SMAD5_HUMAN - dbPTM
SMAD5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMAD5_HUMAN
UniProt AC Q99717
Protein Name Mothers against decapentaplegic homolog 5
Gene Name SMAD5
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.
Protein Description Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD5 is a receptor-regulated SMAD (R-SMAD)..
Protein Sequence MTSMASLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDALVKKLKKKKGAMEELEKALSSPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLDICEFPFGSKQKEVCINPYHYKRVESPVLPPVLVPRHNEFNPQHSLLVQFRNLSHNEPHMPQNATFPDSFHQPNNTPFPLSPNSPYPPSPASSTYPNSPASSGPGSPFQLPADTPPPAYMPPDDQMGQDNSQPMDTSNNMIPQIMPSISSRDVQPVAYEEPKHWCSIVYYELNNRVGEAFHASSTSVLVDGFTDPSNNKSRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNFHHGFHPTTVCKIPSSCSLKIFNNQEFAQLLAQSVNHGFEAVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPLNPISSVS
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------MTSMASLFS
------CCCHHHHHH		27.4926074081
2Acetylation------MTSMASLFS
------CCCHHHHHH		27.4922223895
3Phosphorylation-----MTSMASLFSF
-----CCCHHHHHHC		15.8526074081
6Phosphorylation--MTSMASLFSFTSP
--CCCHHHHHHCCCH		22.7026074081
9PhosphorylationTSMASLFSFTSPAVK
CCHHHHHHCCCHHHH		32.6729255136
11PhosphorylationMASLFSFTSPAVKRL
HHHHHHCCCHHHHHH		32.3829255136
12PhosphorylationASLFSFTSPAVKRLL
HHHHHCCCHHHHHHH		14.6229255136
57PhosphorylationEELEKALSSPGQPSK
HHHHHHHCCCCCCCC		39.0729396449
58PhosphorylationELEKALSSPGQPSKC
HHHHHHCCCCCCCCE		33.6221815630
63PhosphorylationLSSPGQPSKCVTIPR
HCCCCCCCCEEECCC		30.6929396449
64UbiquitinationSSPGQPSKCVTIPRS
CCCCCCCCEEECCCC		39.13-
79PhosphorylationLDGRLQVSHRKGLPH
CCCCEEEECCCCCCE		12.4726670566
82UbiquitinationRLQVSHRKGLPHVIY
CEEEECCCCCCEEEE		60.42-
89PhosphorylationKGLPHVIYCRVWRWP
CCCCEEEEEEEEECC		3.52-
100O-linked_GlycosylationWRWPDLQSHHELKPL
EECCCCCCCCCCCCC		33.8230379171
128PhosphorylationVCINPYHYKRVESPV
EEECCCCCCCCCCCC		8.4712601080
133PhosphorylationYHYKRVESPVLPPVL
CCCCCCCCCCCCCEE		19.9030266825
152PhosphorylationNEFNPQHSLLVQFRN
CCCCCCHHHEEEEEC		20.3926055452
188PhosphorylationNNTPFPLSPNSPYPP
CCCCCCCCCCCCCCC		23.44-
306UbiquitinationFTDPSNNKSRFCLGL
CCCCCCCCCHHHHHH		47.46-
315PhosphorylationRFCLGLLSNVNRNST
HHHHHHHCCCCCCCC		43.7221712546
321PhosphorylationLSNVNRNSTIENTRR
HCCCCCCCCCHHHHH		27.7628348404
322PhosphorylationSNVNRNSTIENTRRH
CCCCCCCCCHHHHHH		35.5422985185
337PhosphorylationIGKGVHLYYVGGEVY
CCCCEEEEEECCEEE		4.9222468782
338PhosphorylationGKGVHLYYVGGEVYA
CCCEEEEEECCEEEE		10.0522468782
344PhosphorylationYYVGGEVYAECLSDS
EEECCEEEEHHCCCC		7.7422468782
418UbiquitinationTIRMSFVKGWGAEYH
CEEHHHHCCCCCCHH		47.1121890473
456PhosphorylationKVLTQMGSPLNPISS
HHHHHCCCCCCCCCC		22.3728555341
462PhosphorylationGSPLNPISSVS----
CCCCCCCCCCC----		26.4122322096
463PhosphorylationSPLNPISSVS-----
CCCCCCCCCC-----		27.4026503892
465PhosphorylationLNPISSVS-------
CCCCCCCC-------		36.1326503892
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
-KUbiquitinationE3 ubiquitin ligaseSMURF2Q9HAU4
PMID:20484049
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:12871975
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMAD5_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 SMAD5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUNX1_HUMANRUNX1physical
10531362
RUNX2_HUMANRUNX2physical
10531362
RUNX3_HUMANRUNX3physical
10531362
SMUF1_HUMANSMURF1physical
18641638
PKHO1_HUMANPLEKHO1physical
18641638
WWP1_HUMANWWP1physical
15221015
SMUF1_HUMANSMURF1physical
15221015
SMUF2_HUMANSMURF2physical
15221015
KAT2A_HUMANKAT2Aphysical
15009097
SKI_HUMANSKIphysical
14699069
HDAC1_HUMANHDAC1physical
14699069
CHIP_HUMANSTUB1physical
21454478
UBA1_HUMANUBA1physical
21900206
SF3B3_HUMANSF3B3physical
21900206
MEN1_HUMANMEN1physical
12649288
YAP1_HUMANYAP1physical
19914168
SMAD6_HUMANSMAD6physical
12857866
SMUF1_HUMANSMURF1physical
12857866
CSN5_HUMANCOPS5physical
17133595
HGS_HUMANHGSphysical
16516194
SMAD4_HUMANSMAD4physical
16516194
SMUF1_HUMANSMURF1physical
16516194
EP300_HUMANEP300physical
16516194
PAX6_HUMANPAX6physical
17251190
PSD11_HUMANPSMD11physical
15231748
SF3B1_HUMANSF3B1physical
15231748
RU17_HUMANSNRNP70physical
15231748
SNRPA_HUMANSNRPAphysical
15231748
SFPQ_HUMANSFPQphysical
15231748
U2AF2_HUMANU2AF2physical
15231748
SOX5_HUMANSOX5physical
15231748
NEDD4_HUMANNEDD4physical
15231748
BCAT1_HUMANBCAT1physical
15231748
PTN12_HUMANPTPN12physical
15231748
HBG2_HUMANHBG2physical
15231748
CXXC5_HUMANCXXC5physical
15231748
AN13A_HUMANANKRD13Aphysical
15231748
PPIL4_HUMANPPIL4physical
15231748
RYR2_HUMANRYR2physical
15231748
PNKP_HUMANPNKPphysical
15231748
SOX7_HUMANSOX7physical
15231748
RBM4_HUMANRBM4physical
15231748
WWP1_HUMANWWP1physical
15231748
SMUF1_HUMANSMURF1physical
15231748
MTMRA_HUMANMTMR10physical
15231748
CHMP3_HUMANCHMP3physical
15231748
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 SMAD5_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-462; SER-463 ANDSER-465, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 AND SER-465, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory