ubiquitination-61.2021890473
14 (in isoform 1)Ubiquitination-61.2021890473
14AcetylationQPAVAGIKGDKADKA
CCCCCCCCCCCCCCC
61.2025953088
17UbiquitinationVAGIKGDKADKASAS
CCCCCCCCCCCCCCC
68.1321890473
17 (in isoform 3)Ubiquitination-68.1321890473
17 (in isoform 2)Ubiquitination-68.1321890473
17 (in isoform 1)Ubiquitination-68.1321890473
20 (in isoform 3)Ubiquitination-49.4521890473
20 (in isoform 2)Ubiquitination-49.4521890473
20 (in isoform 1)Ubiquitination-49.4521890473
20UbiquitinationIKGDKADKASASAPA
CCCCCCCCCCCCCCC
49.4521890473
22PhosphorylationGDKADKASASAPAPA
CCCCCCCCCCCCCCC
28.6225850435
24PhosphorylationKADKASASAPAPASA
CCCCCCCCCCCCCCC
32.0825850435
30PhosphorylationASAPAPASATEILLT
CCCCCCCCCCEEECC
34.3625850435
32PhosphorylationAPAPASATEILLTPA
CCCCCCCCEEECCCC
22.5129255136
37PhosphorylationSATEILLTPAREEQP
CCCEEECCCCCCCCC
16.0829255136
105PhosphorylationVLYEDSLSSQVRTQM
EEECHHCCHHHHHHC
23.7528985074
106PhosphorylationLYEDSLSSQVRTQME
EECHHCCHHHHHHCC
37.6828985074
126PhosphorylationKIYLDENYERINVPV
EEEECCCCCEEECCC
12.4427642862
140 (in isoform 2)Ubiquitination-38.1921890473
164PhosphorylationDISLDKCYVIELNTT
ECCCCCEEEEEECCE
15.3724719451
169N-linked_GlycosylationKCYVIELNTTIVLPP
CEEEEEECCEEEECC
23.5315606899
171PhosphorylationYVIELNTTIVLPPRN
EEEEECCEEEECCCC
14.1724719451
187UbiquitinationWELLMNVKRGTYLPQ
HHHHHHHCCCCCCCC
39.852190698
187 (in isoform 1)Ubiquitination-39.8521890473

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 ITM2C_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITM2C_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 ITM2C_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MB12B_HUMANMVB12Bphysical
26186194
MB12B_HUMANMVB12Bphysical
28514442

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 ITM2C_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; THR-32 AND THR-37,AND MASS SPECTROMETRY.

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