MD2BP_HUMAN - dbPTM
MD2BP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MD2BP_HUMAN
UniProt AC Q15013
Protein Name MAD2L1-binding protein
Gene Name MAD2L1BP
Organism Homo sapiens (Human).
Sequence Length 274
Subcellular Localization Nucleus. Cytoplasm, cytoskeleton, spindle. During early mitosis, unevenly distributed throughout the nucleoplasm. From metaphase to anaphase, concentrated on the spindle.
Protein Description May function to silence the spindle checkpoint and allow mitosis to proceed through anaphase by binding MAD2L1 after it has become dissociated from the MAD2L1-CDC20 complex..
Protein Sequence MAAPEAEVLSSAAVPDLEWYEKSEETHASQIELLETSSTQEPLNASEAFCPRDCMVPVVFPGPVSQEGCCQFTCELLKHIMYQRQQLPLPYEQLKHFYRKPSPQAEEMLKKKPRATTEVSSRKCQQALAELESVLSHLEDFFARTLVPRVLILLGGNALSPKEFYELDLSLLAPYSVDQSLSTAACLRRLFRAIFMADAFSELQAPPLMGTVVMAQGHRNCGEDWFRPKLNYRVPSRGHKLTVTLSCGRPSIRTTAWEDYIWFQAPVTFKGFRE
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
13 (in isoform 3)Phosphorylation-18.47-
13PhosphorylationAEVLSSAAVPDLEWY
HHHHHCCCCCCCCHH		18.47-
23PhosphorylationDLEWYEKSEETHASQ
CCCHHHHCCHHCHHH		28.8222067460
29PhosphorylationKSEETHASQIELLET
HCCHHCHHHEEEEHH		24.8817525332
36PhosphorylationSQIELLETSSTQEPL
HHEEEEHHCCCCCCC		28.1329978859
37PhosphorylationQIELLETSSTQEPLN
HEEEEHHCCCCCCCC		23.2418669648
38PhosphorylationIELLETSSTQEPLNA
EEEEHHCCCCCCCCH		41.3429978859
39PhosphorylationELLETSSTQEPLNAS
EEEHHCCCCCCCCHH		36.4017525332
46PhosphorylationTQEPLNASEAFCPRD
CCCCCCHHHCCCCCC		28.5229978859
61PhosphorylationCMVPVVFPGPVSQEG
CEEEEEECCCCCCCC		34.27-
69PhosphorylationGPVSQEGCCQFTCEL
CCCCCCCHHHHHHHH		1.30-
71PhosphorylationVSQEGCCQFTCELLK
CCCCCHHHHHHHHHH		40.54-
78UbiquitinationQFTCELLKHIMYQRQ
HHHHHHHHHHHHHHC		43.6529967540
91PhosphorylationRQQLPLPYEQLKHFY
HCCCCCCHHHHHHHH		24.8018083107
95UbiquitinationPLPYEQLKHFYRKPS
CCCHHHHHHHHHCCC		31.2223000965
98PhosphorylationYEQLKHFYRKPSPQA
HHHHHHHHHCCCHHH		19.9018083107
100UbiquitinationQLKHFYRKPSPQAEE
HHHHHHHCCCHHHHH		38.1723000965
102PhosphorylationKHFYRKPSPQAEEML
HHHHHCCCHHHHHHH		32.4523401153
110 (in isoform 1)Ubiquitination-58.4021906983
110UbiquitinationPQAEEMLKKKPRATT
HHHHHHHHHCCCCCH		58.4027667366
127UbiquitinationSSRKCQQALAELESV
CHHHHHHHHHHHHHH		5.2621890473
132UbiquitinationQQALAELESVLSHLE
HHHHHHHHHHHHHHH		30.2423000965
134PhosphorylationALAELESVLSHLEDF
HHHHHHHHHHHHHHH		4.6724719451
142UbiquitinationLSHLEDFFARTLVPR
HHHHHHHHHHHHHCH		7.5121963094
160PhosphorylationLLGGNALSPKEFYEL
EECCCCCCHHHHHHC		31.3624719451
201PhosphorylationIFMADAFSELQAPPL
HHHHHHHHHCCCCCC		38.8328555341
229UbiquitinationGEDWFRPKLNYRVPS
CCCCCCCCCCEECCC		45.14-
232PhosphorylationWFRPKLNYRVPSRGH
CCCCCCCEECCCCCC		24.35-
246PhosphorylationHKLTVTLSCGRPSIR
CEEEEEEECCCCCCC		12.74-
251PhosphorylationTLSCGRPSIRTTAWE
EEECCCCCCCCEECC		24.28-
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

Oops, there are no upstream regulatory protein records of MD2BP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MD2BP_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 MD2BP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCH2_HUMANTRIP13physical
16169070
CE126_HUMANKIAA1377physical
16169070
IGS21_HUMANIGSF21physical
16169070
LRIF1_HUMANLRIF1physical
16169070
EF1A1_HUMANEEF1A1physical
16169070
KAT5_HUMANKAT5physical
16169070
PTN_HUMANPTNphysical
16169070
SETB1_HUMANSETDB1physical
16169070
P53_HUMANTP53physical
16169070
CDC20_HUMANCDC20physical
22566641
MD1L1_HUMANMAD1L1physical
22100920
MD2BP_HUMANMAD2L1BPphysical
22100920
CDC20_HUMANCDC20physical
22100920
MD2L1_HUMANMAD2L1physical
22100920
BUB1B_HUMANBUB1Bphysical
22100920
SEP11_HUMANSEPT11physical
22939629
PCH2_HUMANTRIP13physical
19060904
INP5K_HUMANINPP5Kphysical
25416956
HOMEZ_HUMANHOMEZphysical
25416956
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 MD2BP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-29 AND THR-39, AND MASSSPECTROMETRY.

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