BCL7A_HUMAN - dbPTM
BCL7A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BCL7A_HUMAN
UniProt AC Q4VC05
Protein Name B-cell CLL/lymphoma 7 protein family member A
Gene Name BCL7A
Organism Homo sapiens (Human).
Sequence Length 210
Subcellular Localization
Protein Description
Protein Sequence MSGRSVRAETRSRAKDDIKRVMAAIEKVRKWEKKWVTVGDTSLRIYKWVPVTEPKVDDKNKNKKKGKDEKCGSEVTTPENSSSPGMMDMHDDNSNQSSIADASPIKQENSSNSSPAPEPNSAVPSDGTEAKVDEAQADGKEHPGAEDASDEQNSQSSMEHSMNSSEKVDRQPSGDSGLAAETSAISQDLEGVPPSKKMKLEASQQNSEEM
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------MSGRSVRAE
------CCCCCHHHH
42.8029449344
5Phosphorylation---MSGRSVRAETRS
---CCCCCHHHHHHH
21.3426074081
10PhosphorylationGRSVRAETRSRAKDD
CCCHHHHHHHHCHHH
32.7229449344
12PhosphorylationSVRAETRSRAKDDIK
CHHHHHHHHCHHHHH
43.9718452278
19UbiquitinationSRAKDDIKRVMAAIE
HHCHHHHHHHHHHHH
46.0324816145
27 (in isoform 2)Ubiquitination-41.0221890473
27 (in isoform 1)Ubiquitination-41.0221890473
27UbiquitinationRVMAAIEKVRKWEKK
HHHHHHHHHHHHHCC
41.0221890473
27AcetylationRVMAAIEKVRKWEKK
HHHHHHHHHHHHHCC
41.0225953088
30UbiquitinationAAIEKVRKWEKKWVT
HHHHHHHHHHCCEEE
63.7922817900
34 (in isoform 2)Ubiquitination-35.07-
34UbiquitinationKVRKWEKKWVTVGDT
HHHHHHCCEEEECCC
35.07-
41PhosphorylationKWVTVGDTSLRIYKW
CEEEECCCEEEEEEE
24.59-
44MethylationTVGDTSLRIYKWVPV
EECCCEEEEEEEEEC
29.92-
46PhosphorylationGDTSLRIYKWVPVTE
CCCEEEEEEEEECCC
7.74-
47 (in isoform 2)Ubiquitination-39.0721890473
47UbiquitinationDTSLRIYKWVPVTEP
CCEEEEEEEEECCCC
39.0722817900
47 (in isoform 1)Ubiquitination-39.0721890473
73PhosphorylationGKDEKCGSEVTTPEN
CCCCCCCCCCCCCCC
38.0626074081
76PhosphorylationEKCGSEVTTPENSSS
CCCCCCCCCCCCCCC
32.3626074081
77PhosphorylationKCGSEVTTPENSSSP
CCCCCCCCCCCCCCC
33.5126074081
81PhosphorylationEVTTPENSSSPGMMD
CCCCCCCCCCCCCCC
30.4526074081
82PhosphorylationVTTPENSSSPGMMDM
CCCCCCCCCCCCCCC
52.7326074081
83PhosphorylationTTPENSSSPGMMDMH
CCCCCCCCCCCCCCC
25.8726074081
94PhosphorylationMDMHDDNSNQSSIAD
CCCCCCCCCCCCCCC
43.1530576142
97PhosphorylationHDDNSNQSSIADASP
CCCCCCCCCCCCCCC
28.1426074081
98PhosphorylationDDNSNQSSIADASPI
CCCCCCCCCCCCCCC
16.4226074081
103PhosphorylationQSSIADASPIKQENS
CCCCCCCCCCCCCCC
27.9230576142
110PhosphorylationSPIKQENSSNSSPAP
CCCCCCCCCCCCCCC
30.0930278072
111PhosphorylationPIKQENSSNSSPAPE
CCCCCCCCCCCCCCC
52.9230278072
113PhosphorylationKQENSSNSSPAPEPN
CCCCCCCCCCCCCCC
39.3830278072
114PhosphorylationQENSSNSSPAPEPNS
CCCCCCCCCCCCCCC
29.3630278072
121PhosphorylationSPAPEPNSAVPSDGT
CCCCCCCCCCCCCCC
41.1628450419
125PhosphorylationEPNSAVPSDGTEAKV
CCCCCCCCCCCEEEH
41.9122199227
128PhosphorylationSAVPSDGTEAKVDEA
CCCCCCCCEEEHHHH
37.4522199227
149PhosphorylationHPGAEDASDEQNSQS
CCCCCCCCCHHHHHH
54.7430576142
154PhosphorylationDASDEQNSQSSMEHS
CCCCHHHHHHHHHHH
31.0023401153
156PhosphorylationSDEQNSQSSMEHSMN
CCHHHHHHHHHHHCC
31.3230576142
157PhosphorylationDEQNSQSSMEHSMNS
CHHHHHHHHHHHCCC
22.1328450419
161PhosphorylationSQSSMEHSMNSSEKV
HHHHHHHHCCCCCCC
13.3230576142
164PhosphorylationSMEHSMNSSEKVDRQ
HHHHHCCCCCCCCCC
31.0928450419
165PhosphorylationMEHSMNSSEKVDRQP
HHHHCCCCCCCCCCC
36.1130576142
173 (in isoform 2)Phosphorylation-47.0628450419
173PhosphorylationEKVDRQPSGDSGLAA
CCCCCCCCCCCCHHH
47.0630576142
176PhosphorylationDRQPSGDSGLAAETS
CCCCCCCCCHHHHHH
38.9522496350
176 (in isoform 2)Phosphorylation-38.9528450419
182 (in isoform 2)Phosphorylation-20.8028450419
183PhosphorylationSGLAAETSAISQDLE
CCHHHHHHHHHCCCC
18.3428555341
183 (in isoform 2)Phosphorylation-18.3427251275
186PhosphorylationAAETSAISQDLEGVP
HHHHHHHHCCCCCCC
19.8417525332
191 (in isoform 2)Phosphorylation-44.52-
193 (in isoform 2)Phosphorylation-38.00-
195PhosphorylationDLEGVPPSKKMKLEA
CCCCCCCCHHHCHHH
38.5523186163
196AcetylationLEGVPPSKKMKLEAS
CCCCCCCHHHCHHHH
63.7625953088
197 (in isoform 2)Phosphorylation-45.68-
198SulfoxidationGVPPSKKMKLEASQQ
CCCCCHHHCHHHHHH
7.4221406390
199SumoylationVPPSKKMKLEASQQN
CCCCHHHCHHHHHHC
52.6425218447
199SumoylationVPPSKKMKLEASQQN
CCCCHHHCHHHHHHC
52.64-
203PhosphorylationKKMKLEASQQNSEEM
HHHCHHHHHHCCCCC
23.9517525332
207 (in isoform 2)Phosphorylation-30.51-
207PhosphorylationLEASQQNSEEM----
HHHHHHCCCCC----
30.5117525332

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 BCL7A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BCL7A_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 BCL7A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARI1A_HUMANARID1Aphysical
26344197
SMCA4_HUMANSMARCA4physical
26344197
SMRC1_HUMANSMARCC1physical
26344197
SMRC2_HUMANSMARCC2physical
26344197
POTEJ_HUMANPOTEJphysical
28514442
SPIR1_HUMANSPIRE1physical
28514442
PHAR4_HUMANPHACTR4physical
28514442
SPIR2_HUMANSPIRE2physical
28514442
PHAR2_HUMANPHACTR2physical
28514442
BRD9_HUMANBRD9physical
28514442
MKL2_HUMANMKL2physical
28514442
DPF3_HUMANDPF3physical
28514442
BICRA_HUMANGLTSCR1physical
28514442
SMRC2_HUMANSMARCC2physical
28514442
BICRL_HUMANGLTSCR1Lphysical
28514442
MKL1_HUMANMKL1physical
28514442
REQU_HUMANDPF2physical
28514442
SMRD1_HUMANSMARCD1physical
28514442
ARI1B_HUMANARID1Bphysical
28514442
DPF1_HUMANDPF1physical
28514442
BRD7_HUMANBRD7physical
28514442
PB1_HUMANPBRM1physical
28514442
SMRD3_HUMANSMARCD3physical
28514442
SMRD2_HUMANSMARCD2physical
28514442
ADSV_HUMANSCINphysical
28514442
CAP2_HUMANCAP2physical
28514442
ARID2_HUMANARID2physical
28514442
SMCA2_HUMANSMARCA2physical
28514442
SMCA4_HUMANSMARCA4physical
28514442
ARP8_HUMANACTR8physical
28514442
GELS_HUMANGSNphysical
28514442
INO80_HUMANINO80physical
28514442
PHF10_HUMANPHF10physical
28514442
WDR54_HUMANWDR54physical
28514442
SNF5_HUMANSMARCB1physical
28514442
IN80C_HUMANINO80Cphysical
28514442
CAP1_HUMANCAP1physical
28514442
IN80E_HUMANINO80Ephysical
28514442
SSXT_HUMANSS18physical
28514442
ARI1A_HUMANARID1Aphysical
28514442
ACL6B_HUMANACTL6Bphysical
28514442
BCL7C_HUMANBCL7Cphysical
28514442
KLH23_HUMANKLHL23physical
28514442
SMCE1_HUMANSMARCE1physical
28514442
TWF2_HUMANTWF2physical
28514442
SMRC1_HUMANSMARCC1physical
28514442
EMC8_HUMANEMC8physical
28514442
MYO1B_HUMANMYO1Bphysical
28514442
ACTBL_HUMANACTBL2physical
28514442
ACL6A_HUMANACTL6Aphysical
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 BCL7A_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-154; SER-186; SER-203AND SER-207, AND MASS SPECTROMETRY.

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