BEND4_HUMAN - dbPTM
BEND4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BEND4_HUMAN
UniProt AC Q6ZU67
Protein Name BEN domain-containing protein 4
Gene Name BEND4
Organism Homo sapiens (Human).
Sequence Length 534
Subcellular Localization
Protein Description
Protein Sequence MEEEMQPAEEGPSVPKIYKQRSPYSVLKTFPSKRPALAKRYERPTLVELPHVRAPPPPPPPFAPHAAVSISSSEPPPQQFQAQSSYPPGPGRAAAAASSSSPSCTPATSQGHLRTPAQPPPASPAASSSSSFAAVVRYGPGAAAAAGTGGTGSDSASLELSAESRMILDAFAQQCSRVLSLLNCGGKLLDSNHSQSMISCVKQEGSSYNERQEHCHIGKGVHSQTSDNVDIEMQYMQRKQQTSAFLRVFTDSLQNYLLSGSFPTPNPSSASEYGHLADVDPLSTSPVHTLGGWTSPATSESHGHPSSSTLPEEEEEEDEEGYCPRCQELEQEVISLQQENEELRRKLESIPVPCQTVLDYLKMVLQHHNQLLIPQPADQPTEGSKQLLNNYPVYITSKQWDEAVNSSKKDGRRLLRYLIRFVFTTDELKYSCGLGKRKRSVQSGETGPERRPLDPVKVTCLREFIRMHCTSNPDWWMPSEEQINKVFSDAVGHARQGRAVGTFLHNGGSFYEGIDHQASQDEVFNKSSQDGSGD
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
98PhosphorylationGRAAAAASSSSPSCT
CHHHHHHCCCCCCCC
26.4830108239
99PhosphorylationRAAAAASSSSPSCTP
HHHHHHCCCCCCCCC
30.0627732954
100PhosphorylationAAAAASSSSPSCTPA
HHHHHCCCCCCCCCC
43.7127732954
101PhosphorylationAAAASSSSPSCTPAT
HHHHCCCCCCCCCCC
23.8427732954
103PhosphorylationAASSSSPSCTPATSQ
HHCCCCCCCCCCCCC
32.3527732954
105PhosphorylationSSSSPSCTPATSQGH
CCCCCCCCCCCCCCC
21.9427732954
108PhosphorylationSPSCTPATSQGHLRT
CCCCCCCCCCCCCCC
23.8430108239
109PhosphorylationPSCTPATSQGHLRTP
CCCCCCCCCCCCCCC
35.9530108239
123PhosphorylationPAQPPPASPAASSSS
CCCCCCCCCCCCCCC
22.35-
187UbiquitinationSLLNCGGKLLDSNHS
HHHHCCCEECCCCCC
31.03-
202UbiquitinationQSMISCVKQEGSSYN
HHHHHHHHHCCCCHH
47.1329967540
239UbiquitinationEMQYMQRKQQTSAFL
HHHHHHHHHHHHHHH
29.84-
301PhosphorylationTSPATSESHGHPSSS
CCCCCHHCCCCCCCC
34.2424275569
309PhosphorylationHGHPSSSTLPEEEEE
CCCCCCCCCCHHHHH
48.5624275569
346UbiquitinationENEELRRKLESIPVP
HCHHHHHHHHCCCCC
50.61-
385UbiquitinationDQPTEGSKQLLNNYP
CCCCCHHHHHHHCCC
56.6829967540
394PhosphorylationLLNNYPVYITSKQWD
HHHCCCEEEEEHHHH
8.25-
396PhosphorylationNNYPVYITSKQWDEA
HCCCEEEEEHHHHHH
16.51-
397PhosphorylationNYPVYITSKQWDEAV
CCCEEEEEHHHHHHH
17.19-
425PhosphorylationLIRFVFTTDELKYSC
HHHHHCCCCHHHHCC
18.93-
436AcetylationKYSCGLGKRKRSVQS
HHCCCCCCCCCCCCC
60.8425953088
440PhosphorylationGLGKRKRSVQSGETG
CCCCCCCCCCCCCCC
27.7826852163
443PhosphorylationKRKRSVQSGETGPER
CCCCCCCCCCCCCCC
36.1226852163
479PhosphorylationNPDWWMPSEEQINKV
CCCCCCCCHHHHHHH
37.3529759185
519PhosphorylationEGIDHQASQDEVFNK
CCCCCCCCHHHHHHH
31.4317525332
528PhosphorylationDEVFNKSSQDGSGD-
HHHHHHCCCCCCCC-
33.6217525332

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 BEND4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BEND4_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 BEND4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of BEND4_HUMAN !!

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 BEND4_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-519 AND SER-528, ANDMASS SPECTROMETRY.

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