dbPTM

ANR54_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ANR54_HUMAN
UniProt AC	Q6NXT1
Protein Name	Ankyrin repeat domain-containing protein 54
Gene Name	ANKRD54
Organism	Homo sapiens (Human).
Sequence Length	300
Subcellular Localization	Nucleus. Cytoplasm. Midbody. Shuttles between nucleus and cytoplasm during the cell cycle. EPO stimulation induces nuclear accumulation (By similarity)..
Protein Description	Plays an important role in regulating intracellular signaling events associated with erythroid terminal differentiation..
Protein Sequence	MAAAAGDADDEPRSGHSSSEGECAVAPEPLTDAEGLFSFADFGSALGGGGAGLSGRASGGAQSPLRYLHVLWQQDAEPRDELRCKIPAGRLRRAARPHRRLGPTGKEVHALKRLRDSANANDVETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQRDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSKLNILQEGHAQCLEAVRLEVKQIIHMLREYLERLGQHEQRERLDDLCTRLQMTSTKEQVDEVTDLLASFTSLSLQMQSMEKR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAAGDAD ------CCCCCCCCC	13.05	19413330
6 (in isoform 2)	Phosphorylation	-	26.39	24043423
7 (in isoform 2)	Phosphorylation	-	41.94	29116813
13 (in isoform 2)	Phosphorylation	-	53.90	29116813
14	Phosphorylation	DADDEPRSGHSSSEG CCCCCCCCCCCCCCC	52.12	24144214
17	Phosphorylation	DEPRSGHSSSEGECA CCCCCCCCCCCCCEE	38.80	24144214
18	Phosphorylation	EPRSGHSSSEGECAV CCCCCCCCCCCCEEE	27.08	24144214
19	Phosphorylation	PRSGHSSSEGECAVA CCCCCCCCCCCEEEC	53.27	24144214
31	Phosphorylation	AVAPEPLTDAEGLFS EECCCCCCCCCCCCC	43.83	24144214
38	Phosphorylation	TDAEGLFSFADFGSA CCCCCCCCHHHHHHC	25.27	24144214
44	Phosphorylation	FSFADFGSALGGGGA CCHHHHHHCCCCCCC	21.95	24144214
54	Phosphorylation	GGGGAGLSGRASGGA CCCCCCCCCCCCCCC	25.89	24144214
58	Phosphorylation	AGLSGRASGGAQSPL CCCCCCCCCCCCCHH	36.08	23927012
63	Phosphorylation	RASGGAQSPLRYLHV CCCCCCCCHHHHHHH	25.93	29255136
67	Phosphorylation	GAQSPLRYLHVLWQQ CCCCHHHHHHHHHHC	14.61	22199227
85	Ubiquitination	PRDELRCKIPAGRLR CCHHHCCCCCHHHHH	45.34	29967540
90	Methylation	RCKIPAGRLRRAARP CCCCCHHHHHHHCCC	27.42	-
106	Ubiquitination	RRLGPTGKEVHALKR CCCCCCHHHHHHHHH	60.07	33845483
106	Acetylation	RRLGPTGKEVHALKR CCCCCCHHHHHHHHH	60.07	26051181
112	Ubiquitination	GKEVHALKRLRDSAN HHHHHHHHHHHHCCC	50.61	29967540
142	Ubiquitination	DPCAADDKGRTALHF CCCCCCCCCCEEEEE	51.33	29967540
217	Ubiquitination	RTPLHLAKSKLNILQ CCHHHHHHHHHHHHH	55.26	33845483
217	Acetylation	RTPLHLAKSKLNILQ CCHHHHHHHHHHHHH	55.26	25953088
218	Phosphorylation	TPLHLAKSKLNILQE CHHHHHHHHHHHHHH	36.45	82900693
219	Ubiquitination	PLHLAKSKLNILQEG HHHHHHHHHHHHHHH	44.86	29967540
239	Acetylation	EAVRLEVKQIIHMLR HHHHHHHHHHHHHHH	26.80	25953088
266	Phosphorylation	ERLDDLCTRLQMTST HHHHHHHHHHHCCCC	41.53	24275569
271	Phosphorylation	LCTRLQMTSTKEQVD HHHHHHCCCCHHHHH	21.93	24275569
286	Phosphorylation	EVTDLLASFTSLSLQ HHHHHHHHHHHHHHH	29.09	24275569
288	Phosphorylation	TDLLASFTSLSLQMQ HHHHHHHHHHHHHHH	26.68	24275569
289	Phosphorylation	DLLASFTSLSLQMQS HHHHHHHHHHHHHHH	17.60	24275569

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 ANR54_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ANR54_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 ANR54_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ANR54_HUMAN !!

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 ANR54_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASSSPECTROMETRY.	18691976 [Abstract]