SMAD1_HUMAN - dbPTM
SMAD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMAD1_HUMAN
UniProt AC Q15797
Protein Name Mothers against decapentaplegic homolog 1
Gene Name SMAD1
Organism Homo sapiens (Human).
Sequence Length 465
Subcellular Localization Cytoplasm . Nucleus . Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with SMAD4 (PubMed:15647271). Co-localizes with LEMD3 at the nucleus inner membrane (PubMed:15647271). Exported from the nucleus to the cytoplasm when
Protein Description Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD1 is a receptor-regulated SMAD (R-SMAD). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. May act synergistically with SMAD4 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression..
Protein Sequence MNVTSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDALVKKLKKKKGAMEELEKALSCPGQPSNCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVESPVLPPVLVPRHSEYNPQHSLLAQFRNLGQNEPHMPLNATFPDSFQQPNSHPFPHSPNSSYPNSPGSSSSTYPHSPTSSDPGSPFQMPADTPPPAYLPPEDPMTQDGSQPMDTNMMAPPLPSEINRGDVQAVAYEEPKHWCSIVYYELNNRVGEAFHASSTSVLVDGFTDPSNNKNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNYHHGFHPTTVCKIPSGCSLKIFNNQEFAQLLAQSVNHGFETVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS
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
1Acetylation-------MNVTSLFS
-------CCCCCCCC
9.09-
5Phosphorylation---MNVTSLFSFTSP
---CCCCCCCCCCCH
24.1228348404
8PhosphorylationMNVTSLFSFTSPAVK
CCCCCCCCCCCHHHH
32.6726270265
10PhosphorylationVTSLFSFTSPAVKRL
CCCCCCCCCHHHHHH
32.3822199227
11PhosphorylationTSLFSFTSPAVKRLL
CCCCCCCCHHHHHHH
14.6222199227
21UbiquitinationVKRLLGWKQGDEEEK
HHHHHCCCCCCHHHH
42.4729967540
28UbiquitinationKQGDEEEKWAEKAVD
CCCCHHHHHHHHHHH
55.7927667366
32UbiquitinationEEEKWAEKAVDALVK
HHHHHHHHHHHHHHH
46.0629967540
62PhosphorylationLSCPGQPSNCVTIPR
HCCCCCCCCEEEECC
34.6724400094
78PhosphorylationLDGRLQVSHRKGLPH
CCCCEEEECCCCCCE
12.4726670566
81UbiquitinationRLQVSHRKGLPHVIY
CEEEECCCCCCEEEE
60.4233845483
88PhosphorylationKGLPHVIYCRVWRWP
CCCCEEEEEEEEECC
3.52-
116UbiquitinationCEFPFGSKQKEVCIN
ECCCCCCCCCEEEEC
66.8122817900
116SumoylationCEFPFGSKQKEVCIN
ECCCCCCCCCEEEEC
66.81-
118UbiquitinationFPFGSKQKEVCINPY
CCCCCCCCEEEECCC
56.7122817900
118SumoylationFPFGSKQKEVCINPY
CCCCCCCCEEEECCC
56.71-
127PhosphorylationVCINPYHYKRVESPV
EEECCCCCCCCCCCC
8.4712601080
132PhosphorylationYHYKRVESPVLPPVL
CCCCCCCCCCCCCEE
19.9030266825
144PhosphorylationPVLVPRHSEYNPQHS
CEECCCCCCCCCCCC
42.9524719451
146PhosphorylationLVPRHSEYNPQHSLL
ECCCCCCCCCCCCHH
34.8527282143
151PhosphorylationSEYNPQHSLLAQFRN
CCCCCCCCHHHHHHH
21.6029214152
187PhosphorylationNSHPFPHSPNSSYPN
CCCCCCCCCCCCCCC
26.4722817900
195PhosphorylationPNSSYPNSPGSSSST
CCCCCCCCCCCCCCC
26.5722817900
202PhosphorylationSPGSSSSTYPHSPTS
CCCCCCCCCCCCCCC
42.9122817900
206PhosphorylationSSSTYPHSPTSSDPG
CCCCCCCCCCCCCCC
25.9322817900
214PhosphorylationPTSSDPGSPFQMPAD
CCCCCCCCCCCCCCC
28.1222817900
239PhosphorylationDPMTQDGSQPMDTNM
CCCCCCCCCCCCCCC
39.1222588298
265PhosphorylationGDVQAVAYEEPKHWC
CCEEEEEECCCCCEE
17.7727642862
269UbiquitinationAVAYEEPKHWCSIVY
EEEECCCCCEEEEEE
53.6822817900
315PhosphorylationRFCLGLLSNVNRNST
CEEHHHHCCCCCCCC
43.7221712546
321PhosphorylationLSNVNRNSTIENTRR
HCCCCCCCCCHHHHH
27.7628348404
322PhosphorylationSNVNRNSTIENTRRH
CCCCCCCCCHHHHHH
35.5422985185
337PhosphorylationIGKGVHLYYVGGEVY
CCCCEEEEEECCEEE
4.9222468782
338PhosphorylationGKGVHLYYVGGEVYA
CCCEEEEEECCEEEE
10.0522468782
344PhosphorylationYYVGGEVYAECLSDS
EEECCEEEEECCCCC
7.7422468782
418UbiquitinationTIRMSFVKGWGAEYH
CEEHHHHCCCCCCHH
47.1121890473
452PhosphorylationQWLDKVLTQMGSPHN
HHHHHHHHHCCCCCC
21.3525159151
456PhosphorylationKVLTQMGSPHNPISS
HHHHHCCCCCCCCCC
20.0425159151
462PhosphorylationGSPHNPISSVS----
CCCCCCCCCCC----
26.4122322096
463PhosphorylationSPHNPISSVS-----
CCCCCCCCCC-----
27.4022322096
465PhosphorylationHNPISSVS-------
CCCCCCCC-------
36.1322322096

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
187SPhosphorylationKinaseMAPK1P28482
GPS
187SPhosphorylationKinaseCDK8P49336
PSP
187SPhosphorylationKinaseCDK9P50750
PSP
195SPhosphorylationKinaseMAPK1P28482
GPS
195SPhosphorylationKinaseCDK8P49336
PSP
195SPhosphorylationKinaseCDK9P50750
PSP
202TPhosphorylationKinaseGSK3BP49841
PSP
206SPhosphorylationKinaseCDK7P50613
PSP
206SPhosphorylationKinaseCDK8P49336
PSP
206SPhosphorylationKinaseCDK9P50750
PSP
206SPhosphorylationKinaseMAPK1P28482
GPS
214SPhosphorylationKinaseCDK8P49336
PSP
214SPhosphorylationKinaseCDK9P50750
PSP
214SPhosphorylationKinaseMAPK1P28482
GPS
239SPhosphorylationKinaseATMQ13315
PSP
322TPhosphorylationKinaseTNIKQ9UKE5
Uniprot
322TPhosphorylationKinaseMINKQ8N4C8
PSP
322TPhosphorylationKinaseHGKO95819
PSP
462SPhosphorylationKinaseBMR1BO00238
PhosphoELM
463SPhosphorylationKinaseBMR1BO00238
PhosphoELM
465SPhosphorylationKinaseBMR1BO00238
PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:14711801
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:14701756
-KUbiquitinationE3 ubiquitin ligaseSMURF2Q9HAU4
PMID:11158580

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMAD1_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 SMAD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HIPK2_HUMANHIPK2physical
12874272
SKI_HUMANSKIphysical
12874272
SMAD4_HUMANSMAD4physical
12874272
DVL1_HUMANDVL1physical
12650946
ERBIN_HUMANERBB2IPphysical
12650946
NGN1_HUMANNEUROG1physical
11239394
SNIP1_HUMANSNIP1physical
10887155
EP300_HUMANEP300physical
10205054
FOXG1_HUMANFOXG1physical
11387330
PSB4_HUMANPSMB4physical
12097147
RUNX2_HUMANRUNX2physical
10962029
SMUF2_HUMANSMURF2physical
11016919
HXC8_HUMANHOXC8physical
10224145
RUNX1_HUMANRUNX1physical
10531362
RUNX2_HUMANRUNX2physical
10531362
RUNX3_HUMANRUNX3physical
10531362
PSB4_HUMANPSMB4physical
11438941
OAZ3_HUMANOAZ3physical
11438941
CASL_HUMANNEDD9physical
11118211
SMAD4_HUMANSMAD4physical
11700304
SMAD6_HUMANSMAD6physical
9256479
TCF20_HUMANTCF20physical
20211142
CREST_HUMANSS18L1physical
20211142
WWP1_HUMANWWP1physical
15221015
SMUF1_HUMANSMURF1physical
15221015
SMUF2_HUMANSMURF2physical
15221015
NKX32_HUMANNKX3-2physical
14612411
PIAS4_HUMANPIAS4physical
12904571
TYY1_HUMANYY1physical
12808092
MED15_HUMANMED15physical
12167862
MED24_HUMANMED24physical
12167862
MED6_HUMANMED6physical
12167862
SMAD4_HUMANSMAD4physical
12167862
EVI1_HUMANMECOMphysical
15849193
KAT2A_HUMANKAT2Aphysical
15009097
PSB4_HUMANPSMB4physical
11571290
OAZ1_HUMANOAZ1physical
11571290
SKI_HUMANSKIphysical
14699069
HDAC1_HUMANHDAC1physical
14699069
SMUF2_HUMANSMURF2physical
11158580
SMUF1_HUMANSMURF1physical
17289590
NU214_HUMANNUP214physical
17289590
FOXO3_HUMANFOXO3physical
17289590
CHIP_HUMANSTUB1physical
21454478
UCHL3_HUMANUCHL3physical
21453705
SMAD4_HUMANSMAD4physical
14701756
SMUF1_HUMANSMURF1physical
14701756
SMUF2_HUMANSMURF2physical
14701756
CHIP_HUMANSTUB1physical
14701756
USP9X_HUMANUSP9Xphysical
19135894
SKI_HUMANSKIphysical
12426322
SKIL_HUMANSKILphysical
12426322
MEN1_HUMANMEN1physical
12649288
NEDD4_HUMANNEDD4physical
21308777
UBP15_HUMANUSP15physical
21947082
CDK8_HUMANCDK8physical
19914168
YAP1_HUMANYAP1physical
19914168
SMAD6_HUMANSMAD6physical
12857866
SMUF1_HUMANSMURF1physical
21685363
YAP1_HUMANYAP1physical
21685363
SMUF1_HUMANSMURF1physical
19917253
UBP15_HUMANUSP15physical
22344298
HGS_HUMANHGSphysical
11094085
ZCH12_HUMANZCCHC12physical
19416967
PAX6_HUMANPAX6physical
17251190
SMAD6_HUMANSMAD6physical
9436979
SMAD4_HUMANSMAD4physical
9436979
PPM1A_HUMANPPM1Aphysical
22588298
P53_HUMANTP53physical
22588298
A4_HUMANAPPphysical
21832049
SMAD1_HUMANSMAD1physical
9111321
SMAD2_HUMANSMAD2physical
9111321
SMAD3_HUMANSMAD3physical
9111321
SMAD4_HUMANSMAD4physical
9111321
PSD11_HUMANPSMD11physical
15231748
KMT2D_HUMANKMT2Dphysical
15231748
MAST4_HUMANMAST4physical
15231748
ZEB2_HUMANZEB2physical
15231748
HBP1_HUMANHBP1physical
15231748
SF3B1_HUMANSF3B1physical
15231748
PIAS1_HUMANPIAS1physical
15231748
AP2A2_HUMANAP2A2physical
15231748
RU17_HUMANSNRNP70physical
15231748
ALDR_HUMANAKR1B1physical
15231748
RFX1_HUMANRFX1physical
15231748
PSB4_HUMANPSMB4physical
15231748
SOX5_HUMANSOX5physical
15231748
ZNF76_HUMANZNF76physical
15231748
NEDD4_HUMANNEDD4physical
15231748
XPC_HUMANXPCphysical
15231748
NOTC2_HUMANNOTCH2physical
15231748
SMAD4_HUMANSMAD4physical
15231748
CASL_HUMANNEDD9physical
15231748
PUM1_HUMANPUM1physical
15231748
TTF1_HUMANTTF1physical
15231748
SMAD1_HUMANSMAD1physical
15231748
CAMP1_HUMANCAMSAP1physical
15231748
I2BP1_HUMANIRF2BP1physical
15231748
MGAP_HUMANMGAphysical
15231748
PIAS4_HUMANPIAS4physical
15231748
ZSCA4_HUMANZSCAN4physical
15231748
SMCE1_HUMANSMARCE1physical
15231748
ANR27_HUMANANKRD27physical
15231748
INP4A_HUMANINPP4Aphysical
15231748
PSMD1_HUMANPSMD1physical
15231748
SMAD5_HUMANSMAD5physical
15231748
PIGQ_HUMANPIGQphysical
15231748
ZN251_HUMANZNF251physical
15231748
SMUF2_HUMANSMURF2physical
15231748
SMUF1_HUMANSMURF1physical
15231748
ZDHC3_HUMANZDHHC3physical
15231748
MKL2_HUMANMKL2physical
15231748
TTF2_HUMANTTF2physical
15231748
ICK_HUMANICKphysical
15231748
ZN510_HUMANZNF510physical
15231748
MAN1_HUMANLEMD3physical
15231748
CHMP3_HUMANCHMP3physical
15231748
STA13_HUMANSTARD13physical
15231748
GMEB1_HUMANGMEB1physical
15231748
MAN1_HUMANLEMD3physical
15489854
SMAD4_HUMANSMAD4physical
17183365
ANDR_HUMANARphysical
17183365
UBC_HUMANUBCphysical
11438941
SMUF1_HUMANSMURF1physical
24828823
MEP50_HUMANWDR77physical
23734213
ANDR_HUMANARphysical
23734213
LEF1_HUMANLEF1physical
15750622
PARD3_HUMANPARD3physical
12650946
GSK3B_HUMANGSK3Bphysical
25241761
GLI3_HUMANGLI3physical
25241761
SMAD7_HUMANSMAD7physical
26555259
SMAD4_HUMANSMAD4physical
26555259
SMUF1_HUMANSMURF1physical
28881580
SMAD4_HUMANSMAD4physical
28468752
SMUF2_HUMANSMURF2physical
28468752

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 SMAD1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The TGF-beta family mediator Smad1 is phosphorylated directly andactivated functionally by the BMP receptor kinase.";
Kretzschmar M., Liu F., Hata A., Doody J., Massague J.;
Genes Dev. 11:984-995(1997).
Cited for: PHOSPHORYLATION AT SER-463 AND SER-465.
"Smad inhibition by the Ste20 kinase Misshapen.";
Kaneko S., Chen X., Lu P., Yao X., Wright T.G., Rajurkar M.,Kariya K., Mao J., Ip Y.T., Xu L.;
Proc. Natl. Acad. Sci. U.S.A. 108:11127-11132(2011).
Cited for: PHOSPHORYLATION AT THR-322.

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