dbPTM

AN32B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AN32B_MOUSE
UniProt AC	Q9EST5
Protein Name	Acidic leucine-rich nuclear phosphoprotein 32 family member B
Gene Name	Anp32b
Organism	Mus musculus (Mouse).
Sequence Length	272
Subcellular Localization	Nucleus. Accumulates in the nuclei at the S phase..
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. Exhibits histone chaperone properties, stimulating core histones to assemble into a nucleosome (By similarity)..
Protein Sequence	MDMKRRIHLELRNRTPAAVRELVLDNCKAMDGKIEGLTDEFVNLEFLSLISVGLFSVSDLPKLPKLKKLELSENRIFGGLDRLAEELPSLTHLNLSGNNLKDISTLEPLKRLDCLKSLDLFGCEVTNRSDYRETVFRLLPQLSYLDGYDREDQEAPDSDVEVDSVEEAPDSDGEVDGVDKEEEDEEGEDEEEEEDEDGEEEEDEDEEDEDEDEDVEGEDDEDEVSGEEEEFGHDGEVDEDEEDEDEDEDEEEEESGKGEKRKRETDDEGEDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Phosphorylation	HLELRNRTPAAVREL HHHHHCCCHHHHHHH	22.34	25266776
27	S-nitrosocysteine	RELVLDNCKAMDGKI HHHHHHHHHHCCCCC	2.72	-
27	S-nitrosylation	RELVLDNCKAMDGKI HHHHHHHHHHCCCCC	2.72	24926564
68	Ubiquitination	PKLPKLKKLELSENR CCCCCCCCCCCCCCC	58.59	-
72	Phosphorylation	KLKKLELSENRIFGG CCCCCCCCCCCCCCC	24.37	29139429
81	Ubiquitination	NRIFGGLDRLAEELP CCCCCCHHHHHHHCC	46.99	27667366
89	Phosphorylation	RLAEELPSLTHLNLS HHHHHCCCCCEEECC	59.53	29139447
91	Phosphorylation	AEELPSLTHLNLSGN HHHCCCCCEEECCCC	28.75	19854140
96	Phosphorylation	SLTHLNLSGNNLKDI CCCEEECCCCCCCCC	38.10	29139435
101	Ubiquitination	NLSGNNLKDISTLEP ECCCCCCCCCHHCCH	55.96	22790023
101 (in isoform 2)	Ubiquitination	-	55.96	22790023
104	Phosphorylation	GNNLKDISTLEPLKR CCCCCCCHHCCHHHH	36.75	28066266
105	Phosphorylation	NNLKDISTLEPLKRL CCCCCCHHCCHHHHH	35.16	28066266
110	Acetylation	ISTLEPLKRLDCLKS CHHCCHHHHHHHHHH	62.72	23236377
110	Ubiquitination	ISTLEPLKRLDCLKS CHHCCHHHHHHHHHH	62.72	27667366
116	Ubiquitination	LKRLDCLKSLDLFGC HHHHHHHHHCCCCCC	56.13	-
117	Phosphorylation	KRLDCLKSLDLFGCE HHHHHHHHCCCCCCE	17.73	26643407
123	Glutathionylation	KSLDLFGCEVTNRSD HHCCCCCCEECCCHH	2.73	24333276
123	S-nitrosylation	KSLDLFGCEVTNRSD HHCCCCCCEECCCHH	2.73	20925432
123	S-palmitoylation	KSLDLFGCEVTNRSD HHCCCCCCEECCCHH	2.73	28526873
123	S-nitrosocysteine	KSLDLFGCEVTNRSD HHCCCCCCEECCCHH	2.73	-
126	Phosphorylation	DLFGCEVTNRSDYRE CCCCCEECCCHHHHH	11.56	24719451
129	Phosphorylation	GCEVTNRSDYRETVF CCEECCCHHHHHHHH	40.85	25266776
143	Phosphorylation	FRLLPQLSYLDGYDR HHHHHHHHHHCCCCC	20.57	23737553
144	Phosphorylation	RLLPQLSYLDGYDRE HHHHHHHHHCCCCCC	19.87	23737553
148	Phosphorylation	QLSYLDGYDREDQEA HHHHHCCCCCCCCCC	16.11	23737553
158	Phosphorylation	EDQEAPDSDVEVDSV CCCCCCCCCCEECCC	42.36	23737553
164	Phosphorylation	DSDVEVDSVEEAPDS CCCCEECCCEECCCC	36.28	26239621
171	Phosphorylation	SVEEAPDSDGEVDGV CCEECCCCCCCCCCC	46.59	26239621
265	Phosphorylation	GEKRKRETDDEGEDD CCCCCCCCCCCCCCC	53.43	25521595

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 AN32B_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AN32B_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of AN32B_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of AN32B_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-265, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS."; Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.; Mol. Cell. Proteomics 6:669-676(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-265, AND MASSSPECTROMETRY.	17208939 [Abstract]
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells."; Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.; J. Proteome Res. 6:3174-3186(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-265, AND MASSSPECTROMETRY.	17622165 [Abstract]