FBLN4_HUMAN - dbPTM
FBLN4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FBLN4_HUMAN
UniProt AC O95967
Protein Name EGF-containing fibulin-like extracellular matrix protein 2
Gene Name EFEMP2
Organism Homo sapiens (Human).
Sequence Length 443
Subcellular Localization Secreted.
Protein Description
Protein Sequence MLPCASCLPGSLLLWALLLLLLGSASPQDSEEPDSYTECTDGYEWDPDSQHCRDVNECLTIPEACKGEMKCINHYGGYLCLPRSAAVINDLHGEGPPPPVPPAQHPNPCPPGYEPDDQDSCVDVDECAQALHDCRPSQDCHNLPGSYQCTCPDGYRKIGPECVDIDECRYRYCQHRCVNLPGSFRCQCEPGFQLGPNNRSCVDVNECDMGAPCEQRCFNSYGTFLCRCHQGYELHRDGFSCSDIDECSYSSYLCQYRCINEPGRFSCHCPQGYQLLATRLCQDIDECESGAHQCSEAQTCVNFHGGYRCVDTNRCVEPYIQVSENRCLCPASNPLCREQPSSIVHRYMTITSERSVPADVFQIQATSVYPGAYNAFQIRAGNSQGDFYIRQINNVSAMLVLARPVTGPREYVLDLEMVTMNSLMSYRASSVLRLTVFVGAYTF
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
137PhosphorylationALHDCRPSQDCHNLP
HHHHCCCCCCCCCCC
21.2124043423
146PhosphorylationDCHNLPGSYQCTCPD
CCCCCCCCCEEECCC
15.3024043423
147PhosphorylationCHNLPGSYQCTCPDG
CCCCCCCCEEECCCC
17.3324043423
150PhosphorylationLPGSYQCTCPDGYRK
CCCCCEEECCCCCHH
16.1424043423
155PhosphorylationQCTCPDGYRKIGPEC
EEECCCCCHHCCCCE
19.0024043423
183PhosphorylationRCVNLPGSFRCQCEP
CCCCCCCCEEEEECC
13.9525690035
198N-linked_GlycosylationGFQLGPNNRSCVDVN
CCCCCCCCCCCCCHH
40.14UniProtKB CARBOHYD
341PhosphorylationPLCREQPSSIVHRYM
CCCCCCCCCCHHEHH
32.1828348404
342PhosphorylationLCREQPSSIVHRYMT
CCCCCCCCCHHEHHE
35.0028348404
349PhosphorylationSIVHRYMTITSERSV
CCHHEHHEECCCCCC
16.5124719451
351PhosphorylationVHRYMTITSERSVPA
HHEHHEECCCCCCCC
18.5028348404
352PhosphorylationHRYMTITSERSVPAD
HEHHEECCCCCCCCC
27.4528348404
373PhosphorylationTSVYPGAYNAFQIRA
EEECCCCCEEEEEEC
16.97-
394N-linked_GlycosylationFYIRQINNVSAMLVL
EEEEEECCEEEEEEE
30.65UniProtKB CARBOHYD
426PhosphorylationTMNSLMSYRASSVLR
EHHHHHHHHHHHHHH
9.0222817900

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 FBLN4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FBLN4_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 FBLN4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLS4_HUMANPLSCR4physical
16189514
SGTB_HUMANSGTBphysical
16189514
CTSR1_HUMANCATSPER1physical
16189514
PIDD1_HUMANPIDD1physical
16189514
LIGO1_HUMANLINGO1physical
16189514
F124B_HUMANFAM124Bphysical
16189514
ZN426_HUMANZNF426physical
16189514
RHPN1_HUMANRHPN1physical
16189514
RHXF2_HUMANRHOXF2physical
16189514
SGTB_HUMANSGTBphysical
25416956
NUFP2_HUMANNUFIP2physical
25416956
CCD33_HUMANCCDC33physical
25416956
CE024_HUMANC5orf24physical
25416956
LCE2D_HUMANLCE2Dphysical
25416956
LCE3C_HUMANLCE3Cphysical
25416956

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614437Cutis laxa, autosomal recessive, 1B (ARCL1B)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FBLN4_HUMAN

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Related Literatures of Post-Translational Modification

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