MINY3_HUMAN - dbPTM
MINY3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MINY3_HUMAN
UniProt AC Q9H8M7
Protein Name Ubiquitin carboxyl-terminal hydrolase MINDY-3
Gene Name MINDY3 {ECO:0000312|HGNC:HGNC:23578}
Organism Homo sapiens (Human).
Sequence Length 445
Subcellular Localization Nucleus .
Protein Description Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins..
Protein Sequence MSELTKELMELVWGTKSSPGLSDTIFCRWTQGFVFSESEGSALEQFEGGPCAVIAPVQAFLLKKLLFSSEKSSWRDCSEEEQKELLCHTLCDILESACCDHSGSYCLVSWLRGKTTEETASISGSPAESSCQVEHSSALAVEELGFERFHALIQKRSFRSLPELKDAVLDQYSMWGNKFGVLLFLYSVLLTKGIENIKNEIEDASEPLIDPVYGHGSQSLINLLLTGHAVSNVWDGDRECSGMKLLGIHEQAAVGFLTLMEALRYCKVGSYLKSPKFPIWIVGSETHLTVFFAKDMALVAPEAPSEQARRVFQTYDPEDNGFIPDSLLEDVMKALDLVSDPEYINLMKNKLDPEGLGIILLGPFLQEFFPDQGSSGPESFTVYHYNGLKQSNYNEKVMYVEGTAVVMGFEDPMLQTDDTPIKRCLQTKWPYIELLWTTDRSPSLN
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
16UbiquitinationMELVWGTKSSPGLSD
HHHHHCCCCCCCCCC
21963094
17PhosphorylationELVWGTKSSPGLSDT
HHHHCCCCCCCCCCC
25159151
18PhosphorylationLVWGTKSSPGLSDTI
HHHCCCCCCCCCCCE
25159151
63UbiquitinationPVQAFLLKKLLFSSE
HHHHHHHHHHHHCCC
22817900
64UbiquitinationVQAFLLKKLLFSSEK
HHHHHHHHHHHCCCC
21906983
64 (in isoform 2)Ubiquitination-21890473
64 (in isoform 1)Ubiquitination-21890473
71 (in isoform 2)Ubiquitination-21890473
71 (in isoform 1)Ubiquitination-21890473
71UbiquitinationKLLFSSEKSSWRDCS
HHHHCCCCCCCCCCC
23000965
94UbiquitinationCHTLCDILESACCDH
HHHHHHHHHHHHCCC
21890473
114 (in isoform 2)Ubiquitination--
114UbiquitinationLVSWLRGKTTEETAS
EEEECCCCCCCCEEC
29967540
119PhosphorylationRGKTTEETASISGSP
CCCCCCCEECCCCCC
27080861
120UbiquitinationGKTTEETASISGSPA
CCCCCCEECCCCCCC
21890473
123PhosphorylationTEETASISGSPAESS
CCCEECCCCCCCCCC
27080861
125PhosphorylationETASISGSPAESSCQ
CEECCCCCCCCCCCE
25159151
155UbiquitinationRFHALIQKRSFRSLP
HHHHHHHHCCCCCCH
29967540
175UbiquitinationVLDQYSMWGNKFGVL
HHHHHHCCCHHHHHH
29967540
222UbiquitinationHGSQSLINLLLTGHA
CCHHHHHHHHHHCCC
22817900
241PhosphorylationWDGDRECSGMKLLGI
CCCCCCCCCCEEEEE
-
249UbiquitinationGMKLLGIHEQAAVGF
CCEEEEEHHHHHHHH
22817900
267 (in isoform 1)Ubiquitination-21890473
267UbiquitinationMEALRYCKVGSYLKS
HHHHHHCCHHHHCCC
21890473
270PhosphorylationLRYCKVGSYLKSPKF
HHHCCHHHHCCCCCC
-
274PhosphorylationKVGSYLKSPKFPIWI
CHHHHCCCCCCCEEE
24719451
275UbiquitinationVGSYLKSPKFPIWIV
HHHHCCCCCCCEEEE
22817900
296SulfoxidationTVFFAKDMALVAPEA
EEEEECCCCHHCCCC
21406390
348UbiquitinationPEYINLMKNKLDPEG
HHHHHHHCCCCCHHC
29967540
395UbiquitinationLKQSNYNEKVMYVEG
CCCCCCCCCEEEEEC
22817900
399PhosphorylationNYNEKVMYVEGTAVV
CCCCCEEEEECCEEE
24719451
422 (in isoform 1)Ubiquitination-21890473
422UbiquitinationQTDDTPIKRCLQTKW
CCCCCCHHHHHHCCC
21906983

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
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MINY3_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 MINY3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBB_HUMANUBBphysical
26186194
RNF25_HUMANRNF25physical
26186194
LIN7A_HUMANLIN7Aphysical
26186194
MPP6_HUMANMPP6physical
26186194
MCM3_HUMANMCM3physical
26186194
MCM5_HUMANMCM5physical
26186194
PKP2_HUMANPKP2physical
26186194
KIFC1_HUMANKIFC1physical
26186194
ZN644_HUMANZNF644physical
26186194
RUSD3_HUMANRPUSD3physical
26186194
LANC2_HUMANLANCL2physical
26186194
HNRLL_HUMANHNRNPLLphysical
26186194
CSK_HUMANCSKphysical
26186194
SCAF8_HUMANSCAF8physical
26186194
CAF17_HUMANIBA57physical
26186194
NIPA_HUMANZC3HC1physical
26186194
HNRLL_HUMANHNRNPLLphysical
28514442
UBB_HUMANUBBphysical
28514442
KIFC1_HUMANKIFC1physical
28514442
SCAF8_HUMANSCAF8physical
28514442
RNF25_HUMANRNF25physical
28514442
LANC2_HUMANLANCL2physical
28514442
ZN644_HUMANZNF644physical
28514442
MPP6_HUMANMPP6physical
28514442
RUSD3_HUMANRPUSD3physical
28514442
PKP2_HUMANPKP2physical
28514442
MCM3_HUMANMCM3physical
28514442
NTH_HUMANNTHL1physical
28514442
BACD3_HUMANKCTD10physical
28514442
NIPA_HUMANZC3HC1physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MINY3_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP