LOXL4_HUMAN - dbPTM
LOXL4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LOXL4_HUMAN
UniProt AC Q96JB6
Protein Name Lysyl oxidase homolog 4
Gene Name LOXL4
Organism Homo sapiens (Human).
Sequence Length 756
Subcellular Localization Secreted, extracellular space .
Protein Description May modulate the formation of a collagenous extracellular matrix..
Protein Sequence MAWSPPATLFLFLLLLGQPPPSRPQSLGTTKLRLVGPESKPEEGRLEVLHQGQWGTVCDDNFAIQEATVACRQLGFEAALTWAHSAKYGQGEGPIWLDNVRCVGTESSLDQCGSNGWGVSDCSHSEDVGVICHPRRHRGYLSETVSNALGPQGRRLEEVRLKPILASAKQHSPVTEGAVEVKYEGHWRQVCDQGWTMNNSRVVCGMLGFPSEVPVDSHYYRKVWDLKMRDPKSRLKSLTNKNSFWIHQVTCLGTEPHMANCQVQVAPARGKLRPACPGGMHAVVSCVAGPHFRPPKTKPQRKGSWAEEPRVRLRSGAQVGEGRVEVLMNRQWGTVCDHRWNLISASVVCRQLGFGSAREALFGARLGQGLGPIHLSEVRCRGYERTLSDCPALEGSQNGCQHENDAAVRCNVPNMGFQNQVRLAGGRIPEEGLLEVQVEVNGVPRWGSVCSENWGLTEAMVACRQLGLGFAIHAYKETWFWSGTPRAQEVVMSGVRCSGTELALQQCQRHGPVHCSHGGGRFLAGVSCMDSAPDLVMNAQLVQETAYLEDRPLSQLYCAHEENCLSKSADHMDWPYGYRRLLRFSTQIYNLGRTDFRPKTGRDSWVWHQCHRHYHSIEVFTHYDLLTLNGSKVAEGHKASFCLEDTNCPTGLQRRYACANFGEQGVTVGCWDTYRHDIDCQWVDITDVGPGNYIFQVIVNPHYEVAESDFSNNMLQCRCKYDGHRVWLHNCHTGNSYPANAELSLEQEQRLRNNLI
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
140PhosphorylationHPRRHRGYLSETVSN
CCCCCCCCCCHHHHH
13.6526503514
146PhosphorylationGYLSETVSNALGPQG
CCCCHHHHHHHCCCC
24.6526503514
172PhosphorylationLASAKQHSPVTEGAV
HHHHHCCCCCCCCCE
20.6924275569
175PhosphorylationAKQHSPVTEGAVEVK
HHCCCCCCCCCEEEE
31.8924275569
183PhosphorylationEGAVEVKYEGHWRQV
CCCEEEEECCCCEEE
32.1124275569
198N-linked_GlycosylationCDQGWTMNNSRVVCG
ECCCCCCCCCEEEEE
35.63UniProtKB CARBOHYD
304PhosphorylationTKPQRKGSWAEEPRV
CCCCCCCCCCCCCCE
26.5829507054
383PhosphorylationSEVRCRGYERTLSDC
HEEECCCCCCCHHCC
5.2717081983
475PhosphorylationLGFAIHAYKETWFWS
CEEEEEEEECCEECC
8.66-
629N-linked_GlycosylationHYDLLTLNGSKVAEG
EEEEEEECCCCCCCC
47.67UniProtKB CARBOHYD
640PhosphorylationVAEGHKASFCLEDTN
CCCCCCCEEECCCCC
22.6929507054
674"2',4',5'-topaquinone"TVGCWDTYRHDIDCQ
EECEECCCCCCCCCE
11.95-
674OtherTVGCWDTYRHDIDCQ
EECEECCCCCCCCCE
11.95-

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 LOXL4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LOXL4_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 LOXL4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APOE_HUMANAPOEphysical
21163940
LONM_HUMANLONP1physical
21163940
RD23A_HUMANRAD23Aphysical
21163940
PCH2_HUMANTRIP13physical
19060904
KDM1A_HUMANKDM1Aphysical
23455924
ANM6_HUMANPRMT6physical
23455924
SUV91_HUMANSUV39H1physical
23455924
TCPW_HUMANCCT6Bphysical
26186194
SPS2_HUMANSEPHS2physical
26186194
SPS2_HUMANSEPHS2physical
28514442
TCPW_HUMANCCT6Bphysical
28514442
TCPZ_HUMANCCT6Aphysical
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 LOXL4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-383, AND MASSSPECTROMETRY.

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