MEN1_HUMAN - dbPTM
MEN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MEN1_HUMAN
UniProt AC O00255
Protein Name Menin
Gene Name MEN1
Organism Homo sapiens (Human).
Sequence Length 615
Subcellular Localization Nucleus . Concentrated in nuclear body-like structures. Relocates to the nuclear matrix upon gamma irradiation.
Protein Description Essential component of a MLL/SET1 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3 (H3K4). Functions as a transcriptional regulator. Binds to the TERT promoter and represses telomerase expression. Plays a role in TGFB1-mediated inhibition of cell-proliferation, possibly regulating SMAD3 transcriptional activity. Represses JUND-mediated transcriptional activation on AP1 sites, as well as that mediated by NFKB subunit RELA. Positively regulates HOXC8 and HOXC6 gene expression. May be involved in normal hematopoiesis through the activation of HOXA9 expression (By similarity). May be involved in DNA repair..
Protein Sequence MGLKAAQKTLFPLRSIDDVVRLFAAELGREEPDLVLLSLVLGFVEHFLAVNRVIPTNVPELTFQPSPAPDPPGGLTYFPVADLSIIAALYARFTAQIRGAVDLSLYPREGGVSSRELVKKVSDVIWNSLSRSYFKDRAHIQSLFSFITGWSPVGTKLDSSGVAFAVVGACQALGLRDVHLALSEDHAWVVFGPNGEQTAEVTWHGKGNEDRRGQTVNAGVAERSWLYLKGSYMRCDRKMEVAFMVCAINPSIDLHTDSLELLQLQQKLLWLLYDLGHLERYPMALGNLADLEELEPTPGRPDPLTLYHKGIASAKTYYRDEHIYPYMYLAGYHCRNRNVREALQAWADTATVIQDYNYCREDEEIYKEFFEVANDVIPNLLKEAASLLEAGEERPGEQSQGTQSQGSALQDPECFAHLLRFYDGICKWEEGSPTPVLHVGWATFLVQSLGRFEGQVRQKVRIVSREAEAAEAEEPWGEEAREGRRRGPRRESKPEEPPPPKKPALDKGLGTGQGAVSGPPRKPPGTVAGTARGPEGGSTAQVPAPTASPPPEGPVLTFQSEKMKGMKELLVATKINSSAIKLQLTAQSQVQMKKQKVSTPSDYTLSFLKRQRKGL
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
8 (in isoform 2)Ubiquitination-42.33-
8UbiquitinationMGLKAAQKTLFPLRS
CCCHHHHHHHCCCCC		42.33-
120 (in isoform 2)Ubiquitination-39.22-
120UbiquitinationSSRELVKKVSDVIWN
CHHHHHHHHHHHHHH		39.22-
128PhosphorylationVSDVIWNSLSRSYFK
HHHHHHHHHCCHHHC		16.8427732954
130PhosphorylationDVIWNSLSRSYFKDR
HHHHHHHCCHHHCCH		20.9927732954
315UbiquitinationHKGIASAKTYYRDEH
ECCCCCCEEECCCCC		34.27-
386PhosphorylationNLLKEAASLLEAGEE
HHHHHHHHHHHHCCC		40.3028464451
399PhosphorylationEERPGEQSQGTQSQG
CCCCCCCCCCCCCCC		26.6917525332
402PhosphorylationPGEQSQGTQSQGSAL
CCCCCCCCCCCCCHH		19.8730108239
404PhosphorylationEQSQGTQSQGSALQD
CCCCCCCCCCCHHCC		36.0230108239
407PhosphorylationQGTQSQGSALQDPEC
CCCCCCCCHHCCHHH		20.4030108239
443PhosphorylationVLHVGWATFLVQSLG
EEEHHHHHHHHHHHC		15.82-
448PhosphorylationWATFLVQSLGRFEGQ
HHHHHHHHHCCCCCH		25.88-
492PhosphorylationRRGPRRESKPEEPPP
CCCCCCCCCCCCCCC		52.2625159151
502AcetylationEEPPPPKKPALDKGL
CCCCCCCCCCCCCCC		41.1025953088
511PhosphorylationALDKGLGTGQGAVSG
CCCCCCCCCCCCCCC		31.2328555341
526PhosphorylationPPRKPPGTVAGTARG
CCCCCCCCEEEEECC		16.9821888424
530PhosphorylationPPGTVAGTARGPEGG
CCCCEEEEECCCCCC		11.9321888424
546PhosphorylationTAQVPAPTASPPPEG
CCCCCCCCCCCCCCC		41.7028857561
548PhosphorylationQVPAPTASPPPEGPV
CCCCCCCCCCCCCCE		40.1819664995
560PhosphorylationGPVLTFQSEKMKGMK
CCEEEEECHHCCCCH		34.6919690332
588PhosphorylationKLQLTAQSQVQMKKQ
HHHHHHHHHHHHHHC		29.83-
598PhosphorylationQMKKQKVSTPSDYTL
HHHHCCCCCCCHHHH		41.4522199227
599PhosphorylationMKKQKVSTPSDYTLS
HHHCCCCCCCHHHHH		29.7825159151
601PhosphorylationKQKVSTPSDYTLSFL
HCCCCCCCHHHHHHH		43.2522199227
606PhosphorylationTPSDYTLSFLKRQRK
CCCHHHHHHHHHHHC		22.2624719451
609UbiquitinationDYTLSFLKRQRKGL-
HHHHHHHHHHHCCC-		44.46-
609MethylationDYTLSFLKRQRKGL-
HHHHHHHHHHHCCC-		44.4682980487
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
394SPhosphorylationKinaseATMQ13315
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MEN1_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 MEN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPRM_HUMANRPRMphysical
17353931
KMT2A_HUMANKMT2Aphysical
15199122
RBBP5_HUMANRBBP5physical
15199122
WDR5_HUMANWDR5physical
15199122
FACD2_HUMANFANCD2physical
12874027
JUND_HUMANJUNDphysical
9989505
GFAP_HUMANGFAPphysical
12169273
VIME_HUMANVIMphysical
12169273
KMT2A_HUMANKMT2Aphysical
20064463
CTNB1_HUMANCTNNB1physical
19074834
TFE2_HUMANTCF3physical
19074834
SNW1_HUMANSNW1physical
19818711
KMT2A_HUMANKMT2Aphysical
19818711
MYC_HUMANMYCphysical
19818711
H31_HUMANHIST1H3Aphysical
17050672
ASH2L_HUMANASH2Lphysical
17050672
RBBP5_HUMANRBBP5physical
17050672
RPB1_HUMANPOLR2Aphysical
17050672
FOXN3_HUMANFOXN3physical
16951149
HSP74_HUMANHSPA4physical
15254225
CHIP_HUMANSTUB1physical
15254225
PSIP1_HUMANPSIP1physical
18598942
SIN3A_HUMANSIN3Aphysical
14559791
HDAC1_HUMANHDAC1physical
14559791
HDAC2_HUMANHDAC2physical
14559791
HSP7C_HUMANHSPA8physical
15254225
JUND_HUMANJUNDphysical
10500243
WT1_HUMANWT1physical
21378168
CHK1_HUMANCHEK1physical
20969866
RPB2_HUMANPOLR2Bphysical
14992727
KMT2D_HUMANKMT2Dphysical
14992727
ASH2L_HUMANASH2Lphysical
14992727
RBBP5_HUMANRBBP5physical
14992727
WDR5_HUMANWDR5physical
14992727
H31T_HUMANHIST3H3physical
14992727
H2A2A_HUMANHIST2H2AA3physical
14992727
TAF1_HUMANTAF1physical
14992727
DBF4A_HUMANDBF4physical
15374998
MYH9_HUMANMYH9physical
14508515
IQGA1_HUMANIQGAP1physical
19079338
TF7L2_HUMANTCF7L2physical
19074834
FANCA_HUMANFANCAphysical
28215707
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
131100Familial multiple endocrine neoplasia type I (MEN1)
145000Familial isolated hyperparathyroidism (FIHP)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MEN1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND MASSSPECTROMETRY.
"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-548, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, AND MASSSPECTROMETRY.
"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 THR-599, AND MASSSPECTROMETRY.

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