ZBED1_HUMAN - dbPTM
ZBED1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZBED1_HUMAN
UniProt AC O96006
Protein Name Zinc finger BED domain-containing protein 1
Gene Name ZBED1
Organism Homo sapiens (Human).
Sequence Length 694
Subcellular Localization Nucleus . In granular structures.
Protein Description Binds to 5'-TGTCG[CT]GA[CT]A-3' DNA elements found in the promoter regions of a number of genes related to cell proliferation. Binds to the histone H1 promoter and stimulates transcription. Was first identified as gene weakly similar to Ac transposable elements, but does not code for any transposase activity..
Protein Sequence MENKSLESSQTDLKLVAHPRAKSKVWKYFGFDTNAEGCILQWKKIYCRICMAQIAYSGNTSNLSYHLEKNHPEEFCEFVKSNTEQMREAFATAFSKLKPESSQQPGQDALAVKAGHGYDSKKQQELTAAVLGLICEGLYPASIVDEPTFKVLLKTADPRYELPSRKYISTKAIPEKYGAVREVILKELAEATWCGISTDMWRSENQNRAYVTLAAHFLGLGAPNCLSMGSRCLKTFEVPEENTAETITRVLYEVFIEWGISAKVFGATTNYGKDIVKACSLLDVAVHMPCLGHTFNAGIQQAFQLPKLGALLSRCRKLVEYFQQSAVAMYMLYEKQKQQNVAHCMLVSNRVSWWGSTLAMLQRLKEQQFVIAGVLVEDSNNHHLMLEASEWATIEGLVELLQPFKQVAEMLSASRYPTISMVKPLLHMLLNTTLNIKETDSKELSMAKEVIAKELSKTYQETPEIDMFLNVATFLDPRYKRLPFLSAFERQQVENRVVEEAKGLLDKVKDGGYRPAEDKIFPVPEEPPVKKLMRTSTPPPASVINNMLAEIFCQTGGVEDQEEWHAQVVEELSNFKSQKVLGLNEDPLKWWSDRLALFPLLPKVLQKYWCVTATRVAPERLFGSAANVVSAKRNRLAPAHVDEQVFLYENARSGAEAEPEDQDEGEWGLDQEQVFSLGDGVSGGFFGIRDSSFL
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
5Phosphorylation---MENKSLESSQTD
---CCCCCCCCCHHC
49.2925159151
8PhosphorylationMENKSLESSQTDLKL
CCCCCCCCCHHCHHH
32.7928450419
9PhosphorylationENKSLESSQTDLKLV
CCCCCCCCHHCHHHH
27.9425159151
11PhosphorylationKSLESSQTDLKLVAH
CCCCCCHHCHHHHCC
45.2930108239
14UbiquitinationESSQTDLKLVAHPRA
CCCHHCHHHHCCHHH
43.66-
43UbiquitinationEGCILQWKKIYCRIC
CCCEEEHHHHHHHHH
19.14-
80AcetylationEEFCEFVKSNTEQMR
HHHHHHHHHCHHHHH
43.2226051181
80UbiquitinationEEFCEFVKSNTEQMR
HHHHHHHHHCHHHHH
43.22-
96AcetylationAFATAFSKLKPESSQ
HHHHHHHHCCCCCCC
54.8226051181
96UbiquitinationAFATAFSKLKPESSQ
HHHHHHHHCCCCCCC
54.82-
98AcetylationATAFSKLKPESSQQP
HHHHHHCCCCCCCCC
50.9426051181
98UbiquitinationATAFSKLKPESSQQP
HHHHHHCCCCCCCCC
50.94-
102PhosphorylationSKLKPESSQQPGQDA
HHCCCCCCCCCCCCC
31.0428555341
113UbiquitinationGQDALAVKAGHGYDS
CCCCCHHHCCCCCCH
42.9421890473
154UbiquitinationPTFKVLLKTADPRYE
CCCEEEEECCCCCCC
37.19-
167PhosphorylationYELPSRKYISTKAIP
CCCCCCCCCCCCCCH
10.0519664994
170PhosphorylationPSRKYISTKAIPEKY
CCCCCCCCCCCHHHH
18.2219664994
171AcetylationSRKYISTKAIPEKYG
CCCCCCCCCCHHHHC
37.2126051181
171UbiquitinationSRKYISTKAIPEKYG
CCCCCCCCCCHHHHC
37.21-
176UbiquitinationSTKAIPEKYGAVREV
CCCCCHHHHCHHHHH
43.56-
210PhosphorylationSENQNRAYVTLAAHF
CCCCCHHHHHHHHHH
7.25-
212PhosphorylationNQNRAYVTLAAHFLG
CCCHHHHHHHHHHHC
9.67-
227PhosphorylationLGAPNCLSMGSRCLK
CCCCCHHHCCCCCEE
24.25-
268PhosphorylationSAKVFGATTNYGKDI
CEEECCCCCCCHHHH
18.8921406692
269PhosphorylationAKVFGATTNYGKDIV
EEECCCCCCCHHHHH
26.3821406692
271PhosphorylationVFGATTNYGKDIVKA
ECCCCCCCHHHHHHH
24.3821406692
273UbiquitinationGATTNYGKDIVKACS
CCCCCCHHHHHHHHH
33.64-
313PhosphorylationPKLGALLSRCRKLVE
HHHHHHHHHHHHHHH
30.1325348772
317AcetylationALLSRCRKLVEYFQQ
HHHHHHHHHHHHHHH
61.5819811495
416PhosphorylationEMLSASRYPTISMVK
HHHHCCCCCCHHHHH
11.3930266825
418PhosphorylationLSASRYPTISMVKPL
HHCCCCCCHHHHHHH
19.4230266825
420PhosphorylationASRYPTISMVKPLLH
CCCCCCHHHHHHHHH
21.7230266825
453UbiquitinationMAKEVIAKELSKTYQ
HHHHHHHHHHHHHHC
48.33-
502UbiquitinationNRVVEEAKGLLDKVK
HHHHHHHHHHHHHHH
54.06-
509UbiquitinationKGLLDKVKDGGYRPA
HHHHHHHHCCCCCCC
57.29-
519UbiquitinationGYRPAEDKIFPVPEE
CCCCCCCCCCCCCCC
37.44-
519AcetylationGYRPAEDKIFPVPEE
CCCCCCCCCCCCCCC
37.4426051181
530UbiquitinationVPEEPPVKKLMRTST
CCCCCCHHHHHCCCC
46.06-
535PhosphorylationPVKKLMRTSTPPPAS
CHHHHHCCCCCCCHH
24.0024275569
536PhosphorylationVKKLMRTSTPPPASV
HHHHHCCCCCCCHHH
28.6627251275
537PhosphorylationKKLMRTSTPPPASVI
HHHHCCCCCCCHHHH
38.9227251275
542PhosphorylationTSTPPPASVINNMLA
CCCCCCHHHHHHHHH
29.3324275569
579UbiquitinationLSNFKSQKVLGLNED
HHCCCCCCCCCCCCC
46.66-
607AcetylationLLPKVLQKYWCVTAT
HHHHHHHHCCCCCCE
36.2426051181
607UbiquitinationLLPKVLQKYWCVTAT
HHHHHHHHCCCCCCE
36.2421890473
632UbiquitinationAANVVSAKRNRLAPA
HHHHHHHHCCCCCCC
42.57-
648PhosphorylationVDEQVFLYENARSGA
CCCHHHHCCCCCCCC
8.8227642862

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 ZBED1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZBED1_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 ZBED1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPEF1_HUMANSPEF1physical
16189514
NIF3L_HUMANNIF3L1physical
16189514
GPN1_HUMANGPN1physical
16189514
NUD18_HUMANNUDT18physical
16189514
GPSM1_HUMANGPSM1physical
16189514
NIP7_HUMANNIP7physical
16189514
VINEX_HUMANSORBS3physical
16189514
ZBED1_HUMANZBED1physical
25416956
UCHL5_HUMANUCHL5physical
25416956
AMOL2_HUMANAMOTL2physical
25416956
CA109_HUMANC1orf109physical
25416956
LRC20_HUMANLRRC20physical
25416956
KLH40_HUMANKLHL40physical
25416956
CSTF1_HUMANCSTF1physical
28514442
CREG1_HUMANCREG1physical
28514442
UBP22_HUMANUSP22physical
28514442
P66B_HUMANGATAD2Bphysical
28514442
JIP4_HUMANSPAG9physical
28514442
TPC2A_HUMANTRAPPC2physical
28514442
TPC2B_HUMANTRAPPC2physical
28514442
CDK7_HUMANCDK7physical
28514442
MBD3_HUMANMBD3physical
28514442
MTA2_HUMANMTA2physical
28514442
GDAP2_HUMANGDAP2physical
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 ZBED1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP