MND1_HUMAN - dbPTM
MND1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MND1_HUMAN
UniProt AC Q9BWT6
Protein Name Meiotic nuclear division protein 1 homolog
Gene Name MND1 {ECO:0000312|EMBL:EAX04964.1}
Organism Homo sapiens (Human).
Sequence Length 205
Subcellular Localization Nucleus .
Protein Description Required for proper homologous chromosome pairing and efficient cross-over and intragenic recombination during meiosis (By similarity). Stimulates both DMC1- and RAD51-mediated homologous strand assimilation, which is required for the resolution of meiotic double-strand breaks..
Protein Sequence MSKKKGLSAEEKRTRMMEIFSETKDVFQLKDLEKIAPKEKGITAMSVKEVLQSLVDDGMVDCERIGTSNYYWAFPSKALHARKHKLEVLESQLSEGSQKHASLQKSIEKAKIGRCETEERTRLAKELSSLRDQREQLKAEVEKYKDCDPQVVEEIRQANKVAKEAANRWTDNIFAIKSWAKRKFGFEENKIDRTFGIPEDFDYID
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------MSKKKGLSA
------CCCCCCCCH
53.8622814378
14PhosphorylationLSAEEKRTRMMEIFS
CCHHHHHHHHHHHHH
33.7029759185
30UbiquitinationTKDVFQLKDLEKIAP
CCCCHHHCCHHHHCC
49.8621890473
46PhosphorylationEKGITAMSVKEVLQS
CCCCCCCCHHHHHHH
27.8124719451
67PhosphorylationVDCERIGTSNYYWAF
EEHHHCCCCCCEEEC
16.0728796482
68PhosphorylationDCERIGTSNYYWAFP
EHHHCCCCCCEEECC
20.0228796482
70PhosphorylationERIGTSNYYWAFPSK
HHCCCCCCEEECCHH
10.5128796482
71PhosphorylationRIGTSNYYWAFPSKA
HCCCCCCEEECCHHH
8.4328796482
77UbiquitinationYYWAFPSKALHARKH
CEEECCHHHHHHHHH
56.03-
77AcetylationYYWAFPSKALHARKH
CEEECCHHHHHHHHH
56.0326051181
102PhosphorylationEGSQKHASLQKSIEK
HHHHHHHHHHHHHHH
30.9326270265
105UbiquitinationQKHASLQKSIEKAKI
HHHHHHHHHHHHHHC
59.71-
106PhosphorylationKHASLQKSIEKAKIG
HHHHHHHHHHHHHCC
24.0226270265
121O-linked_GlycosylationRCETEERTRLAKELS
CCCHHHHHHHHHHHH
33.0630379171
125UbiquitinationEERTRLAKELSSLRD
HHHHHHHHHHHHHHH
64.87-
128PhosphorylationTRLAKELSSLRDQRE
HHHHHHHHHHHHHHH
28.5530301811
129PhosphorylationRLAKELSSLRDQREQ
HHHHHHHHHHHHHHH
39.8025954137
138UbiquitinationRDQREQLKAEVEKYK
HHHHHHHHHHHHHHC
42.04-
145AcetylationKAEVEKYKDCDPQVV
HHHHHHHCCCCHHHH
64.0526051181
177UbiquitinationTDNIFAIKSWAKRKF
HHCCHHHHHHHHHHH
36.19-
190UbiquitinationKFGFEENKIDRTFGI
HHCCCCCCCCCCCCC
49.62-
203PhosphorylationGIPEDFDYID-----
CCCCCCCCCC-----
13.64-

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 MND1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MND1_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 MND1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
HOP2_HUMANPSMC3IPphysical
26344197
RED_HUMANIKphysical
26496610
HOP2_HUMANPSMC3IPphysical
26496610
HOP2_HUMANPSMC3IPphysical
28514442
MTEF4_HUMANMTERF4physical
28514442
NSUN4_HUMANNSUN4physical
28514442
JIP4_HUMANSPAG9physical
28514442

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MND1_HUMAN

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Related Literatures of Post-Translational Modification

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