SMAD6_HUMAN - dbPTM
SMAD6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMAD6_HUMAN
UniProt AC O43541
Protein Name Mothers against decapentaplegic homolog 6
Gene Name SMAD6
Organism Homo sapiens (Human).
Sequence Length 496
Subcellular Localization Nucleus .
Protein Description Acts as a mediator of TGF-beta and BMP antiflammatory activity. Suppresses IL1R-TLR signaling through its direct interaction with PEL1, preventing NF-kappa-B activation, nuclear transport and NF-kappa-B-mediated expression of proinflammatory genes. May block the BMP-SMAD1 signaling pathway by competing with SMAD4 for receptor-activated SMAD1-binding. Binds to regulatory elements in target promoter regions..
Protein Sequence MFRSKRSGLVRRLWRSRVVPDREEGGSGGGGGGDEDGSLGSRAEPAPRAREGGGCGRSEVRPVAPRRPRDAVGQRGAQGAGRRRRAGGPPRPMSEPGAGAGSSLLDVAEPGGPGWLPESDCETVTCCLFSERDAAGAPRDASDPLAGAALEPAGGGRSREARSRLLLLEQELKTVTYSLLKRLKERSLDTLLEAVESRGGVPGGCVLVPRADLRLGGQPAPPQLLLGRLFRWPDLQHAVELKPLCGCHSFAAAADGPTVCCNPYHFSRLCGPESPPPPYSRLSPRDEYKPLDLSDSTLSYTETEATNSLITAPGEFSDASMSPDATKPSHWCSVAYWEHRTRVGRLYAVYDQAVSIFYDLPQGSGFCLGQLNLEQRSESVRRTRSKIGFGILLSKEPDGVWAYNRGEHPIFVNSPTLDAPGGRALVVRKVPPGYSIKVFDFERSGLQHAPEPDAADGPYDPNSVRISFAKGWGPCYSRQFITSCPCWLEILLNNPR
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
2 (in isoform 2)Phosphorylation-14.02-
4Phosphorylation----MFRSKRSGLVR
----CCCCHHHHHHH		22.5830622161
7Phosphorylation-MFRSKRSGLVRRLW
-CCCCHHHHHHHHHH		39.9730622161
19 (in isoform 2)Phosphorylation-3.87-
27PhosphorylationPDREEGGSGGGGGGD
CCCCCCCCCCCCCCC		45.1629262532
38PhosphorylationGGGDEDGSLGSRAEP
CCCCCCCCCCCCCCC		41.7129262532
41PhosphorylationDEDGSLGSRAEPAPR
CCCCCCCCCCCCCCC		33.3429262532
75MethylationPRDAVGQRGAQGAGR
CCCCCCCCCCCCCCC		36.16115917153
82MethylationRGAQGAGRRRRAGGP
CCCCCCCCCCCCCCC		28.53-
173UbiquitinationLLLEQELKTVTYSLL
HHHHHHHHHHHHHHH		39.95PubMed
177PhosphorylationQELKTVTYSLLKRLK
HHHHHHHHHHHHHHH		7.9324719451
178PhosphorylationELKTVTYSLLKRLKE
HHHHHHHHHHHHHHH		20.1924719451
190PhosphorylationLKERSLDTLLEAVES
HHHCCHHHHHHHHHH		38.2422199227
197PhosphorylationTLLEAVESRGGVPGG
HHHHHHHHCCCCCCC		29.6222199227
274PhosphorylationSRLCGPESPPPPYSR
HHHCCCCCCCCCCCC		45.9327732954
280PhosphorylationESPPPPYSRLSPRDE
CCCCCCCCCCCCCCC		32.3020363803
283PhosphorylationPPPYSRLSPRDEYKP
CCCCCCCCCCCCCCC		19.4420068231
385O-linked_GlycosylationESVRRTRSKIGFGIL
HHHHHHHHHHCCEEE		28.1931492838
386UbiquitinationSVRRTRSKIGFGILL
HHHHHHHHHCCEEEE		43.4933845483
394O-linked_GlycosylationIGFGILLSKEPDGVW
HCCEEEEECCCCCEE		31.3731492838
435PhosphorylationRKVPPGYSIKVFDFE
EECCCCCEEEEEEEE		23.1122817900
459PhosphorylationPDAADGPYDPNSVRI
CCCCCCCCCCCCEEE		49.9532142685
467PhosphorylationDPNSVRISFAKGWGP
CCCCEEEEEECCCCC		14.4832142685
470UbiquitinationSVRISFAKGWGPCYS
CEEEEEECCCCCCCC		53.86-
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
435SPhosphorylationKinasePRKXP51817
Uniprot
-KUbiquitinationE3 ubiquitin ligaseWWP1Q9H0M0
PMID:15221015
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:16299379
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
173Kubiquitylation

23455153
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 SMAD6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTBP1_HUMANCTBP1physical
14645520
M3K7_HUMANMAP3K7physical
11737269
TAB1_HUMANTAB1physical
11737269
HXC8_HUMANHOXC8physical
10722652
STRAP_HUMANSTRAPphysical
10757800
SMAD7_HUMANSMAD7physical
9256479
SMAD4_HUMANSMAD4physical
15817471
NEDD4_HUMANNEDD4physical
15496141
WWP1_HUMANWWP1physical
15221015
SMUF1_HUMANSMURF1physical
15221015
SMUF2_HUMANSMURF2physical
15221015
ZEB1_HUMANZEB1physical
20514018
T22D1_HUMANTSC22D1physical
21791611
PELI1_HUMANPELI1physical
16951688
STABP_HUMANSTAMBPphysical
11483516
SMAD1_HUMANSMAD1physical
11483516
BMR1B_HUMANBMPR1Bphysical
9436979
TGFR1_HUMANTGFBR1physical
9436979
ACTY_HUMANACTR1Bphysical
9436979
SMAD1_HUMANSMAD1physical
9436979
BAMBI_HUMANBAMBIphysical
19758997
BMPR2_HUMANBMPR2physical
20663871
ACVR1_HUMANACVR1physical
20663871
BMR1A_HUMANBMPR1Aphysical
20663871
ACV1B_HUMANACVR1Bphysical
20663871
TGFR1_HUMANTGFBR1physical
20663871
AVR2B_HUMANACVR2Bphysical
20663871
MYD88_HUMANMYD88physical
21897371
SMUF1_HUMANSMURF1physical
21897371
UBE2O_HUMANUBE2Ophysical
23455153
ACVR1_HUMANACVR1physical
23455153
UBP11_HUMANUSP11physical
24850914
UBP15_HUMANUSP15physical
24850914
BPIA1_HUMANBPIFA1physical
24850914
LYSC_HUMANLYZphysical
24850914
PIGR_HUMANPIGRphysical
24850914
WWP1_HUMANWWP1physical
24850914
WWP2_HUMANWWP2physical
24850914
ITCH_HUMANITCHphysical
24850914
NED4L_HUMANNEDD4Lphysical
24850914
SMUF2_HUMANSMURF2physical
24850914
NASP_HUMANNASPphysical
24850914
IMA1_HUMANKPNA2physical
24850914
CTBP1_HUMANCTBP1physical
24850914
CTBP2_HUMANCTBP2physical
24850914
SMAD7_HUMANSMAD7physical
26555259
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614823Aortic valve disease 2 (AOVD2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMAD6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Smad6 is a protein kinase X phosphorylation substrate and is requiredfor HL-60 cell differentiation.";
Glesne D., Huberman E.;
Oncogene 25:4086-4098(2006).
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRKX, MUTAGENESIS OFSER-435, AND PHOSPHORYLATION AT SER-435.

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