MD2L1_HUMAN - dbPTM
MD2L1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MD2L1_HUMAN
UniProt AC Q13257
Protein Name Mitotic spindle assembly checkpoint protein MAD2A
Gene Name MAD2L1
Organism Homo sapiens (Human).
Sequence Length 205
Subcellular Localization Nucleus. Chromosome, centromere, kinetochore. Cytoplasm. Cytoplasm, cytoskeleton, spindle pole. Recruited by MAD1L1 to unattached kinetochores (Probable). Recruited to the nuclear pore complex by TPR during interphase. Recruited to kinetochores in la
Protein Description Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. Required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate..
Protein Sequence MALQLSREQGITLRGSAEIVAEFFSFGINSILYQRGIYPSETFTRVQKYGLTLLVTTDLELIKYLNNVVEQLKDWLYKCSVQKLVVVISNIESGEVLERWQFDIECDKTAKDDSAPREKSQKAIQDEIRSVIRQITATVTFLPLLEVSCSFDLLIYTDKDLVVPEKWEESGPQFITNSEEVRLRSFTTTIHKVNSMVAYKIPVND
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
2Acetylation------MALQLSREQ
------CCCCCCHHH		12.19-
6Phosphorylation--MALQLSREQGITL
--CCCCCCHHHCCCC		22.3220068231
77PhosphorylationEQLKDWLYKCSVQKL
HHHHHHHHHCCCCEE		12.99-
106S-nitrosocysteineRWQFDIECDKTAKDD
EEEEEEECCCCCCCC		7.12-
106S-nitrosylationRWQFDIECDKTAKDD
EEEEEEECCCCCCCC		7.1219483679
108AcetylationQFDIECDKTAKDDSA
EEEEECCCCCCCCCC		63.1423749302
108UbiquitinationQFDIECDKTAKDDSA
EEEEECCCCCCCCCC		63.14-
111UbiquitinationIECDKTAKDDSAPRE
EECCCCCCCCCCCHH		68.2633845483
119UbiquitinationDDSAPREKSQKAIQD
CCCCCHHHHHHHHHH		60.5122817900
122UbiquitinationAPREKSQKAIQDEIR
CCHHHHHHHHHHHHH		55.3221906983
129MethylationKAIQDEIRSVIRQIT
HHHHHHHHHHHHHHH		23.87115482475
130PhosphorylationAIQDEIRSVIRQITA
HHHHHHHHHHHHHHH		27.7923186163
166UbiquitinationKDLVVPEKWEESGPQ
CCCCCCCHHHHHCCC		54.5621906983
170PhosphorylationVPEKWEESGPQFITN
CCCHHHHHCCCCCCC		44.2322817900
178PhosphorylationGPQFITNSEEVRLRS
CCCCCCCCHHEEEEE		26.8722817900
185PhosphorylationSEEVRLRSFTTTIHK
CHHEEEEEEEEEEEC		31.3825159151
187PhosphorylationEVRLRSFTTTIHKVN
HEEEEEEEEEEECCC		25.03-
192UbiquitinationSFTTTIHKVNSMVAY
EEEEEEECCCCEEEE		38.9823000965
192AcetylationSFTTTIHKVNSMVAY
EEEEEEECCCCEEEE		38.9825953088
195PhosphorylationTTIHKVNSMVAYKIP
EEEECCCCEEEEECC		20.0223401153
199PhosphorylationKVNSMVAYKIPVND-
CCCCEEEEECCCCC-		9.6829978859
199NitrationKVNSMVAYKIPVND-
CCCCEEEEECCCCC-		9.68-
200UbiquitinationVNSMVAYKIPVND--
CCCEEEEECCCCC--		30.6921906983
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
185SPhosphorylationKinaseCHEK1O14757
GPS
187TPhosphorylationKinaseCHEK1O14757
GPS
-KUbiquitinationE3 ubiquitin ligaseSMURF2Q9HAU4
PMID:18852296
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MD2L1_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 MD2L1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ESR2_HUMANESR2physical
10706629
T22D4_HUMANTSC22D4physical
16189514
MD1L1_HUMANMAD1L1physical
16189514
MD1L1_HUMANMAD1L1physical
11707408
CDC20_HUMANCDC20physical
11707408
ADA17_HUMANADAM17physical
10527948
CDC20_HUMANCDC20physical
9736712
MD2BP_HUMANMAD2L1BPphysical
12456649
CDC20_HUMANCDC20physical
9637688
APC_HUMANAPCphysical
9637688
REV3L_HUMANREV3Lphysical
10660610
MD2L2_HUMANMAD2L2physical
10660610
MD1L1_HUMANMAD1L1physical
10660610
CDC20_HUMANCDC20physical
11274370
CDC20_HUMANCDC20physical
18592005
BUB1B_HUMANBUB1Bphysical
20512932
CDC20_HUMANCDC20physical
20512932
CDC16_HUMANCDC16physical
9356466
CDC27_HUMANCDC27physical
9356466
NSL1_HUMANNSL1physical
20231385
UBD_HUMANUBDphysical
16495226
CDC20_HUMANCDC20physical
14561775
CDC20_HUMANCDC20physical
11702782
MD1L1_HUMANMAD1L1physical
11459826
ANC2_HUMANANAPC2physical
11438673
MD2L1_HUMANMAD2L1physical
18022367
BUB1B_HUMANBUB1Bphysical
21525009
CDC20_HUMANCDC20physical
21525009
CDC27_HUMANCDC27physical
21525009
BUB3_HUMANBUB3physical
21525009
CDC20_HUMANCDC20physical
16497171
CDC20_HUMANCDC20physical
15694304
MD2L1_HUMANMAD2L1physical
15694304
MD1L1_HUMANMAD1L1physical
15694304
A4_HUMANAPPphysical
21832049
MD1L1_HUMANMAD1L1physical
21772247
CDC20_HUMANCDC20physical
21772247
MD2BP_HUMANMAD2L1BPphysical
21772247
MD2L1_HUMANMAD2L1physical
16525508
MD2BP_HUMANMAD2L1BPphysical
16525508
BUB1B_HUMANBUB1Bphysical
23754430
CDC20_HUMANCDC20physical
23754430
PRAF1_HUMANRABAC1physical
21988832
BUB1B_HUMANBUB1Bphysical
25012665
CDC20_HUMANCDC20physical
25012665
PCH2_HUMANTRIP13physical
25012665
SDCB1_HUMANSDCBPphysical
25416956
MD2BP_HUMANMAD2L1BPphysical
25416956
KEAP1_HUMANKEAP1physical
25416956
T22D4_HUMANTSC22D4physical
25416956
CDC27_HUMANCDC27physical
20054826
CDC20_HUMANCDC20physical
20054826
BASI_HUMANBSGphysical
26496610
PYR1_HUMANCADphysical
26496610
CDC20_HUMANCDC20physical
26496610
CDC27_HUMANCDC27physical
26496610
RAF1_HUMANRAF1physical
26496610
RS3A_HUMANRPS3Aphysical
26496610
S39A7_HUMANSLC39A7physical
26496610
MD1L1_HUMANMAD1L1physical
26496610
DYL1_HUMANDYNLL1physical
26496610
BCL7C_HUMANBCL7Cphysical
26496610
MD2BP_HUMANMAD2L1BPphysical
26496610
ABCF2_HUMANABCF2physical
26496610
KI20A_HUMANKIF20Aphysical
26496610
IPO7_HUMANIPO7physical
26496610
NUDT5_HUMANNUDT5physical
26496610
MACF1_HUMANMACF1physical
26496610
CHM2B_HUMANCHMP2Bphysical
26496610
TOIP1_HUMANTOR1AIP1physical
26496610
NEB1_HUMANPPP1R9Aphysical
26496610
WDR35_HUMANWDR35physical
26496610
APC1_HUMANANAPC1physical
26496610
TM10A_HUMANTRMT10Aphysical
26496610
TBB5_HUMANTUBBphysical
26496610
FILA2_HUMANFLG2physical
26496610
BUB1B_HUMANBUB1Bphysical
24151075
CDC20_HUMANCDC20physical
24151075
BUB3_HUMANBUB3physical
24151075
BUB3_HUMANBUB3physical
26986935
CDC20_HUMANCDC20physical
26986935
MD1L1_HUMANMAD1L1physical
26986935
APC7_HUMANANAPC7physical
26986935
BUB1B_HUMANBUB1Bphysical
26986935
PSMD8_HUMANPSMD8physical
26986935
APC1_HUMANANAPC1physical
26986935
CDC27_HUMANCDC27physical
26986935
KI20A_HUMANKIF20Aphysical
26986935
PCH2_HUMANTRIP13physical
26986935
H31_HUMANHIST1H3Aphysical
27198228
CDC20_HUMANCDC20physical
18318601
MD2L1_HUMANMAD2L1physical
18318601
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 MD2L1_HUMAN

loading...

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-195, AND MASSSPECTROMETRY.
"Mad2 phosphorylation regulates its association with Mad1 and theAPC/C.";
Wassmann K., Liberal V., Benezra R.;
EMBO J. 22:797-806(2003).
Cited for: PHOSPHORYLATION AT SER-170; SER-178 AND SER-195, INTERACTION WITHMAD1L1 AND CDC20, AND MUTAGENESIS OF SER-170; SER-178 AND SER-195.

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