ACVL1_HUMAN - dbPTM
ACVL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACVL1_HUMAN
UniProt AC P37023
Protein Name Serine/threonine-protein kinase receptor R3
Gene Name ACVRL1
Organism Homo sapiens (Human).
Sequence Length 503
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Type I receptor for TGF-beta family ligands BMP9/GDF2 and BMP10 and important regulator of normal blood vessel development. On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. May bind activin as well..
Protein Sequence MTLGSPRKGLLMLLMALVTQGDPVKPSRGPLVTCTCESPHCKGPTCRGAWCTVVLVREEGRHPQEHRGCGNLHRELCRGRPTEFVNHYCCDSHLCNHNVSLVLEATQPPSEQPGTDGQLALILGPVLALLALVALGVLGLWHVRRRQEKQRGLHSELGESSLILKASEQGDSMLGDLLDSDCTTGSGSGLPFLVQRTVARQVALVECVGKGRYGEVWRGLWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWLITHYHEHGSLYDFLQRQTLEPHLALRLAVSAACGLAHLHVEIFGTQGKPAIAHRDFKSRNVLVKSNLQCCIADLGLAVMHSQGSDYLDIGNNPRVGTKRYMAPEVLDEQIRTDCFESYKWTDIWAFGLVLWEIARRTIVNGIVEDYRPPFYDVVPNDPSFEDMKKVVCVDQQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKKTLQKISNSPEKPKVIQ
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
5Phosphorylation---MTLGSPRKGLLM
---CCCCCHHHHHHH
25.3320562096
98N-linked_GlycosylationDSHLCNHNVSLVLEA
CHHHCCCCEEEEEEE
15.87UniProtKB CARBOHYD
155PhosphorylationEKQRGLHSELGESSL
HHHCCCCCCCCCCCE
39.2923403867
160PhosphorylationLHSELGESSLILKAS
CCCCCCCCCEEEEHH
28.7526657352
161PhosphorylationHSELGESSLILKASE
CCCCCCCCEEEEHHH
18.3523403867
375PhosphorylationPRVGTKRYMAPEVLD
CCCCCCEECCHHHHC
10.1371763
412PhosphorylationLWEIARRTIVNGIVE
HHHHHHHHHHHCHHC
24.5924719451
421PhosphorylationVNGIVEDYRPPFYDV
HHCHHCCCCCCCCCC
16.12119601
439AcetylationDPSFEDMKKVVCVDQ
CCCHHHHCEEEEECC
55.537366015
440AcetylationPSFEDMKKVVCVDQQ
CCHHHHCEEEEECCC
33.017366025
481PhosphorylationPNPSARLTALRIKKT
CCHHHHHHHHHHHHH
20.3524719451
495PhosphorylationTLQKISNSPEKPKVI
HHHHHHCCCCCCCCC
27.8723403867

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 ACVL1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACVL1_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 ACVL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TGFB1_HUMANTGFB1physical
10716993
T22D1_HUMANTSC22D1physical
21791611
IGSF1_HUMANIGSF1physical
11266516
HS90A_HUMANHSP90AA1physical
21465483
BAMBI_HUMANBAMBIphysical
19758997
EGLN_HUMANENGphysical
15702480
PEG10_HUMANPEG10physical
15611116
NR1H2_HUMANNR1H2physical
12393874
CSK2B_HUMANCSNK2Bphysical
19592636
FKB1A_HUMANFKBP1Aphysical
19592636
SMAD1_HUMANSMAD1physical
19592636
TGFB1_HUMANTGFB1physical
8242742
INHBA_HUMANINHBAphysical
8242742
TGFR1_HUMANTGFBR1physical
8242742
SCMC1_HUMANSLC25A24physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACVL1_HUMAN

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Related Literatures of Post-Translational Modification

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