dbPTM

AN32B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AN32B_HUMAN
UniProt AC	Q92688
Protein Name	Acidic leucine-rich nuclear phosphoprotein 32 family member B
Gene Name	ANP32B
Organism	Homo sapiens (Human).
Sequence Length	251
Subcellular Localization	Isoform 1: Nucleus. Accumulates in the nuclei at the S phase.. Isoform 2: Cytoplasm. Lacks a nuclear localization signal.
Protein Description	Multifunctional protein working as a cell cycle progression factor as well as a cell survival factor. Required for the progression from the G1 to the S phase. Anti-apoptotic protein which functions as a caspase-3 inhibitor. Has no phosphatase 2A (PP2A) inhibitor activity (By similarity). Exhibits histone chaperone properties, stimulating core histones to assemble into a nucleosome..
Protein Sequence	MDMKRRIHLELRNRTPAAVRELVLDNCKSNDGKIEGLTAEFVNLEFLSLINVGLISVSNLPKLPKLKKLELSENRIFGGLDMLAEKLPNLTHLNLSGNKLKDISTLEPLKKLECLKSLDLFNCEVTNLNDYRESVFKLLPQLTYLDGYDREDQEAPDSDAEVDGVDEEEEDEEGEDEEDEDDEDGEEEEFDEEDDEDEDVEGDEDDDEVSEEEEEFGLDEEDEDEDEDEEEEEGGKGEKRKRETDDEGEDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Methylation	RRIHLELRNRTPAAV HHHHHHHHCCCHHHH	22.62	-
15	Phosphorylation	HLELRNRTPAAVREL HHHHHCCCHHHHHHH	22.34	20068231
27	S-nitrosylation	RELVLDNCKSNDGKI HHHHHHHHHCCCCCE	5.23	2212679
28	Acetylation	ELVLDNCKSNDGKIE HHHHHHHHCCCCCEE	59.56	25953088
28	Ubiquitination	ELVLDNCKSNDGKIE HHHHHHHHCCCCCEE	59.56	33845483
33	Acetylation	NCKSNDGKIEGLTAE HHHCCCCCEECEEEE	40.21	11921455
67	Ubiquitination	LPKLPKLKKLELSEN CCCCCCCCCCCCCCC	62.53	-
68	Sumoylation	PKLPKLKKLELSENR CCCCCCCCCCCCCCC	58.59	-
68	Ubiquitination	PKLPKLKKLELSENR CCCCCCCCCCCCCCC	58.59	29967540
68	Sumoylation	PKLPKLKKLELSENR CCCCCCCCCCCCCCC	58.59	-
72	Phosphorylation	KLKKLELSENRIFGG CCCCCCCCCCCCCCH	24.37	20873877
75	Methylation	KLELSENRIFGGLDM CCCCCCCCCCCHHHH	22.89	-
82	Sulfoxidation	RIFGGLDMLAEKLPN CCCCHHHHHHHHCCC	4.61	21406390
86	Ubiquitination	GLDMLAEKLPNLTHL HHHHHHHHCCCCCEE	64.73	19608861
86	Acetylation	GLDMLAEKLPNLTHL HHHHHHHHCCCCCEE	64.73	19608861
96	Phosphorylation	NLTHLNLSGNKLKDI CCCEEECCCCCCCCH	38.97	20873877
99	Acetylation	HLNLSGNKLKDISTL EEECCCCCCCCHHHC	61.51	23749302
99	Ubiquitination	HLNLSGNKLKDISTL EEECCCCCCCCHHHC	61.51	23000965
99 (in isoform 2)	Ubiquitination	-	61.51	21890473
99 (in isoform 1)	Ubiquitination	-	61.51	21890473
99	Malonylation	HLNLSGNKLKDISTL EEECCCCCCCCHHHC	61.51	26320211
101	Malonylation	NLSGNKLKDISTLEP ECCCCCCCCHHHCHH	55.41	26320211
101	Acetylation	NLSGNKLKDISTLEP ECCCCCCCCHHHCHH	55.41	23954790
101	Ubiquitination	NLSGNKLKDISTLEP ECCCCCCCCHHHCHH	55.41	23000965
101 (in isoform 1)	Ubiquitination	-	55.41	21890473
101 (in isoform 2)	Ubiquitination	-	55.41	21890473
104	Phosphorylation	GNKLKDISTLEPLKK CCCCCCHHHCHHHHH	36.75	21815630
105	Phosphorylation	NKLKDISTLEPLKKL CCCCCHHHCHHHHHH	35.16	21815630
110	Acetylation	ISTLEPLKKLECLKS HHHCHHHHHHHHHHH	67.06	23749302
110	Malonylation	ISTLEPLKKLECLKS HHHCHHHHHHHHHHH	67.06	32601280
110	Ubiquitination	ISTLEPLKKLECLKS HHHCHHHHHHHHHHH	67.06	32142685
111	Ubiquitination	STLEPLKKLECLKSL HHCHHHHHHHHHHHC	58.14	-
111	Acetylation	STLEPLKKLECLKSL HHCHHHHHHHHHHHC	58.14	25953088
116	Acetylation	LKKLECLKSLDLFNC HHHHHHHHHCCCCCC	61.71	25953088
116	Ubiquitination	LKKLECLKSLDLFNC HHHHHHHHHCCCCCC	61.71	29967540
117	Phosphorylation	KKLECLKSLDLFNCE HHHHHHHHCCCCCCE	17.73	20873877
123	Glutathionylation	KSLDLFNCEVTNLND HHCCCCCCEECCHHH	3.31	22555962
123	S-palmitoylation	KSLDLFNCEVTNLND HHCCCCCCEECCHHH	3.31	26865113
126	Phosphorylation	DLFNCEVTNLNDYRE CCCCCEECCHHHHHH	16.22	21406692
131	Phosphorylation	EVTNLNDYRESVFKL EECCHHHHHHHHHHH	18.40	21406692
134	Phosphorylation	NLNDYRESVFKLLPQ CHHHHHHHHHHHHHH	24.69	26552605
137	Ubiquitination	DYRESVFKLLPQLTY HHHHHHHHHHHHHHC	47.13	32015554
143	Phosphorylation	FKLLPQLTYLDGYDR HHHHHHHHCCCCCCC	19.45	26356563
144	Phosphorylation	KLLPQLTYLDGYDRE HHHHHHHCCCCCCCC	16.04	26356563
148	Phosphorylation	QLTYLDGYDREDQEA HHHCCCCCCCCCCCC	16.11	25884760
158	Phosphorylation	EDQEAPDSDAEVDGV CCCCCCCCCCCCCCC	37.35	19529061
236	Acetylation	EEEEEGGKGEKRKRE HHHHCCCCCCCCCCC	74.81	30584399
239	Acetylation	EEGGKGEKRKRETDD HCCCCCCCCCCCCCC	72.40	155627
244	Phosphorylation	GEKRKRETDDEGEDD CCCCCCCCCCCCCCC	53.43	29255136

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
244	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AN32B_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 AN32B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
HNF4A_HUMAN	HNF4A	physical	21988832
IMA5_HUMAN	KPNA1	physical	21988832
SMRD1_HUMAN	SMARCD1	physical	21988832
ARP2_HUMAN	ACTR2	physical	22863883
ARP3_HUMAN	ACTR3	physical	22863883
ARC1B_HUMAN	ARPC1B	physical	22863883
ARPC2_HUMAN	ARPC2	physical	22863883
GRPE1_HUMAN	GRPEL1	physical	22863883
RFA1_HUMAN	RPA1	physical	22863883
SH3G1_HUMAN	SH3GL1	physical	22863883
SAHH2_HUMAN	AHCYL1	physical	26344197
SAHH3_HUMAN	AHCYL2	physical	26344197
DMAP1_HUMAN	DMAP1	physical	26344197
VPS72_HUMAN	VPS72	physical	26344197
KLF5_HUMAN	KLF5	physical	18039846
H2A1A_HUMAN	HIST1H2AA	physical	18039846
H2B1A_HUMAN	HIST1H2BA	physical	18039846
H31_HUMAN	HIST1H3A	physical	18039846
ELAV1_HUMAN	ELAVL1	physical	11565755
XPO1_HUMAN	XPO1	physical	11565755
IMA6_HUMAN	KPNA5	physical	21516116
FAM3A_HUMAN	FAM3A	physical	21516116

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 AN32B_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-86, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, AND MASSSPECTROMETRY.	18318008 [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 THR-244, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, AND MASSSPECTROMETRY.	16094384 [Abstract]