MCAF2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MCAF2_HUMAN
• UniProt AC: Q5U623
• Protein Name: Activating transcription factor 7-interacting protein 2
• Gene Name: ATF7IP2
• Organism: Homo sapiens (Human).
• Sequence Length: 682
• Subcellular Localization: Nucleus.
• Protein Description: Recruiter that couples transcriptional factors to general transcription apparatus and thereby modulates transcription regulation and chromatin formation. Can both act as an activator or a repressor depending on the context. Mediates MBD1-dependent transcriptional repression, probably by recruiting complexes containing SETDB1. The complex formed with MBD1 and SETDB1 represses transcription and probably couples DNA methylation and histone H3 'Lys-9' trimethylation (H3K9me3) activity (Probable)..
• Protein Sequence: MASPDRSKRKILKAKKTMPLSCRKQVEMLNKSRNVEALKTAIGSNVPSGNQSFSPSVITRTTEITKCSPSENGASSLDSNKNSISEKSKVFSQNCIKPVEEIVHSETKLEQVVCSYQKPSRTTESPSRVFTEEAKDSLNTSENDSEHQTNVTRSLFEHEGACSLKSSCCPPSVLSGVVQMPESTVTSTVGDKKTDQMVFHLETNSNSESHDKRQSDNILCSEDSGFVPVEKTPNLVNSVTSNNCADDILKTDECSRTSISNCESADSTWQSSLDTNNNSHYQKKRMFSENEENVKRMKTSEQINENICVSLERQTAFLEQVRHLIQQEIYSINYELFDKKLKELNQRIGKTECRNKHEGIADKLLAKIAKLQRRIKTVLLFQRNCLKPNMLSSNGASKVANSEAMILDKNLESVNSPIEKSSVNYEPSNPSEKGSKKINLSSDQNKSVSESNNDDVMLISVESPNLTTPITSNPTDTRKITSGNSSNSPNAEVMAVQKKLDSIIDLTKEGLSNCNTESPVSPLESHSKAASNSKETTPLAQNAVQVPESFEHLPPLPEPPAPLPELVDKTRDTLPPQKPELKVKRVFRPNGIALTWNITKINPKCAPVESYHLFLCHENSNNKLIWKKIGEIKALPLPMACTLSQFLASNRYYFTVQSKDIFGRYGPFCDIKSIPGFSENLT

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
3	Phosphorylation	-----MASPDRSKRK -----CCCCHHHHHH	26.49	29083192
7	Phosphorylation	-MASPDRSKRKILKA -CCCCHHHHHHHHHH	44.16	29083192
52	Phosphorylation	NVPSGNQSFSPSVIT CCCCCCCCCCCEEEE	31.52	28787133
54	Phosphorylation	PSGNQSFSPSVITRT CCCCCCCCCEEEEEE	22.85	29759185
56	Phosphorylation	GNQSFSPSVITRTTE CCCCCCCEEEEEECE	25.59	29759185
59	Phosphorylation	SFSPSVITRTTEITK CCCCEEEEEECEEEE	21.58	29759185
122	Phosphorylation	SYQKPSRTTESPSRV HCCCCCCCCCCCCCC	38.97	23186163
123	Phosphorylation	YQKPSRTTESPSRVF CCCCCCCCCCCCCCC	33.10	23186163
125	Phosphorylation	KPSRTTESPSRVFTE CCCCCCCCCCCCCCH	26.53	28450419
127	Phosphorylation	SRTTESPSRVFTEEA CCCCCCCCCCCCHHH	50.81	23186163
131	Phosphorylation	ESPSRVFTEEAKDSL CCCCCCCCHHHHHHC	30.02	23186163
140	Phosphorylation	EAKDSLNTSENDSEH HHHHHCCCCCCCHHH	42.59	28348404
141	Phosphorylation	AKDSLNTSENDSEHQ HHHHCCCCCCCHHHH	33.07	28348404
257	Phosphorylation	KTDECSRTSISNCES HCCCCCCCCHHCCCC	17.70	-
258	Phosphorylation	TDECSRTSISNCESA CCCCCCCCHHCCCCC	23.94	-
279	Phosphorylation	SLDTNNNSHYQKKRM CCCCCCCHHHHHHHC	26.20	-
310	Phosphorylation	INENICVSLERQTAF HHHCCCCCHHHHHHH	21.80	24719451
330	Phosphorylation	HLIQQEIYSINYELF HHHHHHHHHHCHHHH	11.62	27732954
331	Phosphorylation	LIQQEIYSINYELFD HHHHHHHHHCHHHHH	15.26	27732954
334	Phosphorylation	QEIYSINYELFDKKL HHHHHHCHHHHHHHH	16.61	27732954
363	Ubiquitination	KHEGIADKLLAKIAK CCCCHHHHHHHHHHH	36.06	29967540
392	Phosphorylation	CLKPNMLSSNGASKV CCCHHHCCCCCCCHH	15.81	23403867
393	Phosphorylation	LKPNMLSSNGASKVA CCHHHCCCCCCCHHH	35.01	23403867
397	Phosphorylation	MLSSNGASKVANSEA HCCCCCCCHHHCCCE	29.12	23403867
413	Phosphorylation	ILDKNLESVNSPIEK EECCCHHHCCCCCHH	29.75	23186163
416	Phosphorylation	KNLESVNSPIEKSSV CCHHHCCCCCHHHCC	25.71	28348404
468	Phosphorylation	VESPNLTTPITSNPT EECCCCCCCCCCCCC	18.83	32142685
477	Phosphorylation	ITSNPTDTRKITSGN CCCCCCCCCCCCCCC	36.02	32142685
481	Phosphorylation	PTDTRKITSGNSSNS CCCCCCCCCCCCCCC	33.35	23186163
482	Phosphorylation	TDTRKITSGNSSNSP CCCCCCCCCCCCCCC	39.18	23186163
485	Phosphorylation	RKITSGNSSNSPNAE CCCCCCCCCCCCCHH	34.13	23186163
486	Phosphorylation	KITSGNSSNSPNAEV CCCCCCCCCCCCHHH	45.38	23186163
488	Phosphorylation	TSGNSSNSPNAEVMA CCCCCCCCCCHHHHH	22.83	28450419
502	Phosphorylation	AVQKKLDSIIDLTKE HHHHHHHHHHHHHHH	31.70	19651622
507	Phosphorylation	LDSIIDLTKEGLSNC HHHHHHHHHHHHHCC	24.25	19651622
518	Phosphorylation	LSNCNTESPVSPLES HHCCCCCCCCCCCHH	28.67	23186163
521	Phosphorylation	CNTESPVSPLESHSK CCCCCCCCCCHHHHC	27.44	25849741
525	Phosphorylation	SPVSPLESHSKAASN CCCCCCHHHHCHHCC	40.52	23186163
527	Phosphorylation	VSPLESHSKAASNSK CCCCHHHHCHHCCCC	33.01	23186163
570	Phosphorylation	LPELVDKTRDTLPPQ CHHHHHCCCCCCCCC	29.34	24719451
665	Phosphorylation	SKDIFGRYGPFCDIK CCCCCCCCCCCCCCC	29.54	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of MCAF2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MCAF2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of MCAF2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MBD1_HUMAN	MBD1	physical	15691849
SETB1_HUMAN	SETDB1	physical	15691849
SP1_HUMAN	SP1	physical	15691849

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND MASSSPECTROMETRY.
PubMed: 19413330