SIMC1_HUMAN - dbPTM
SIMC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SIMC1_HUMAN
UniProt AC Q8NDZ2
Protein Name SUMO-interacting motif-containing protein 1
Gene Name SIMC1
Organism Homo sapiens (Human).
Sequence Length 872
Subcellular Localization
Protein Description
Protein Sequence MAPASASGEDLRKLPTMAEVNGEQDFIDLTRETRPRTKDRSGLYVIDLTRAEGENRPIATLDLTLEPVTPSQKEPTSLQTCASLSGKAVMEGHVDRSSQPTARRIINSDPVDLDLVEENTFVGPPPATSISGGSVYPTEPNCSSATFTGNLSFLASLQLSSDVSSLSPTSNNSRSSSSSSNQKAPLPCPQQDVSRPPQALPCPLRPLPCPPRASPCPPRASSCPPRALSCPSQTMQCQLPALTHPPQEVPCPRQNIPGPPQDSLGLPQDVPGLPQSILHPQDVAYLQDMPRSPGDVPQSPSDVSPSPDAPQSPGGMPHLPGDVLHSPGDMPHSSGDVTHSPRDIPHLPGDRPDFTQNDVQNRDMPMDISALSSPSCSPSPQSETPLEKVPWLSVMETPARKEISLSEPAKPGSAHVQSRTPQGGLYNRPCLHRLKYFLRPPVHHLFFQTLIPDKDTRENKGQKLEPIPHRRLRMVTNTIEENFPLGTVQFLMDFVSPQHYPPREIVAHIIQKILLSGSETVDVLKEAYMLLMKIQQLHPANAKTVEWDWKLLTYVMEEEGQTLPGRVLFLRYVVQTLEDDFQQTLRRQRQHLQQSIANMVLSCDKQPHNVRDVIKWLVKAVTEDGLTQPPNGNQTSSGTGILKASSSHPSSQPNLTKNTNQLIVCQLQRMLSIAVEVDRTPTCSSNKIAEMMFGFVLDIPERSQREMFFTTMESHLLRCKVLEIIFLHSCETPTRLPLSLAQALYFLNNSTSLLKCQSDKSQWQTWDELVEHLQFLLSSYQHVLREHLRSSVIDRKDLIIKRIKPKPQQGDDITVVDVEKQIEAFRSRLIQMLGEPLVPQLQDKVHLLKLLLFYAADLNPDAEPFQKGWSGS
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
7O-linked_Glycosylation-MAPASASGEDLRKL
-CCCCCCCHHHHHCC
30379171
8PhosphorylationMAPASASGEDLRKLP
CCCCCCCHHHHHCCC
28450419
8 (in isoform 3)Phosphorylation-28450419
11PhosphorylationASASGEDLRKLPTMA
CCCCHHHHHCCCCCE
28450419
11 (in isoform 3)Phosphorylation-28450419
13PhosphorylationASGEDLRKLPTMAEV
CCHHHHHCCCCCEEE
20363803
13 (in isoform 3)Phosphorylation-20363803
15PhosphorylationGEDLRKLPTMAEVNG
HHHHHCCCCCEEECC
28450419
15 (in isoform 3)Phosphorylation-28450419
16 (in isoform 3)Phosphorylation-30177828
16PhosphorylationEDLRKLPTMAEVNGE
HHHHCCCCCEEECCC
30177828
30PhosphorylationEQDFIDLTRETRPRT
CCCCHHCCCCCCCCC
22210691
34 (in isoform 3)Phosphorylation-23684312
34PhosphorylationIDLTRETRPRTKDRS
HHCCCCCCCCCCCCC
23684312
35 (in isoform 3)Phosphorylation-23684312
35PhosphorylationDLTRETRPRTKDRSG
HCCCCCCCCCCCCCC
23684312
44PhosphorylationTKDRSGLYVIDLTRA
CCCCCCEEEEECEEC
29496907
76 (in isoform 4)Ubiquitination-21890473
80 (in isoform 4)Ubiquitination-21890473
104 (in isoform 4)Ubiquitination-21890473
128 (in isoform 3)Ubiquitination-21890473
175PhosphorylationPTSNNSRSSSSSSNQ
CCCCCCCCCCCCCCC
29052541
176PhosphorylationTSNNSRSSSSSSNQK
CCCCCCCCCCCCCCC
29052541
177PhosphorylationSNNSRSSSSSSNQKA
CCCCCCCCCCCCCCC
29052541
178PhosphorylationNNSRSSSSSSNQKAP
CCCCCCCCCCCCCCC
29052541
179PhosphorylationNSRSSSSSSNQKAPL
CCCCCCCCCCCCCCC
29052541
180PhosphorylationSRSSSSSSNQKAPLP
CCCCCCCCCCCCCCC
29052541
200 (in isoform 3)Ubiquitination-21890473
204 (in isoform 3)Ubiquitination-21890473
214PhosphorylationLPCPPRASPCPPRAS
CCCCCCCCCCCCCHH
28985074
228 (in isoform 3)Ubiquitination-21890473
305 (in isoform 4)Ubiquitination-21890473
312PhosphorylationPSPDAPQSPGGMPHL
CCCCCCCCCCCCCCC
26074081
328 (in isoform 4)Ubiquitination-21890473
401UbiquitinationVMETPARKEISLSEP
EECCCCCCEECCCCC
-
410UbiquitinationISLSEPAKPGSAHVQ
ECCCCCCCCCCCCCC
-
420PhosphorylationSAHVQSRTPQGGLYN
CCCCCCCCCCCCCCC
28985074
426PhosphorylationRTPQGGLYNRPCLHR
CCCCCCCCCCHHHHH
29496907
429 (in isoform 3)Ubiquitination-21890473
452 (in isoform 3)Ubiquitination-21890473
463UbiquitinationTRENKGQKLEPIPHR
CCCCCCCCCCCCCHH
-
520PhosphorylationILLSGSETVDVLKEA
HHHCCCCHHHHHHHH
-
528PhosphorylationVDVLKEAYMLLMKIQ
HHHHHHHHHHHHHHH
27762562
543UbiquitinationQLHPANAKTVEWDWK
HHCCCCCCCEEEHHH
21890473
543 (in isoform 1)Ubiquitination-21890473
550AcetylationKTVEWDWKLLTYVME
CCEEEHHHHHHHHHH
20167786
553PhosphorylationEWDWKLLTYVMEEEG
EEHHHHHHHHHHHCC
-
584PhosphorylationLEDDFQQTLRRQRQH
HHHHHHHHHHHHHHH
-
605UbiquitinationNMVLSCDKQPHNVRD
HHHHHCCCCCCCHHH
-
615UbiquitinationHNVRDVIKWLVKAVT
CCHHHHHHHHHHHHC
21890473
615 (in isoform 1)Ubiquitination-21890473
619UbiquitinationDVIKWLVKAVTEDGL
HHHHHHHHHHCCCCC
21906983
619 (in isoform 1)Ubiquitination-21890473
643UbiquitinationSSGTGILKASSSHPS
CCCCCEEECCCCCCC
21906983
643 (in isoform 1)Ubiquitination-21890473
647PhosphorylationGILKASSSHPSSQPN
CEEECCCCCCCCCCC
-
651PhosphorylationASSSHPSSQPNLTKN
CCCCCCCCCCCCCCC
17525332
657UbiquitinationSSQPNLTKNTNQLIV
CCCCCCCCCCCHHHH
-
752PhosphorylationYFLNNSTSLLKCQSD
HHHHCCCCHHCCCCC
24719451
791PhosphorylationLREHLRSSVIDRKDL
HHHHHHHHCCCCHHH
14729942
804UbiquitinationDLIIKRIKPKPQQGD
HHEEEECCCCCCCCC
-
806UbiquitinationIIKRIKPKPQQGDDI
EEEECCCCCCCCCCE
-
820UbiquitinationITVVDVEKQIEAFRS
EEEEEHHHHHHHHHH
-
844 (in isoform 1)Ubiquitination-21890473
844UbiquitinationLVPQLQDKVHLLKLL
CHHHHHHHHHHHHHH
2190698
849UbiquitinationQDKVHLLKLLLFYAA
HHHHHHHHHHHHHHH
-
867 (in isoform 1)Ubiquitination-21890473
867UbiquitinationPDAEPFQKGWSGS--
CCCCCCCCCCCCC--
-

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 SIMC1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SIMC1_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 SIMC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUMO2_HUMANSUMO2physical
23086935
SUMO1_HUMANSUMO1physical
23086935

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 SIMC1_HUMAN

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Related Literatures of Post-Translational Modification

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