ICE2_HUMAN - dbPTM
ICE2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ICE2_HUMAN
UniProt AC Q659A1
Protein Name Little elongation complex subunit 2
Gene Name ICE2
Organism Homo sapiens (Human).
Sequence Length 982
Subcellular Localization Nucleus . Colocalizes with COIL in subnuclear Cajal and histone locus bodies. Translocates in the LEC complex to Cajal and histone locus bodies at snRNA genes in a ICE1-dependent manner. Associates to transcriptionally active chromatin at snRNA genes
Protein Description Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III..
Protein Sequence MSSKMVISEPGLNWDISPKNGLKTFFSRENYKDHSMAPSLKELRVLSNRRIGENLNASASSVENEPAVSSATQAKEKVKTTIGMVLLPKPRVPYPRFSRFSQREQRSYVDLLVKYAKIPANSKAVGINKNDYLQYLDMKKHVNEEVTEFLKFLQNSAKKCAQDYNMLSDDARLFTEKILRACIEQVKKYSEFYTLHEVTSLMGFFPFRVEMGLKLEKTLLALGSVKYVKTVFPSMPIKLQLSKDDIATIETSEQTAEAMHYDISKDPNAEKLVSRYHPQIALTSQSLFTLLNNHGPTYKEQWEIPVCIQVIPVAGSKPVKVIYINSPLPQKKMTMRERNQIFHEVPLKFMMSKNTSVPVSAVFMDKPEEFISEMDMSCEVNECRKIESLENLYLDFDDDVTELETFGVTTTKVSKSPSPASTSTVPNMTDAPTAPKAGTTTVAPSAPDISANSRSLSQILMEQLQKEKQLVTGMDGGPEECKNKDDQGFESCEKVSNSDKPLIQDSDLKTSDALQLENSQEIETSNKNDMTIDILHADGERPNVLENLDNSKEKTVGSEAAKTEDTVLCSSDTDEECLIIDTECKNNSDGKTAVVGSNLSSRPASPNSSSGQASVGNQTNTACSPEESCVLKKPIKRVYKKFDPVGEILKMQDELLKPISRKVPELPLMNLENSKQPSVSEQLSGPSDSSSWPKSGWPSAFQKPKGRLPYELQDYVEDTSEYLAPQEGNFVYKLFSLQDLLLLVRCSVQRIETRPRSKKRKKIRRQFPVYVLPKVEYQACYGVEALTESELCRLWTESLLHSNSSFYVGHIDAFTSKLFLLEEITSEELKEKLSALKISNLFNILQHILKKLSSLQEGSYLLSHAAEDSSLLIYKASDGKVTRTAYNLYKTHCGLPGVPSSLSVPWVPLDPSLLLPYHIHHGRIPCTFPPKSLDTTTQQKIGGTRMPTRSHRNPVSMETKSSCLPAQQVETEGVAPHKRKIT
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
2Phosphorylation------MSSKMVISE
------CCCCEEECC
24719451
3Phosphorylation-----MSSKMVISEP
-----CCCCEEECCC
23401153
8PhosphorylationMSSKMVISEPGLNWD
CCCCEEECCCCCCCC
29978859
17PhosphorylationPGLNWDISPKNGLKT
CCCCCCCCCCCCCHH
23401153
24PhosphorylationSPKNGLKTFFSRENY
CCCCCCHHHHCCCCC
24719451
60PhosphorylationENLNASASSVENEPA
CCCCCCCCHHCCCCC
28555341
61PhosphorylationNLNASASSVENEPAV
CCCCCCCHHCCCCCC
28555341
75AcetylationVSSATQAKEKVKTTI
CCCHHHHHHHHCCEE
20167786
89 (in isoform 2)Ubiquitination-21890473
101PhosphorylationYPRFSRFSQREQRSY
CCCCCCCCHHHHHHH
24719451
108PhosphorylationSQREQRSYVDLLVKY
CHHHHHHHHHHHHHH
-
115PhosphorylationYVDLLVKYAKIPANS
HHHHHHHHCCCCCCC
24719451
117UbiquitinationDLLVKYAKIPANSKA
HHHHHHCCCCCCCCC
-
123UbiquitinationAKIPANSKAVGINKN
CCCCCCCCCCCCCHH
-
129UbiquitinationSKAVGINKNDYLQYL
CCCCCCCHHHHHHHH
-
132PhosphorylationVGINKNDYLQYLDMK
CCCCHHHHHHHHHHH
-
135PhosphorylationNKNDYLQYLDMKKHV
CHHHHHHHHHHHHHC
-
139AcetylationYLQYLDMKKHVNEEV
HHHHHHHHHHCCHHH
7696619
140UbiquitinationLQYLDMKKHVNEEVT
HHHHHHHHHCCHHHH
-
140AcetylationLQYLDMKKHVNEEVT
HHHHHHHHHCCHHHH
7696629
151AcetylationEEVTEFLKFLQNSAK
HHHHHHHHHHHHHHH
7696639
159UbiquitinationFLQNSAKKCAQDYNM
HHHHHHHHHHHHHCC
-
177UbiquitinationDARLFTEKILRACIE
HHHHHHHHHHHHHHH
-
226UbiquitinationLLALGSVKYVKTVFP
HHHHCCCEEEEECCC
21890473
226 (in isoform 1)Ubiquitination-21890473
226UbiquitinationLLALGSVKYVKTVFP
HHHHCCCEEEEECCC
21890473
248PhosphorylationLSKDDIATIETSEQT
ECHHCCEEEECHHHH
-
271UbiquitinationSKDPNAEKLVSRYHP
CCCCCHHHHHHHHCH
-
274PhosphorylationPNAEKLVSRYHPQIA
CCHHHHHHHHCHHHE
-
284PhosphorylationHPQIALTSQSLFTLL
CHHHEEEHHHHHHHH
20068231
323PhosphorylationSKPVKVIYINSPLPQ
CCCEEEEEECCCCCC
29396449
326PhosphorylationVKVIYINSPLPQKKM
EEEEEECCCCCCCCC
25159151
348UbiquitinationIFHEVPLKFMMSKNT
HHHHHCHHHHCCCCC
-
388PhosphorylationNECRKIESLENLYLD
HHCCCCHHHCCEEEC
27732954
393PhosphorylationIESLENLYLDFDDDV
CHHHCCEEECCCCCC
27732954
414PhosphorylationGVTTTKVSKSPSPAS
CEEEEECCCCCCCCC
23401153
416PhosphorylationTTTKVSKSPSPASTS
EEEECCCCCCCCCCC
30266825
418PhosphorylationTKVSKSPSPASTSTV
EECCCCCCCCCCCCC
23401153
421PhosphorylationSKSPSPASTSTVPNM
CCCCCCCCCCCCCCC
23401153
422PhosphorylationKSPSPASTSTVPNMT
CCCCCCCCCCCCCCC
30266825
423PhosphorylationSPSPASTSTVPNMTD
CCCCCCCCCCCCCCC
30266825
424PhosphorylationPSPASTSTVPNMTDA
CCCCCCCCCCCCCCC
30266825
429PhosphorylationTSTVPNMTDAPTAPK
CCCCCCCCCCCCCCC
20068231
433PhosphorylationPNMTDAPTAPKAGTT
CCCCCCCCCCCCCCC
20068231
455PhosphorylationDISANSRSLSQILME
CCCCCCCCHHHHHHH
22617229
457PhosphorylationSANSRSLSQILMEQL
CCCCCCHHHHHHHHH
22617229
468UbiquitinationMEQLQKEKQLVTGMD
HHHHHHHHCHHHCCC
-
472PhosphorylationQKEKQLVTGMDGGPE
HHHHCHHHCCCCCHH
-
496PhosphorylationFESCEKVSNSDKPLI
CHHHHHCCCCCCCCC
25627689
519PhosphorylationDALQLENSQEIETSN
CHHHHCCCCCCCCCC
25159151
551PhosphorylationVLENLDNSKEKTVGS
HHHCCCCCCCCCCCC
25159151
570PhosphorylationTEDTVLCSSDTDEEC
CCCEEEECCCCCCCE
25137130
571PhosphorylationEDTVLCSSDTDEECL
CCEEEECCCCCCCEE
25137130
573PhosphorylationTVLCSSDTDEECLII
EEEECCCCCCCEEEE
25137130
592PhosphorylationKNNSDGKTAVVGSNL
ECCCCCCEEEECCCC
28450419
597PhosphorylationGKTAVVGSNLSSRPA
CCEEEECCCCCCCCC
28450419
600PhosphorylationAVVGSNLSSRPASPN
EEECCCCCCCCCCCC
23927012
601PhosphorylationVVGSNLSSRPASPNS
EECCCCCCCCCCCCC
23927012
605PhosphorylationNLSSRPASPNSSSGQ
CCCCCCCCCCCCCCC
23401153
608PhosphorylationSRPASPNSSSGQASV
CCCCCCCCCCCCCCC
29255136
609PhosphorylationRPASPNSSSGQASVG
CCCCCCCCCCCCCCC
29255136
610PhosphorylationPASPNSSSGQASVGN
CCCCCCCCCCCCCCC
29255136
614PhosphorylationNSSSGQASVGNQTNT
CCCCCCCCCCCCCCC
29255136
619PhosphorylationQASVGNQTNTACSPE
CCCCCCCCCCCCCHH
30576142
621PhosphorylationSVGNQTNTACSPEES
CCCCCCCCCCCHHHH
25850435
624PhosphorylationNQTNTACSPEESCVL
CCCCCCCCHHHHHCC
25159151
628PhosphorylationTACSPEESCVLKKPI
CCCCHHHHHCCCCCH
20873877
678PhosphorylationLENSKQPSVSEQLSG
CCCCCCCCHHHHHCC
27251275
680PhosphorylationNSKQPSVSEQLSGPS
CCCCCCHHHHHCCCC
27251275
684PhosphorylationPSVSEQLSGPSDSSS
CCHHHHHCCCCCCCC
27251275
687PhosphorylationSEQLSGPSDSSSWPK
HHHHCCCCCCCCCCC
27251275
689PhosphorylationQLSGPSDSSSWPKSG
HHCCCCCCCCCCCCC
27251275
690PhosphorylationLSGPSDSSSWPKSGW
HCCCCCCCCCCCCCC
25627689
691PhosphorylationSGPSDSSSWPKSGWP
CCCCCCCCCCCCCCC
27251275
695PhosphorylationDSSSWPKSGWPSAFQ
CCCCCCCCCCCCHHC
27251275
699PhosphorylationWPKSGWPSAFQKPKG
CCCCCCCCHHCCCCC
27251275
853PhosphorylationQHILKKLSSLQEGSY
HHHHHHHHHCCCCCH
19690332
860PhosphorylationSSLQEGSYLLSHAAE
HHCCCCCHHHHHCCC
19690332
932PhosphorylationPCTFPPKSLDTTTQQ
CCCCCCCCCCCCCCH
-
935PhosphorylationFPPKSLDTTTQQKIG
CCCCCCCCCCCHHCC
-
940UbiquitinationLDTTTQQKIGGTRMP
CCCCCCHHCCCCCCC
-
944PhosphorylationTQQKIGGTRMPTRSH
CCHHCCCCCCCCCCC
-
948PhosphorylationIGGTRMPTRSHRNPV
CCCCCCCCCCCCCCC
-
978AcetylationTEGVAPHKRKIT---
CCCCCCCCCCCC---
25953088

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 ICE2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ICE2_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 ICE2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ELL_HUMANELLphysical
21729782
EAF1_HUMANEAF1physical
21729782
ICE1_HUMANICE1physical
21729782
TBP_HUMANTBPphysical
21729782
ACTA_HUMANACTA2physical
26186194
TCPW_HUMANCCT6Bphysical
26186194
PIGR_HUMANPIGRphysical
26186194
HPT_HUMANHPphysical
26186194
TRFL_HUMANLTFphysical
26186194
MUC5B_HUMANMUC5Bphysical
26186194
A1AT_HUMANSERPINA1physical
26186194
BPIA1_HUMANBPIFA1physical
26186194
ZG16B_HUMANZG16Bphysical
26186194
PERM_HUMANMPOphysical
26186194
DMBT1_HUMANDMBT1physical
26186194
CATG_HUMANCTSGphysical
26186194
MUC5B_HUMANMUC5Bphysical
28514442
PERM_HUMANMPOphysical
28514442
BPIA1_HUMANBPIFA1physical
28514442
TRFL_HUMANLTFphysical
28514442
PIGR_HUMANPIGRphysical
28514442
A1AT_HUMANSERPINA1physical
28514442
HPT_HUMANHPphysical
28514442
CATG_HUMANCTSGphysical
28514442
DMBT1_HUMANDMBT1physical
28514442
IGJ_HUMANIGJphysical
28514442

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 ICE2_HUMAN

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Related Literatures of Post-Translational Modification

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