BANP_HUMAN - dbPTM
BANP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BANP_HUMAN
UniProt AC Q8N9N5
Protein Name Protein BANP
Gene Name BANP
Organism Homo sapiens (Human).
Sequence Length 519
Subcellular Localization Nucleus .
Protein Description Controls V(D)J recombination during T-cell development by repressing T-cell receptor (TCR) beta enhancer function. Binds to scaffold/matrix attachment region beta (S/MARbeta), an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Represses cyclin D1 transcription by recruiting HDAC1 to its promoter, thereby diminishing H3K9ac, H3S10ph and H4K8ac levels. Promotes TP53 'Ser-15' phosphorylation and nuclear accumulation, which causes cell cycle arrest (By similarity)..
Protein Sequence MMSEHDLADVVQIAVEDLSPDHPVVLENHVVTDEDEPALKRQRLEINCQDPSIKTICLRLDSIEAKLQALEATCKSLEEKLDLVTNKQHSPIQVPMVAGSPLGATQTCNKVRCVVPQTTVILNNDRQNAIVAKMEDPLSNRAPDSLENVISNAVPGRRQNTIVVKVPGQEDSHHEDGESGSEASDSVSSCGQAGSQSIGSNVTLITLNSEEDYPNGTWLGDENNPEMRVRCAIIPSDMLHISTNCRTAEKMALTLLDYLFHREVQAVSNLSGQGKHGKKQLDPLTIYGIRCHLFYKFGITESDWYRIKQSIDSKCRTAWRRKQRGQSLAVKSFSRRTPNSSSYCPSEPMMSTPPPASELPQPQPQPQALHYALANAQQVQIHQIGEDGQVQVGHLHIAQVPQGEQVQITQDSEGNLQIHHVGQDGQLLEATRIPCLLAPSVFKASSGQVLQGAQLIAVASSDPAAAGVDGSPLQGSDIQVQYVQLAPVSDHTAGAQTAEALQPTLQPEMQLEHGAIQIQ
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
19PhosphorylationQIAVEDLSPDHPVVL
HHHHHHCCCCCCEEE
40.3726074081
32PhosphorylationVLENHVVTDEDEPAL
EEECCEECCCCCHHH
32.3626074081
55PhosphorylationCQDPSIKTICLRLDS
CCCCCHHHHEEEHHH
18.4326074081
62PhosphorylationTICLRLDSIEAKLQA
HHEEEHHHHHHHHHH
27.2426074081
73PhosphorylationKLQALEATCKSLEEK
HHHHHHHHHHHHHHH
15.8726074081
75UbiquitinationQALEATCKSLEEKLD
HHHHHHHHHHHHHHH
54.44-
80UbiquitinationTCKSLEEKLDLVTNK
HHHHHHHHHHHHCCC
37.62-
85PhosphorylationEEKLDLVTNKQHSPI
HHHHHHHCCCCCCCC
43.9521712546
87UbiquitinationKLDLVTNKQHSPIQV
HHHHHCCCCCCCCCC
39.77-
89 (in isoform 3)Phosphorylation-36.8320068231
90PhosphorylationLVTNKQHSPIQVPMV
HHCCCCCCCCCCCEE
22.6223401153
91 (in isoform 3)Phosphorylation-20.9320068231
100PhosphorylationQVPMVAGSPLGATQT
CCCEECCCCCCCCCC
13.7623401153
105PhosphorylationAGSPLGATQTCNKVR
CCCCCCCCCCCCEEE
23.7130108239
107PhosphorylationSPLGATQTCNKVRCV
CCCCCCCCCCEEEEE
17.4330108239
113 (in isoform 4)Phosphorylation-3.9720068231
113 (in isoform 2)Phosphorylation-3.9720068231
113 (in isoform 6)Phosphorylation-3.9720068231
115 (in isoform 4)Phosphorylation-3.1320068231
115 (in isoform 6)Phosphorylation-3.1320068231
115 (in isoform 2)Phosphorylation-3.1320068231
119 (in isoform 5)Phosphorylation-10.5720068231
121 (in isoform 5)Phosphorylation-2.9820068231
133SumoylationRQNAIVAKMEDPLSN
CCCEEEEECCCCHHC
31.7428112733
133UbiquitinationRQNAIVAKMEDPLSN
CCCEEEEECCCCHHC
31.74-
139PhosphorylationAKMEDPLSNRAPDSL
EECCCCHHCCCCCHH
29.6520058876
145PhosphorylationLSNRAPDSLENVISN
HHCCCCCHHHHHHHH
36.2025849741
151PhosphorylationDSLENVISNAVPGRR
CHHHHHHHHCCCCCC
17.91-
275UbiquitinationSNLSGQGKHGKKQLD
HCCCCCCCCCCCCCC
41.1019608861
275AcetylationSNLSGQGKHGKKQLD
HCCCCCCCCCCCCCC
41.1026051181
278UbiquitinationSGQGKHGKKQLDPLT
CCCCCCCCCCCCCEE
36.75-
279UbiquitinationGQGKHGKKQLDPLTI
CCCCCCCCCCCCEEE
61.76-
287PhosphorylationQLDPLTIYGIRCHLF
CCCCEEEEEEEEEEE
10.98-
308UbiquitinationESDWYRIKQSIDSKC
HHHHHHHHHHHCHHH
29.06-
324MethylationTAWRRKQRGQSLAVK
HHHHHHHHCCCEEEE
48.42-
327PhosphorylationRRKQRGQSLAVKSFS
HHHHHCCCEEEEECC
22.56-
331UbiquitinationRGQSLAVKSFSRRTP
HCCCEEEEECCCCCC
39.93-
331AcetylationRGQSLAVKSFSRRTP
HCCCEEEEECCCCCC
39.9325953088
334PhosphorylationSLAVKSFSRRTPNSS
CEEEEECCCCCCCCC
28.1317081983
337PhosphorylationVKSFSRRTPNSSSYC
EEECCCCCCCCCCCC
26.22-
352PhosphorylationPSEPMMSTPPPASEL
CCCCCCCCCCCHHHC
23.17-

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
337TPhosphorylationKinaseMAPK1P28482
GPS
337TPhosphorylationKinaseMAPK3P27361
GPS
352TPhosphorylationKinaseMAPK1P28482
GPS
352TPhosphorylationKinaseMAPK3P27361
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BANP_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 BANP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
19303885
MDM2_HUMANMDM2physical
19303885
TF65_HUMANRELAphysical
18981184
NFKB1_HUMANNFKB1physical
18981184
HDAC1_HUMANHDAC1physical
20075864
P53_HUMANTP53physical
20075864
PML_HUMANPMLphysical
20075864
FOXM1_HUMANFOXM1physical
21988832
MDM2_HUMANMDM2physical
25086032
HDAC1_HUMANHDAC1physical
25086032
P53_HUMANTP53physical
22074660
PARP1_HUMANPARP1physical
22074660
EP300_HUMANEP300physical
22074660
BANP_HUMANBANPphysical
25416956
PRP39_HUMANPRPF39physical
25416956
PCLI1_HUMANPID1physical
25416956
F90A1_HUMANFAM90A1physical
25416956
DNJA4_HUMANDNAJA4physical
25416956
LMO3_HUMANLMO3physical
25416956
PPL13_HUMANLGALS14physical
25416956
ZN471_HUMANZNF471physical
25416956
LSM2_HUMANLSM2physical
25416956
LENG1_HUMANLENG1physical
25416956
ZC21C_HUMANZC2HC1Cphysical
25416956
CEP76_HUMANCEP76physical
25416956
ZMIZ2_HUMANZMIZ2physical
25416956
NRIP2_HUMANNRIP2physical
25416956
PDIP3_HUMANPOLDIP3physical
25416956
RRF2M_HUMANGFM2physical
25416956
LMBL3_HUMANL3MBTL3physical
25416956
CA094_HUMANC1orf94physical
25416956
RAB3I_HUMANRAB3IPphysical
25416956
ZN488_HUMANZNF488physical
25416956
CV039_HUMANC22orf39physical
25416956
DCD2B_HUMANDCDC2Bphysical
25416956
F117B_HUMANFAM117Bphysical
25416956
SH3R2_HUMANSH3RF2physical
25416956
CF206_HUMANC6orf165physical
25416956
FA71C_HUMANFAM71Cphysical
25416956
AFG1L_HUMANLACE1physical
25416956
FOXR1_HUMANFOXR1physical
25416956
EPHAA_HUMANEPHA10physical
25416956
KHDR1_HUMANKHDRBS1physical
26080397
HDAC6_HUMANHDAC6physical
26080397
SP2_HUMANSP2physical
21516116
TENX_HUMANTNXBphysical
21516116
RRFM_HUMANMRRFphysical
21516116
XRCC6_HUMANXRCC6physical
25299772
HDAC6_HUMANHDAC6physical
25299772
H2AX_HUMANH2AFXphysical
25299772
ATM_HUMANATMphysical
25299772
CDC20_HUMANCDC20physical
28617439
MK08_HUMANMAPK8physical
28617439

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 BANP_HUMAN

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Related Literatures of Post-Translational Modification

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