ACV1C_HUMAN - dbPTM
ACV1C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACV1C_HUMAN
UniProt AC Q8NER5
Protein Name Activin receptor type-1C
Gene Name ACVR1C {ECO:0000312|HGNC:HGNC:18123}
Organism Homo sapiens (Human).
Sequence Length 493
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description Serine/threonine protein kinase which forms a receptor complex on ligand binding. The receptor complex consisting of 2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators, SMAD2 and SMAD3. Receptor for activin AB, activin B and NODAL. Plays a role in cell differentiation, growth arrest and apoptosis..
Protein Sequence MTRALCSALRQALLLLAAAAELSPGLKCVCLLCDSSNFTCQTEGACWASVMLTNGKEQVIKSCVSLPELNAQVFCHSSNNVTKTECCFTDFCNNITLHLPTASPNAPKLGPMELAIIITVPVCLLSIAAMLTVWACQGRQCSYRKKKRPNVEEPLSECNLVNAGKTLKDLIYDVTASGSGSGLPLLVQRTIARTIVLQEIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEYHEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSILNTIDIPQNPKVGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLVYWEIARRCSVGGIVEEYQLPYYDMVPSDPSIEEMRKVVCDQKFRPSIPNQWQSCEALRVMGRIMRECWYANGAARLTALRIKKTISQLCVKEDCKA
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
2Phosphorylation------MTRALCSAL
------CHHHHHHHH
25.3429083192
7Phosphorylation-MTRALCSALRQALL
-CHHHHHHHHHHHHH
31.0529083192
23PhosphorylationLAAAAELSPGLKCVC
HHHHHHCCCCCEEEE
14.3924719451
147AcetylationQCSYRKKKRPNVEEP
CCCCCCCCCCCCCCC
75.9111688409
165AcetylationCNLVNAGKTLKDLIY
CCCCCCCCCHHHHHE
48.5511688419
168AcetylationVNAGKTLKDLIYDVT
CCCCCCHHHHHEEEC
56.5711688429
172PhosphorylationKTLKDLIYDVTASGS
CCHHHHHEEECCCCC
16.2023607784
175PhosphorylationKDLIYDVTASGSGSG
HHHHEEECCCCCCCC
16.5323607784
177PhosphorylationLIYDVTASGSGSGLP
HHEEECCCCCCCCHH
24.9123607784
179PhosphorylationYDVTASGSGSGLPLL
EEECCCCCCCCHHHH
27.5623607784
181PhosphorylationVTASGSGSGLPLLVQ
ECCCCCCCCHHHHHH
38.5623607784
190PhosphorylationLPLLVQRTIARTIVL
HHHHHHHHHHHHHHH
11.2523607784
327UbiquitinationAHRDIKSKNILVKKC
ECCCCCCCCEEEEEC
42.90-
368PhosphorylationPKVGTKRYMAPEMLD
CCCCCCCCCCHHHHC
10.1322468782
377PhosphorylationAPEMLDDTMNVNIFE
CHHHHCCCCCCCHHH
15.4322468782
474PhosphorylationANGAARLTALRIKKT
HCHHHHHHHHHHHHH
20.3524719451

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 ACV1C_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACV1C_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 ACV1C_HUMAN !!

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

Oops, there are no PPI records of ACV1C_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACV1C_HUMAN

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Related Literatures of Post-Translational Modification

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