LRC42_HUMAN - dbPTM
LRC42_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRC42_HUMAN
UniProt AC Q9Y546
Protein Name Leucine-rich repeat-containing protein 42
Gene Name LRRC42
Organism Homo sapiens (Human).
Sequence Length 428
Subcellular Localization
Protein Description
Protein Sequence MSYYLSSENHLDPGPIYMRENGQLHMVNLALDGVRSSLQKPRPFRLFPKGFSVELCMNREDDTARKEKTDHFIFTYTREGNLRYSAKSLFSLVLGFISDNVDHIDSLIGFPEQIAEKLFSAAEARQKFTEPGAGLRALQKFTEAYGSLVLCSLCLRNRYLVISEKLEEIKSFRELTCLDLSCCKLGDEHELLEHLTNEALSSVTQLHLKDNCLSDAGVRKMTAPVRVMKRGLENLTLLDLSCNPEITDAGIGYLFSFRKLNCLDISGTGLKDIKTVKHKLQTHIGLVHSKVPLKEFDHSNCKTEGWADQIVLQWERVTAEAVKPRETSEPRAAAQRFYGKRSRAEAPLKCPLADTHMNSSEKLQFYKEKAPDCHGPVLKHEAISSQESKKSKKRPFEESETEQNNSSQPSKQKYVCLAVEDWDLLNSY
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------MSYYLSSEN
------CCCCCCCCC
23.6124043423
3Phosphorylation-----MSYYLSSENH
-----CCCCCCCCCC
13.7127642862
4Phosphorylation----MSYYLSSENHL
----CCCCCCCCCCC
7.8727642862
6Phosphorylation--MSYYLSSENHLDP
--CCCCCCCCCCCCC
21.3427642862
7Phosphorylation-MSYYLSSENHLDPG
-CCCCCCCCCCCCCC
39.5627642862
17PhosphorylationHLDPGPIYMRENGQL
CCCCCCEEECCCCEE
8.0227642862
36PhosphorylationLALDGVRSSLQKPRP
EHHHHHHHHCCCCCC
32.7527251275
37PhosphorylationALDGVRSSLQKPRPF
HHHHHHHHCCCCCCC
25.0227251275
40UbiquitinationGVRSSLQKPRPFRLF
HHHHHCCCCCCCCCC
48.5723000965
40AcetylationGVRSSLQKPRPFRLF
HHHHHCCCCCCCCCC
48.5725953088
52PhosphorylationRLFPKGFSVELCMNR
CCCCCCEEEEEECCC
24.2928348404
66UbiquitinationREDDTARKEKTDHFI
CCCCCHHHHHCCEEE
62.18-
68UbiquitinationDDTARKEKTDHFIFT
CCCHHHHHCCEEEEE
63.39-
127UbiquitinationSAAEARQKFTEPGAG
HHHHHHHHCCCCCHH
49.0121906983
129PhosphorylationAEARQKFTEPGAGLR
HHHHHHCCCCCHHHH
48.5925954137
140UbiquitinationAGLRALQKFTEAYGS
HHHHHHHHHHHHHHH
55.92-
145PhosphorylationLQKFTEAYGSLVLCS
HHHHHHHHHHHHHHH
10.8725954137
147PhosphorylationKFTEAYGSLVLCSLC
HHHHHHHHHHHHHHH
11.5725954137
165UbiquitinationRYLVISEKLEEIKSF
CEEEEEHHHHHHHCH
55.1721906983
170UbiquitinationSEKLEEIKSFRELTC
EHHHHHHHCHHHCEE
46.9821906983
209UbiquitinationSVTQLHLKDNCLSDA
HCCHHHCCCCCCCCC
35.8321963094
220SumoylationLSDAGVRKMTAPVRV
CCCCCCCCCCCCHHH
37.89-
220UbiquitinationLSDAGVRKMTAPVRV
CCCCCCCCCCCCHHH
37.8929967540
220SumoylationLSDAGVRKMTAPVRV
CCCCCCCCCCCCHHH
37.89-
256PhosphorylationAGIGYLFSFRKLNCL
CCHHHHEEEEECCCE
22.8824719451
259UbiquitinationGYLFSFRKLNCLDIS
HHHEEEEECCCEECC
41.88-
271UbiquitinationDISGTGLKDIKTVKH
ECCCCCCCHHHHHHH
59.7721963094
274UbiquitinationGTGLKDIKTVKHKLQ
CCCCCHHHHHHHHHH
58.3522817900
279UbiquitinationDIKTVKHKLQTHIGL
HHHHHHHHHHHCCCC
36.2529967540
290UbiquitinationHIGLVHSKVPLKEFD
CCCCCCCCCCHHHCC
32.7521906983
294UbiquitinationVHSKVPLKEFDHSNC
CCCCCCHHHCCCCCC
50.7121963094
302UbiquitinationEFDHSNCKTEGWADQ
HCCCCCCCCCCCHHH
54.5929967540
323UbiquitinationRVTAEAVKPRETSEP
EEEHHHCCCCCCCCH
45.4621906983
349AcetylationSRAEAPLKCPLADTH
CCCCCCCCCCCCCCC
32.5225953088
349MethylationSRAEAPLKCPLADTH
CCCCCCCCCCCCCCC
32.52-
349UbiquitinationSRAEAPLKCPLADTH
CCCCCCCCCCCCCCC
32.5221963094
355PhosphorylationLKCPLADTHMNSSEK
CCCCCCCCCCCHHHH
19.8822210691
359PhosphorylationLADTHMNSSEKLQFY
CCCCCCCHHHHHHHH
32.0922210691
360PhosphorylationADTHMNSSEKLQFYK
CCCCCCHHHHHHHHH
33.4722210691
362UbiquitinationTHMNSSEKLQFYKEK
CCCCHHHHHHHHHHH
49.9229967540
367UbiquitinationSEKLQFYKEKAPDCH
HHHHHHHHHHCCCCC
54.7729967540
369UbiquitinationKLQFYKEKAPDCHGP
HHHHHHHHCCCCCCC
62.1529967540
379UbiquitinationDCHGPVLKHEAISSQ
CCCCCHHCHHHCCCC
39.3729967540
379SumoylationDCHGPVLKHEAISSQ
CCCCCHHCHHHCCCC
39.37-
379AcetylationDCHGPVLKHEAISSQ
CCCCCHHCHHHCCCC
39.3719827773
379SumoylationDCHGPVLKHEAISSQ
CCCCCHHCHHHCCCC
39.37-
385PhosphorylationLKHEAISSQESKKSK
HCHHHCCCCCHHHHC
31.6728985074
389UbiquitinationAISSQESKKSKKRPF
HCCCCCHHHHCCCCC
61.3822817900
390UbiquitinationISSQESKKSKKRPFE
CCCCCHHHHCCCCCC
76.4322817900
392UbiquitinationSQESKKSKKRPFEES
CCCHHHHCCCCCCCC
62.7822817900
393UbiquitinationQESKKSKKRPFEESE
CCHHHHCCCCCCCCC
72.8421906983
399PhosphorylationKKRPFEESETEQNNS
CCCCCCCCCCCCCCC
42.4928555341
401PhosphorylationRPFEESETEQNNSSQ
CCCCCCCCCCCCCCC
52.7528555341
406PhosphorylationSETEQNNSSQPSKQK
CCCCCCCCCCCCCCC
37.59-
407PhosphorylationETEQNNSSQPSKQKY
CCCCCCCCCCCCCCE
48.5117525332
411UbiquitinationNNSSQPSKQKYVCLA
CCCCCCCCCCEEEEE
58.4521906983
413UbiquitinationSSQPSKQKYVCLAVE
CCCCCCCCEEEEEEC
43.3022817900

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 LRC42_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRC42_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 LRC42_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
SYNC_HUMANNARSphysical
22939629
ZC3HE_HUMANZC3H14physical
22939629
SGT1_HUMANSUGT1physical
26186194
PXDC2_HUMANPLXDC2physical
26186194
AMRA1_HUMANAMBRA1physical
26186194
CUL3_HUMANCUL3physical
28514442
PXDC2_HUMANPLXDC2physical
28514442
SGT1_HUMANSUGT1physical
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 LRC42_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND MASSSPECTROMETRY.

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