SMAD7_HUMAN - dbPTM
SMAD7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMAD7_HUMAN
UniProt AC O15105
Protein Name Mothers against decapentaplegic homolog 7
Gene Name SMAD7
Organism Homo sapiens (Human).
Sequence Length 426
Subcellular Localization Nucleus . Cytoplasm . Interaction with NEDD4L or RNF111 induces translocation from the nucleus to the cytoplasm (PubMed:16601693). TGF-beta stimulates its translocation from the nucleus to the cytoplasm. PDPK1 inhibits its translocation from the nucl
Protein Description Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access. Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator..
Protein Sequence MFRTKRSALVRRLWRSRAPGGEDEEEGAGGGGGGGELRGEGATDSRAHGAGGGGPGRAGCCLGKAVRGAKGHHHPHPPAAGAGAAGGAEADLKALTHSVLKKLKERQLELLLQAVESRGGTRTACLLLPGRLDCRLGPGAPAGAQPAQPPSSYSLPLLLCKVFRWPDLRHSSEVKRLCCCESYGKINPELVCCNPHHLSRLCELESPPPPYSRYPMDFLKPTADCPDAVPSSAETGGTNYLAPGGLSDSQLLLEPGDRSHWCVVAYWEEKTRVGRLYCVQEPSLDIFYDLPQGNGFCLGQLNSDNKSQLVQKVRSKIGCGIQLTREVDGVWVYNRSSYPIFIKSATLDNPDSRTLLVHKVFPGFSIKAFDYEKAYSLQRPNDHEFMQQPWTGFTVQISFVKGWGQCYTRQFISSCPCWLEVIFNSR
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
64AcetylationRAGCCLGKAVRGAKG
CCHHHHHHHHHCCCC		30.6612408818
64UbiquitinationRAGCCLGKAVRGAKG
CCHHHHHHHHHCCCC		30.6612408818
70MethylationGKAVRGAKGHHHPHP
HHHHHCCCCCCCCCC		62.6912408818
70AcetylationGKAVRGAKGHHHPHP
HHHHHCCCCCCCCCC		62.6912408818
70UbiquitinationGKAVRGAKGHHHPHP
HHHHHCCCCCCCCCC		62.6912408818
96PhosphorylationEADLKALTHSVLKKL
HHHHHHHHHHHHHHH		19.5722817900
101UbiquitinationALTHSVLKKLKERQL
HHHHHHHHHHHHHHH		54.63-
117PhosphorylationLLLQAVESRGGTRTA
HHHHHHHHCCCCEEE		29.62-
121PhosphorylationAVESRGGTRTACLLL
HHHHCCCCEEEEEEE		27.89-
206PhosphorylationSRLCELESPPPPYSR
HHHHHCCCCCCCCCC		56.16-
249PhosphorylationAPGGLSDSQLLLEPG
CCCCCCCCCEEECCC		21.25-
354PhosphorylationLDNPDSRTLLVHKVF
CCCCCCCEEEEEEEC		28.53-
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
96TPhosphorylationKinaseMELKQ61846
PSP
-KUbiquitinationE3 ubiquitin ligaseWWP2O00308
PMID:21258410
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:11278251
-KUbiquitinationE3 ubiquitin ligaseRNF111Q6ZNA4
PMID:14657019
-KUbiquitinationE3 ubiquitin ligaseSMURF2Q9HAU4
PMID:11163210
-KUbiquitinationE3 ubiquitin ligaseWWP1Q9H0M0
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseITCHQ96J02
PMID:15946939
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
249SPhosphorylation

17327236
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 SMAD7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WWP2_MOUSEWwp2physical
15761153
BMR1A_HUMANBMPR1Aphysical
15148321
TGFR1_HUMANTGFBR1physical
15148321
CTNB1_HUMANCTNNB1physical
15684397
LEF1_HUMANLEF1physical
15684397
SMUF2_HUMANSMURF2physical
14722617
SMUF1_HUMANSMURF1physical
14722617
RN111_HUMANRNF111physical
14657019
DVL1_HUMANDVL1physical
12650946
ERBIN_HUMANERBB2IPphysical
12650946
MP2K3_HUMANMAP2K3physical
12589052
MP2K6_HUMANMAP2K6physical
12589052
M3K7_HUMANMAP3K7physical
12589052
TAB1_HUMANTAB1physical
12589052
EP300_HUMANEP300physical
12408818
TGFR1_HUMANTGFBR1physical
11163210
TGFR2_HUMANTGFBR2physical
11163210
TGFR1_HUMANTGFBR1physical
9215638
AKT1_HUMANAKT1physical
16362038
TAB1_HUMANTAB1physical
11737269
STRAP_HUMANSTRAPphysical
10757800
TGFR1_HUMANTGFBR1physical
10757800
SMAD3_HUMANSMAD3genetic
10757800
YAP1_HUMANYAP1physical
12118366
SMAD6_HUMANSMAD6physical
9256479
FKB1A_HUMANFKBP1Aphysical
16720724
ACV1B_HUMANACVR1Bphysical
16720724
SMUF1_HUMANSMURF1physical
16720724
KAT2B_HUMANKAT2Bphysical
16285943
UCHL5_HUMANUCHL5physical
16027725
TGFR1_HUMANTGFBR1physical
16027725
ITCH_HUMANITCHphysical
15946939
TGFR1_HUMANTGFBR1physical
15946939
HDAC1_HUMANHDAC1physical
15831498
SMAD4_HUMANSMAD4physical
15817471
NEDD4_HUMANNEDD4physical
15496141
SRF_HUMANSRFphysical
16690609
WWP1_HUMANWWP1physical
15221015
SMUF1_HUMANSMURF1physical
15221015
SMUF2_HUMANSMURF2physical
15221015
SMUF1_HUMANSMURF1physical
11278251
SIR1_HUMANSIRT1physical
17098745
ZEB1_HUMANZEB1physical
20514018
T22D1_HUMANTSC22D1physical
21791611
WWP2_HUMANWWP2physical
21258410
SMUF2_HUMANSMURF2physical
22624557
TGFR1_HUMANTGFBR1physical
22624557
WWP1_HUMANWWP1physical
15359284
TGFR1_HUMANTGFBR1physical
15359284
ITCH_HUMANITCHphysical
22773947
NEDD4_HUMANNEDD4physical
22773947
NED4L_HUMANNEDD4Lphysical
22773947
SMUF1_HUMANSMURF1physical
22773947
SMUF2_HUMANSMURF2physical
22773947
WWP1_HUMANWWP1physical
22773947
WWP2_HUMANWWP2physical
22773947
UBP11_HUMANUSP11physical
22773947
UBP15_HUMANUSP15physical
22344298
SMUF1_HUMANSMURF1physical
12151385
SMUF1_HUMANSMURF1physical
22921829
NED4L_HUMANNEDD4Lphysical
22921829
SMUF2_HUMANSMURF2physical
22921829
YAP1_HUMANYAP1physical
22921829
CSN5_HUMANCOPS5physical
14993265
TAB2_HUMANTAB2physical
17384642
TAB3_HUMANTAB3physical
17384642
TOLIP_HUMANTOLLIPphysical
23027871
TGFR1_HUMANTGFBR1physical
23027871
TGFR1_HUMANTGFBR1physical
9335507
TGFR2_HUMANTGFBR2physical
9335507
P53_HUMANTP53physical
17172861
TGFI1_HUMANTGFB1I1physical
18762808
PR15A_HUMANPPP1R15Aphysical
14718519
BAMBI_HUMANBAMBIphysical
19758997
CTNB1_HUMANCTNNB1physical
18593713
CADH1_HUMANCDH1physical
18593713
AXIN1_HUMANAXIN1physical
18593713
BMPR2_HUMANBMPR2physical
20663871
ACVR1_HUMANACVR1physical
20663871
BMR1A_HUMANBMPR1Aphysical
20663871
ACV1B_HUMANACVR1Bphysical
20663871
TGFR1_HUMANTGFBR1physical
20663871
AVR2B_HUMANACVR2Bphysical
20663871
UBE2O_HUMANUBE2Ophysical
23455153
PIAS1_HUMANPIAS1physical
15231748
ZBT11_HUMANZBTB11physical
15231748
XRCC6_HUMANXRCC6physical
15231748
MYOD1_HUMANMYOD1physical
15231748
SOX5_HUMANSOX5physical
15231748
TTF1_HUMANTTF1physical
15231748
CXXC5_HUMANCXXC5physical
15231748
PIAS4_HUMANPIAS4physical
15231748
SOX7_HUMANSOX7physical
15231748
HEYL_HUMANHEYLphysical
15231748
ASH1L_HUMANASH1Lphysical
15231748
ZN107_HUMANZNF107physical
15231748
MKL2_HUMANMKL2physical
15231748
SOX13_HUMANSOX13physical
15231748
TTF2_HUMANTTF2physical
15231748
KDM2A_HUMANKDM2Aphysical
15231748
SMUF1_HUMANSMURF1physical
23959799
MYC_HUMANMYCphysical
24259667
SKP2_HUMANSKP2physical
24259667
SMUF2_HUMANSMURF2physical
23973329
UBP11_HUMANUSP11physical
24850914
LEF1_HUMANLEF1physical
15750622
CBL_HUMANCBLphysical
26055326
TF7L2_HUMANTCF7L2physical
15684397
PARD3_HUMANPARD3physical
12650946
TGFR1_HUMANTGFBR1physical
12151385
NR4A1_HUMANNR4A1physical
24584437
SMUF2_HUMANSMURF2physical
26679521
RN111_HUMANRNF111physical
27292644
SMUF1_HUMANSMURF1physical
27292644
SMUF2_HUMANSMURF2physical
27292644
AXIN2_HUMANAXIN2physical
27292644
ITCH_HUMANITCHphysical
28400336
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612229Colorectal cancer 3 (CRCS3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMAD7_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Control of Smad7 stability by competition between acetylation andubiquitination.";
Gronroos E., Hellman U., Heldin C.H., Ericsson J.;
Mol. Cell 10:483-493(2002).
Cited for: INTERACTION WITH EP300, ACETYLATION AT LYS-64 AND LYS-70,UBIQUITINATION AT LYS-64 AND LYS-70, AND MUTAGENESIS OF LYS-64 ANDLYS-70.
Ubiquitylation
ReferencePubMed
"Control of Smad7 stability by competition between acetylation andubiquitination.";
Gronroos E., Hellman U., Heldin C.H., Ericsson J.;
Mol. Cell 10:483-493(2002).
Cited for: INTERACTION WITH EP300, ACETYLATION AT LYS-64 AND LYS-70,UBIQUITINATION AT LYS-64 AND LYS-70, AND MUTAGENESIS OF LYS-64 ANDLYS-70.

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