dbPTM

BEND3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BEND3_HUMAN
UniProt AC	Q5T5X7
Protein Name	BEN domain-containing protein 3
Gene Name	BEND3
Organism	Homo sapiens (Human).
Sequence Length	828
Subcellular Localization	Nucleus . Nucleus, nucleolus . In the nucleus, observed in heterochromatic foci containing CBX1, CBX3, CBX5 and histone H3 trimethylated at 'Lys-9'. Released from chromatin during decondensation. Association with heterochromatin does not depend on su
Protein Description	Transcriptional repressor which associates with the NoRC (nucleolar remodeling complex) complex and plays a key role in repressing rDNA transcription. The sumoylated form modulates the stability of the NoRC complex component BAZ2A/TIP5 by controlling its USP21-mediated deubiquitination. [PubMed: 21914818]
Protein Sequence	MNSTEFTEDVEEVLKSITVKVETEAEDAALDCSVNSRTSEKHSVDSVLTALQDSSKRKQLVSDGLLDSVPGVKRRRLIPEALLAGMRNRENSSPCQGNGEQAGRGRSLGNVWPGEEEPCNDATTPSYKKPLYGISHKIMEKKNPPSGDLLNVYELFEKANASNSPSSLRLLNEPQKRDCGSTGAGTDNDPNIYFLIQKMFYMLNTLTSNMSQLHSKVDLLSLEVSRIKKQVSPTEMVAKFQPPPEYQLTAAELKQIVDQSLSGGDLACRLLVQLFPELFSDVDFSRGCSACGFAAKRKLESLHLQLIRNYVEVYYPSVKDTAVWQAECLPQLNDFFSRFWAQREMEDSQPSGQVASFFEAEQVDPGHFLDNKDQEEALSLDRSSTIASDHVVDTQDLTEFLDEASSPGEFAVFLLHRLFPELFDHRKLGEQYSCYGDGGKQELDPQRLQIIRNYTEIYFPDMQEEEAWLQQCAQRINDELEGLGLDAGSEGDPPRDDCYDSSSLPDDISVVKVEDSFEGERPGRRSKKIWLVPIDFDKLEIPQPDFEVPGADCLLSKEQLRSIYESSLSIGNFASRLLVHLFPELFTHENLRKQYNCSGSLGKKQLDPSRIKLIRHYVQLLYPRAKNDRVWTLEFVGKLDERCRRRDTEQRRSYQQQRKVHVPGPECRDLTSYAINPERFREEFEGPPLPPERSSKDFCKIPLDELVVPSPDFPVPSPYLLSDKEVREIVQQSLSVGNFAARLLVRLFPELFTAENLRLQYNHSGACNKKQLDPTRLRLIRHYVEAVYPVEKMEEVWHYECIPSIDERCRRPNRKKCDILKKAKKVEK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MNSTEFTEDV -----CCCCCCHHHH	28.19	28348404
4	Phosphorylation	----MNSTEFTEDVE ----CCCCCCHHHHH	30.07	28348404
7	Phosphorylation	-MNSTEFTEDVEEVL -CCCCCCHHHHHHHH	25.66	25849741
16	Phosphorylation	DVEEVLKSITVKVET HHHHHHHHCEEEEEE	21.23	20068231
18	Phosphorylation	EEVLKSITVKVETEA HHHHHHCEEEEEECH	22.74	20068231
20	Sumoylation	VLKSITVKVETEAED HHHHCEEEEEECHHH	26.21	-
20	Sumoylation	VLKSITVKVETEAED HHHHCEEEEEECHHH	26.21	21914818
23	Phosphorylation	SITVKVETEAEDAAL HCEEEEEECHHHHHH	43.41	20068231
33	Phosphorylation	EDAALDCSVNSRTSE HHHHHCCCCCCCCCC	24.81	20068231
36	Phosphorylation	ALDCSVNSRTSEKHS HHCCCCCCCCCCCCC	34.48	20068231
38	Phosphorylation	DCSVNSRTSEKHSVD CCCCCCCCCCCCCHH	40.85	23090842
39	Phosphorylation	CSVNSRTSEKHSVDS CCCCCCCCCCCCHHH	43.46	23090842
41	Sumoylation	VNSRTSEKHSVDSVL CCCCCCCCCCHHHHH	40.73	28112733
41	Ubiquitination	VNSRTSEKHSVDSVL CCCCCCCCCCHHHHH	40.73	29967540
54	Phosphorylation	VLTALQDSSKRKQLV HHHHHHCCHHHHHHH	25.46	25159151
55	Phosphorylation	LTALQDSSKRKQLVS HHHHHCCHHHHHHHH	44.78	30576142
56	Sumoylation	TALQDSSKRKQLVSD HHHHCCHHHHHHHHC	68.51	28112733
56	Ubiquitination	TALQDSSKRKQLVSD HHHHCCHHHHHHHHC	68.51	29967540
58	Sumoylation	LQDSSKRKQLVSDGL HHCCHHHHHHHHCCH	52.28	28112733
62	Phosphorylation	SKRKQLVSDGLLDSV HHHHHHHHCCHHHCC	34.26	24732914
68	Phosphorylation	VSDGLLDSVPGVKRR HHCCHHHCCCCCCHH	30.13	25159151
73	Sumoylation	LDSVPGVKRRRLIPE HHCCCCCCHHHCCHH	46.21	28112733
73	Ubiquitination	LDSVPGVKRRRLIPE HHCCCCCCHHHCCHH	46.21	29967540
92	Phosphorylation	GMRNRENSSPCQGNG HHCCCCCCCCCCCCC	30.79	22115753
93	Phosphorylation	MRNRENSSPCQGNGE HCCCCCCCCCCCCCC	41.08	22617229
107	Phosphorylation	EQAGRGRSLGNVWPG CCCCCCCCCCCCCCC	43.37	25159151
123	Phosphorylation	EEPCNDATTPSYKKP CCCCCCCCCCCCCCC	41.94	28450419
124	Phosphorylation	EPCNDATTPSYKKPL CCCCCCCCCCCCCCC	16.38	28450419
126	Phosphorylation	CNDATTPSYKKPLYG CCCCCCCCCCCCCCC	47.71	28450419
127	Phosphorylation	NDATTPSYKKPLYGI CCCCCCCCCCCCCCC	25.00	28450419
128	Sumoylation	DATTPSYKKPLYGIS CCCCCCCCCCCCCCC	52.86	28112733
129	Sumoylation	ATTPSYKKPLYGISH CCCCCCCCCCCCCCH	31.83	-
129	Sumoylation	ATTPSYKKPLYGISH CCCCCCCCCCCCCCH	31.83	28112733
129	Ubiquitination	ATTPSYKKPLYGISH CCCCCCCCCCCCCCH	31.83	29967540
132	Phosphorylation	PSYKKPLYGISHKIM CCCCCCCCCCCHHHH	22.42	24719451
135	Phosphorylation	KKPLYGISHKIMEKK CCCCCCCCHHHHHHC	17.86	24719451
137	Acetylation	PLYGISHKIMEKKNP CCCCCCHHHHHHCCC	36.64	25953088
137	Sumoylation	PLYGISHKIMEKKNP CCCCCCHHHHHHCCC	36.64	28112733
142	Sumoylation	SHKIMEKKNPPSGDL CHHHHHHCCCCCCCC	62.47	28112733
142	Ubiquitination	SHKIMEKKNPPSGDL CHHHHHHCCCCCCCC	62.47	29967540
146	Phosphorylation	MEKKNPPSGDLLNVY HHHCCCCCCCCHHHH	46.31	28796482
153	Phosphorylation	SGDLLNVYELFEKAN CCCCHHHHHHHHHHC	13.07	28796482
158	Sumoylation	NVYELFEKANASNSP HHHHHHHHHCCCCCH	39.34	28112733
158	Ubiquitination	NVYELFEKANASNSP HHHHHHHHHCCCCCH	39.34	21963094
162	Phosphorylation	LFEKANASNSPSSLR HHHHHCCCCCHHHHH	37.33	30266825
164	Phosphorylation	EKANASNSPSSLRLL HHHCCCCCHHHHHHC	24.54	30266825
166	Phosphorylation	ANASNSPSSLRLLNE HCCCCCHHHHHHCCC	41.65	30266825
167	Phosphorylation	NASNSPSSLRLLNEP CCCCCHHHHHHCCCC	22.38	30266825
176	Sumoylation	RLLNEPQKRDCGSTG HHCCCCCCCCCCCCC	62.00	28112733
176	Ubiquitination	RLLNEPQKRDCGSTG HHCCCCCCCCCCCCC	62.00	29967540
181	Phosphorylation	PQKRDCGSTGAGTDN CCCCCCCCCCCCCCC	29.96	25159151
182	Phosphorylation	QKRDCGSTGAGTDND CCCCCCCCCCCCCCC	19.14	30576142
186	Phosphorylation	CGSTGAGTDNDPNIY CCCCCCCCCCCCCHH	30.97	30576142
201	Phosphorylation	FLIQKMFYMLNTLTS HHHHHHHHHHHHHHC	9.37	25072903
205	Phosphorylation	KMFYMLNTLTSNMSQ HHHHHHHHHHCCHHH	27.70	25072903
207	Phosphorylation	FYMLNTLTSNMSQLH HHHHHHHHCCHHHHH	18.93	25072903
208	Phosphorylation	YMLNTLTSNMSQLHS HHHHHHHCCHHHHHH	33.38	20068231
211	Phosphorylation	NTLTSNMSQLHSKVD HHHHCCHHHHHHHHH	33.56	25072903
215	Phosphorylation	SNMSQLHSKVDLLSL CCHHHHHHHHHHHHH	42.86	25850435
221	Phosphorylation	HSKVDLLSLEVSRIK HHHHHHHHHHHHHHH	29.76	20068231
225	Phosphorylation	DLLSLEVSRIKKQVS HHHHHHHHHHHCCCC	20.93	20068231
232	Phosphorylation	SRIKKQVSPTEMVAK HHHHCCCCCHHHHHC	24.50	23911959
234	Phosphorylation	IKKQVSPTEMVAKFQ HHCCCCCHHHHHCCC	29.25	23911959
246	Phosphorylation	KFQPPPEYQLTAAEL CCCCCCHHCCCHHHH	18.01	23911959
296	Acetylation	SACGFAAKRKLESLH CCCCHHHHHHHHHHH	46.78	25953088
301	Phosphorylation	AAKRKLESLHLQLIR HHHHHHHHHHHHHHH	31.37	26657352
310	Phosphorylation	HLQLIRNYVEVYYPS HHHHHHHHHEHHCCC	6.53	27732954
314	Phosphorylation	IRNYVEVYYPSVKDT HHHHHEHHCCCCCHH	8.99	27732954
315	Phosphorylation	RNYVEVYYPSVKDTA HHHHEHHCCCCCHHH	8.33	26657352
317	Phosphorylation	YVEVYYPSVKDTAVW HHEHHCCCCCHHHHH	26.19	27732954
348	Phosphorylation	AQREMEDSQPSGQVA HHHHCCCCCCCCCCE	30.59	29523821
351	Phosphorylation	EMEDSQPSGQVASFF HCCCCCCCCCCEEEE	33.93	29523821
356	Phosphorylation	QPSGQVASFFEAEQV CCCCCCEEEEEEEEC	31.45	21712546
379	Phosphorylation	KDQEEALSLDRSSTI CCHHHHHCCCCCCCH	34.96	19664994
383	Phosphorylation	EALSLDRSSTIASDH HHHCCCCCCCHHHCC	31.34	21406692
384	Phosphorylation	ALSLDRSSTIASDHV HHCCCCCCCHHHCCC	25.40	21406692
385	Phosphorylation	LSLDRSSTIASDHVV HCCCCCCCHHHCCCC	23.08	21406692
388	Phosphorylation	DRSSTIASDHVVDTQ CCCCCHHHCCCCCHH	25.13	21406692
394	Phosphorylation	ASDHVVDTQDLTEFL HHCCCCCHHHHHHHH	16.63	21406692
398	Phosphorylation	VVDTQDLTEFLDEAS CCCHHHHHHHHHHCC	32.74	21406692
405	Phosphorylation	TEFLDEASSPGEFAV HHHHHHCCCHHHHHH	34.71	21406692
406	Phosphorylation	EFLDEASSPGEFAVF HHHHHCCCHHHHHHH	43.93	21406692
427	Sumoylation	PELFDHRKLGEQYSC HHHHCCCHHCCCCCC	58.38	-
427	Sumoylation	PELFDHRKLGEQYSC HHHHCCCHHCCCCCC	58.38	28112733
489	Phosphorylation	GLGLDAGSEGDPPRD CCCCCCCCCCCCCCC	39.88	19664994
499	Phosphorylation	DPPRDDCYDSSSLPD CCCCCCCCCCCCCCC	26.34	23663014
501	Phosphorylation	PRDDCYDSSSLPDDI CCCCCCCCCCCCCCE	8.71	23663014
502	Phosphorylation	RDDCYDSSSLPDDIS CCCCCCCCCCCCCEE	32.75	23663014
503	Phosphorylation	DDCYDSSSLPDDISV CCCCCCCCCCCCEEE	48.12	28348404
509	Phosphorylation	SSLPDDISVVKVEDS CCCCCCEEEEEEECC	28.05	23663014
512	Sumoylation	PDDISVVKVEDSFEG CCCEEEEEEECCCCC	37.44	-
512	Sumoylation	PDDISVVKVEDSFEG CCCEEEEEEECCCCC	37.44	17000644
516	Phosphorylation	SVVKVEDSFEGERPG EEEEEECCCCCCCCC	16.22	29255136
528	Sumoylation	RPGRRSKKIWLVPID CCCCCCCEEEEEEEC	40.12	-
528	Sumoylation	RPGRRSKKIWLVPID CCCCCCCEEEEEEEC	40.12	28112733
598	Phosphorylation	LRKQYNCSGSLGKKQ HHHHHCCCCCCCCCC	27.98	26699800
600	Phosphorylation	KQYNCSGSLGKKQLD HHHCCCCCCCCCCCC	20.04	26699800
617	Phosphorylation	RIKLIRHYVQLLYPR HHHHHHHHHHHHCCC	4.69	21888424
622	Phosphorylation	RHYVQLLYPRAKNDR HHHHHHHCCCCCCCC	10.16	21888424
654	Phosphorylation	DTEQRRSYQQQRKVH CHHHHHHHHHHHCCC	14.45	-
673	Phosphorylation	ECRDLTSYAINPERF HHHHCCHHCCCHHHH	13.28	27642862
694	Phosphorylation	PPLPPERSSKDFCKI CCCCCCCCCCCCCCC	39.83	25627689
700	Sumoylation	RSSKDFCKIPLDELV CCCCCCCCCCHHHCC	47.56	28112733
700	Ubiquitination	RSSKDFCKIPLDELV CCCCCCCCCCHHHCC	47.56	29967540
710	Phosphorylation	LDELVVPSPDFPVPS HHHCCCCCCCCCCCC	26.03	29802988
717	Phosphorylation	SPDFPVPSPYLLSDK CCCCCCCCCCCCCHH	26.81	28348404
775	Phosphorylation	NKKQLDPTRLRLIRH CHHHCCHHHHHHHHH	41.84	24043423

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
-	K	Ubiquitination	E3 ubiquitin ligase	ICP0	P08393	PMID:32416261

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
20	K	Sumoylation	21914818
Sumoylated at Lys-20 by SUMO1 and at Lys-512 by SUMO1, SUMO2 and SUMO3.
20	K	Sumoylation	21914818
Sumoylation probably occurs sequentially, with that of Lys-20 preceding that of Lys-512.
512	K	Sumoylation	21914818
Sumoylated at Lys-20 by SUMO1 and at Lys-512 by SUMO1, SUMO2 and SUMO3.
512	K	Sumoylation	21914818
Sumoylation probably occurs sequentially, with that of Lys-20 preceding that of Lys-512.

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 BEND3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BEND3_HUMAN	BEND3	physical	25416956
F161A_HUMAN	FAM161A	physical	25416956
MORN4_HUMAN	MORN4	physical	25416956
BAZ2A_HUMAN	BAZ2A	physical	26100909
SMCA5_HUMAN	SMARCA5	physical	26100909
UBP21_HUMAN	USP21	physical	26100909

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 BEND3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489, AND MASSSPECTROMETRY.	17081983 [Abstract]

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