ACVR1_HUMAN - dbPTM
ACVR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACVR1_HUMAN
UniProt AC Q04771
Protein Name Activin receptor type-1
Gene Name ACVR1
Organism Homo sapiens (Human).
Sequence Length 509
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description 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. Receptor for activin. May be involved for left-right pattern formation during embryogenesis (By similarity)..
Protein Sequence MVDGVMILPVLIMIALPSPSMEDEKPKVNPKLYMCVCEGLSCGNEDHCEGQQCFSSLSINDGFHVYQKGCFQVYEQGKMTCKTPPSPGQAVECCQGDWCNRNITAQLPTKGKSFPGTQNFHLEVGLIILSVVFAVCLLACLLGVALRKFKRRNQERLNPRDVEYGTIEGLITTNVGDSTLADLLDHSCTSGSGSGLPFLVQRTVARQITLLECVGKGRYGEVWRGSWQGENVAVKIFSSRDEKSWFRETELYNTVMLRHENILGFIASDMTSRHSSTQLWLITHYHEMGSLYDYLQLTTLDTVSCLRIVLSIASGLAHLHIEIFGTQGKPAIAHRDLKSKNILVKKNGQCCIADLGLAVMHSQSTNQLDVGNNPRVGTKRYMAPEVLDETIQVDCFDSYKRVDIWAFGLVLWEVARRMVSNGIVEDYKPPFYDVVPNDPSFEDMRKVVCVDQQRPNIPNRWFSDPTLTSLAKLMKECWYQNPSARLTALRIKKTLTKIDNSLDKLKTDC
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
20PhosphorylationMIALPSPSMEDEKPK
HHHCCCCCCCCCCCC		38.8624260401
102N-linked_GlycosylationQGDWCNRNITAQLPT
CCCCCCCCEEEECCC		23.2117660510
203PhosphorylationLPFLVQRTVARQITL
HHHHHHHHHHHHEEE		11.0472880217
226PhosphorylationYGEVWRGSWQGENVA
CCEEECCEECCCEEE		13.9814891623
252PhosphorylationWFRETELYNTVMLRH
CCCHHHHHHHHEECC		11.5327642862
340UbiquitinationAHRDLKSKNILVKKN
ECCCCCCCCEEEEEC		46.55-
362PhosphorylationLGLAVMHSQSTNQLD
CEEEEECCCCCCCCC		14.0230377224
364PhosphorylationLAVMHSQSTNQLDVG
EEEECCCCCCCCCCC		32.1330377224
365PhosphorylationAVMHSQSTNQLDVGN
EEECCCCCCCCCCCC		21.2430377224
381PhosphorylationPRVGTKRYMAPEVLD
CCCCCCEECCHHHHC		10.1323401153
390PhosphorylationAPEVLDETIQVDCFD
CHHHHCCCEEEECCC		19.1723401153
446UbiquitinationPSFEDMRKVVCVDQQ
CCHHHHHCEEEEECC		32.17-
472UbiquitinationPTLTSLAKLMKECWY
HHHHHHHHHHHHHHH		55.17-
475UbiquitinationTSLAKLMKECWYQNP
HHHHHHHHHHHHCCH		61.22-
487PhosphorylationQNPSARLTALRIKKT
CCHHHHHHHHHHHHH		20.3524719451
494PhosphorylationTALRIKKTLTKIDNS
HHHHHHHHHHHHHHH		34.3622817900
496PhosphorylationLRIKKTLTKIDNSLD
HHHHHHHHHHHHHHH		31.0522817900
497UbiquitinationRIKKTLTKIDNSLDK
HHHHHHHHHHHHHHH		51.69-
497MalonylationRIKKTLTKIDNSLDK
HHHHHHHHHHHHHHH		51.6926320211
501PhosphorylationTLTKIDNSLDKLKTD
HHHHHHHHHHHHHCC		33.9119085907
504UbiquitinationKIDNSLDKLKTDC--
HHHHHHHHHHCCC--		58.12-
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 ACVR1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACVR1_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 ACVR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FNTA_HUMANFNTAphysical
8599089
RAB17_MOUSERab17physical
15761153
RHOJ_MOUSERhojphysical
15761153
RB33B_MOUSERab33bphysical
15761153
RHOD_MOUSERhodphysical
15761153
RAB3B_MOUSERab3bphysical
15761153
RRAS2_MOUSERras2physical
15761153
CHIN_MOUSEChn1physical
15761153
RS27A_MOUSERps27aphysical
15761153
SQSTM_MOUSESqstm1physical
15761153
TGFR1_MOUSETgfbr1physical
15761153
PLEK_MOUSEPlekphysical
15761153
PKHB1_MOUSEPlekhb1physical
15761153
AJUBA_MOUSEAjubaphysical
15761153
FKBP4_MOUSEFkbp4physical
15761153
KBRS1_MOUSENkiras1physical
15761153
RHES_MOUSERasd2physical
15761153
RAB6B_MOUSERab6bphysical
15761153
RHBT1_MOUSERhobtb1physical
15761153
SNUT2_MOUSEUsp39physical
15761153
UBP21_MOUSEUsp21physical
15761153
UB2E3_MOUSEUbe2e3physical
15761153
UB2R2_MOUSEUbe2r2physical
15761153
FBX3_MOUSEFbxo3physical
15761153
WDR61_MOUSEWdr61physical
15761153
IKKB_MOUSEIkbkbphysical
15761153
NUAK2_MOUSENuak2physical
15761153
FANCL_MOUSEFanclphysical
15761153
UHMK1_MOUSEUhmk1physical
15761153
CDK14_MOUSECdk14physical
15761153
FGD6_MOUSEFgd6physical
15761153
ILKAP_MOUSEIlkapphysical
15761153
NAA20_MOUSENaa20physical
15761153
AP2B1_MOUSEAp2b1physical
15761153
STX8_MOUSEStx8physical
15761153
REBL1_MOUSERhebl1physical
15761153
RAP2A_MOUSERap2aphysical
15761153
FCHO1_MOUSEFcho1physical
15761153
BMPR2_HUMANBMPR2physical
7791754
GDF5_HUMANGDF5physical
8702914
SMAD5_HUMANSMAD5physical
10652350
SMAD1_HUMANSMAD1physical
10652350
SMAD1_HUMANSMAD1physical
9748228
SMAD5_HUMANSMAD5physical
9748228
T22D1_HUMANTSC22D1physical
21791611
IGSF1_HUMANIGSF1physical
11266516
SMUF1_HUMANSMURF1physical
12857866
BAMBI_HUMANBAMBIphysical
19758997
PEG10_HUMANPEG10physical
15611116
INHBA_HUMANINHBAphysical
8242742
AVR2A_HUMANACVR2Aphysical
8242742
BMR1A_HUMANBMPR1Aphysical
18436533
ACVR1_HUMANACVR1physical
18436533
BMR1A_HUMANBMPR1Aphysical
26186194
ACV1B_HUMANACVR1Bphysical
26186194
ACVL1_HUMANACVRL1physical
26186194
TGFA1_HUMANTGFBRAP1physical
26186194
GRM1A_HUMANGRAMD1Aphysical
26186194
MED16_HUMANMED16physical
26186194
RN149_HUMANRNF149physical
26186194
ARV1_HUMANARV1physical
26186194
OTUB1_HUMANOTUB1physical
25872870
TGFA1_HUMANTGFBRAP1physical
28514442
BMR1A_HUMANBMPR1Aphysical
28514442
BMPR2_HUMANBMPR2physical
28514442
RN149_HUMANRNF149physical
28514442
GRM1A_HUMANGRAMD1Aphysical
28514442
ACVL1_HUMANACVRL1physical
28514442
CD320_HUMANCD320physical
28514442
ARV1_HUMANARV1physical
28514442
Drug and Disease Associations
Kegg Disease
H00430 Fibrodysplasia ossificans progressiva (FOP)
OMIM Disease
135100Fibrodysplasia ossificans progressiva (FOP)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00171Adenosine triphosphate
Regulatory Network of ACVR1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-501, ANDMASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND MASSSPECTROMETRY.

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