HNRC1_HUMAN - dbPTM
HNRC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRC1_HUMAN
UniProt AC O60812
Protein Name Heterogeneous nuclear ribonucleoprotein C-like 1
Gene Name HNRNPCL1
Organism Homo sapiens (Human).
Sequence Length 293
Subcellular Localization Nucleus. Component of ribonucleosomes..
Protein Description May play a role in nucleosome assembly by neutralizing basic proteins such as A and B core hnRNPs..
Protein Sequence MASNVTNKMDPHSMNSRVFIGNLNTLVVKKSDVEAIFSKYGKIAGCSVHKGFAFVQYDKEKNARAAVAGEDGRMIASQVVDINLAAEPKVNRGNAGVKRSAAEMYGSSFDLDYGFQRDYYDGMYSFPARVPPPPPIALAVVPSKRQRLSGNTSRRGKSGFNSKSGKRGSSKSGKLKGDDLQAIKQELTQIKQKVDSLLENLEKIEKEQSKQEVEVKNAKSEEEQSSSSMKKDETHVKMESEGGAEDSAEEGDPLDDDVNEDQGDDQLELIKDDEKEAEEGEDDRDSTNGQDDS
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------MASNVTNKM
------CCCCCCCCC
-
3Phosphorylation-----MASNVTNKMD
-----CCCCCCCCCC
-
25PhosphorylationVFIGNLNTLVVKKSD
EEEEECCEEEEEHHH
30576142
29UbiquitinationNLNTLVVKKSDVEAI
ECCEEEEEHHHHHHH
21890473
29AcetylationNLNTLVVKKSDVEAI
ECCEEEEEHHHHHHH
25953088
29UbiquitinationNLNTLVVKKSDVEAI
ECCEEEEEHHHHHHH
23000965
30AcetylationLNTLVVKKSDVEAIF
CCEEEEEHHHHHHHH
26051181
30UbiquitinationLNTLVVKKSDVEAIF
CCEEEEEHHHHHHHH
23000965
30MalonylationLNTLVVKKSDVEAIF
CCEEEEEHHHHHHHH
26320211
31PhosphorylationNTLVVKKSDVEAIFS
CEEEEEHHHHHHHHH
30266825
38PhosphorylationSDVEAIFSKYGKIAG
HHHHHHHHHHCCCCC
21712546
39SumoylationDVEAIFSKYGKIAGC
HHHHHHHHHCCCCCC
-
39UbiquitinationDVEAIFSKYGKIAGC
HHHHHHHHHCCCCCC
32015554
39MethylationDVEAIFSKYGKIAGC
HHHHHHHHHCCCCCC
88743
39MalonylationDVEAIFSKYGKIAGC
HHHHHHHHHCCCCCC
26320211
39AcetylationDVEAIFSKYGKIAGC
HHHHHHHHHCCCCCC
25825284
42UbiquitinationAIFSKYGKIAGCSVH
HHHHHHCCCCCCEEE
-
50UbiquitinationIAGCSVHKGFAFVQY
CCCCEEECCEEEEEE
22817900
89UbiquitinationINLAAEPKVNRGNAG
EEECCCCCCCCCCCC
29967540
100PhosphorylationGNAGVKRSAAEMYGS
CCCCCCHHHHHHHCC
24043423
105PhosphorylationKRSAAEMYGSSFDLD
CHHHHHHHCCCCCCC
18669648
107PhosphorylationSAAEMYGSSFDLDYG
HHHHHHCCCCCCCCC
22496350
108PhosphorylationAAEMYGSSFDLDYGF
HHHHHCCCCCCCCCC
24043423
113PhosphorylationGSSFDLDYGFQRDYY
CCCCCCCCCCCCCCC
24043423
120PhosphorylationYGFQRDYYDGMYSFP
CCCCCCCCCCCEECC
30576142
124PhosphorylationRDYYDGMYSFPARVP
CCCCCCCEECCCCCC
30576142
125PhosphorylationDYYDGMYSFPARVPP
CCCCCCEECCCCCCC
30576142
143PhosphorylationIALAVVPSKRQRLSG
EEEEECCCCCCCCCC
30266825
144AcetylationALAVVPSKRQRLSGN
EEEECCCCCCCCCCC
25953088
144UbiquitinationALAVVPSKRQRLSGN
EEEECCCCCCCCCCC
24816145
149PhosphorylationPSKRQRLSGNTSRRG
CCCCCCCCCCCCCCC
22817900
152PhosphorylationRQRLSGNTSRRGKSG
CCCCCCCCCCCCCCC
22817900
157UbiquitinationGNTSRRGKSGFNSKS
CCCCCCCCCCCCCCC
27667366
157AcetylationGNTSRRGKSGFNSKS
CCCCCCCCCCCCCCC
26051181
158PhosphorylationNTSRRGKSGFNSKSG
CCCCCCCCCCCCCCC
28985074
163AcetylationGKSGFNSKSGKRGSS
CCCCCCCCCCCCCCC
90171
164PhosphorylationKSGFNSKSGKRGSSK
CCCCCCCCCCCCCCC
22817900
166AcetylationGFNSKSGKRGSSKSG
CCCCCCCCCCCCCCC
61177
169PhosphorylationSKSGKRGSSKSGKLK
CCCCCCCCCCCCCCC
24260401
171AcetylationSGKRGSSKSGKLKGD
CCCCCCCCCCCCCHH
90173
171UbiquitinationSGKRGSSKSGKLKGD
CCCCCCCCCCCCCHH
23000965
172PhosphorylationGKRGSSKSGKLKGDD
CCCCCCCCCCCCHHH
26546556
174AcetylationRGSSKSGKLKGDDLQ
CCCCCCCCCCHHHHH
23749302
174UbiquitinationRGSSKSGKLKGDDLQ
CCCCCCCCCCHHHHH
23000965
176AcetylationSSKSGKLKGDDLQAI
CCCCCCCCHHHHHHH
26051181
176SumoylationSSKSGKLKGDDLQAI
CCCCCCCCHHHHHHH
-
176UbiquitinationSSKSGKLKGDDLQAI
CCCCCCCCHHHHHHH
23000965
176MethylationSSKSGKLKGDDLQAI
CCCCCCCCHHHHHHH
-
191AcetylationKQELTQIKQKVDSLL
HHHHHHHHHHHHHHH
25953088
191UbiquitinationKQELTQIKQKVDSLL
HHHHHHHHHHHHHHH
23000965
193UbiquitinationELTQIKQKVDSLLEN
HHHHHHHHHHHHHHH
23000965
193UbiquitinationELTQIKQKVDSLLEN
HHHHHHHHHHHHHHH
21890473
193AcetylationELTQIKQKVDSLLEN
HHHHHHHHHHHHHHH
26051181
193MalonylationELTQIKQKVDSLLEN
HHHHHHHHHHHHHHH
26320211
196PhosphorylationQIKQKVDSLLENLEK
HHHHHHHHHHHHHHH
30266825
203UbiquitinationSLLENLEKIEKEQSK
HHHHHHHHHHHHHHH
21890473
203AcetylationSLLENLEKIEKEQSK
HHHHHHHHHHHHHHH
23749302
206UbiquitinationENLEKIEKEQSKQEV
HHHHHHHHHHHHHHH
22817900
210UbiquitinationKIEKEQSKQEVEVKN
HHHHHHHHHHHHHHH
22817900
216AcetylationSKQEVEVKNAKSEEE
HHHHHHHHHCCCHHH
7987643
219AcetylationEVEVKNAKSEEEQSS
HHHHHHCCCHHHHCC
7987651
220PhosphorylationVEVKNAKSEEEQSSS
HHHHHCCCHHHHCCC
28102081
225PhosphorylationAKSEEEQSSSSMKKD
CCCHHHHCCCCCCCC
28102081
226PhosphorylationKSEEEQSSSSMKKDE
CCHHHHCCCCCCCCC
28102081
227PhosphorylationSEEEQSSSSMKKDET
CHHHHCCCCCCCCCC
28102081
228PhosphorylationEEEQSSSSMKKDETH
HHHHCCCCCCCCCCC
28102081
234PhosphorylationSSMKKDETHVKMESE
CCCCCCCCCEEEECC
-
237SumoylationKKDETHVKMESEGGA
CCCCCCEEEECCCCC
-
240PhosphorylationETHVKMESEGGAEDS
CCCEEEECCCCCCCC
26657352
247PhosphorylationSEGGAEDSAEEGDPL
CCCCCCCCCCCCCCC
24173317
271UbiquitinationDDQLELIKDDEKEAE
CCHHEEEECCHHHHH
32015554

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 HNRC1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HNRC1_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 HNRC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HNRL2_HUMANHNRNPUL2physical
22939629
HNRPC_HUMANHNRNPCphysical
22939629

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 HNRC1_HUMAN

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Related Literatures of Post-Translational Modification

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