dbPTM

YBOX2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	YBOX2_HUMAN
UniProt AC	Q9Y2T7
Protein Name	Y-box-binding protein 2
Gene Name	YBX2
Organism	Homo sapiens (Human).
Sequence Length	364
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Major constituent of messenger ribonucleoprotein particles (mRNPs). Involved in the regulation of the stability and/or translation of germ cell mRNAs. Binds to Y-box consensus promoter element. Binds to full-length mRNA with high affinity in a sequence-independent manner. Binds to short RNA sequences containing the consensus site 5'-UCCAUCA-3' with low affinity and limited sequence specificity. Its binding with maternal mRNAs is necessary for its cytoplasmic retention. May mark specific mRNAs (those transcribed from Y-box promoters) in the nucleus for cytoplasmic storage, thereby linking transcription and mRNA storage/translational delay (By similarity)..
Protein Sequence	MSEVEAAAGATAVPAATVPATAAGVVAVVVPVPAGEPQKGGGAGGGGGAASGPAAGTPSAPGSRTPGNPATAVSGTPAPPARSQADKPVLAIQVLGTVKWFNVRNGYGFINRNDTKEDVFVHQTAIKRNNPRKFLRSVGDGETVEFDVVEGEKGAEATNVTGPGGVPVKGSRYAPNRRKSRRFIPRPPSVAPPPMVAEIPSAGTGPGSKGERAEDSGQRPRRWCPPPFFYRRRFVRGPRPPNQQQPIEGTDRVEPKETAPLEGHQQQGDERVPPPRFRPRYRRPFRPRPRQQPTTEGGDGETKPSQGPADGSRPEPQRPRNRPYFQRRRQQAPGPQQAPGPRQPAAPETSAPVNSGDPTTTILE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSEVEAAAG ------CCHHHHHCC	50.80	28348404
57	Phosphorylation	ASGPAAGTPSAPGSR CCCCCCCCCCCCCCC	14.89	21712546
65	Phosphorylation	PSAPGSRTPGNPATA CCCCCCCCCCCCCCC	36.93	25849741
71	Phosphorylation	RTPGNPATAVSGTPA CCCCCCCCCCCCCCC	28.93	24719451
74	Phosphorylation	GNPATAVSGTPAPPA CCCCCCCCCCCCCCC	34.19	23312004
76	Phosphorylation	PATAVSGTPAPPARS CCCCCCCCCCCCCCC	14.58	25849741
83	Phosphorylation	TPAPPARSQADKPVL CCCCCCCCCCCCCEE	31.65	24719451
99	Acetylation	IQVLGTVKWFNVRNG EEEEEEEEEEECCCC	46.00	7216853
99	Ubiquitination	IQVLGTVKWFNVRNG EEEEEEEEEEECCCC	46.00	21890473
107	Phosphorylation	WFNVRNGYGFINRND EEECCCCEEEECCCC	16.65	28152594
115	Phosphorylation	GFINRNDTKEDVFVH EEECCCCCCCCEEEE	39.62	27050516
116	Acetylation	FINRNDTKEDVFVHQ EECCCCCCCCEEEEH	55.57	22644183
116	Ubiquitination	FINRNDTKEDVFVHQ EECCCCCCCCEEEEH	55.57	21890473
127	Ubiquitination	FVHQTAIKRNNPRKF EEEHHHHHCCCHHHH	46.76	-
137	Phosphorylation	NPRKFLRSVGDGETV CHHHHHHHCCCCCEE	32.38	19664994
143	Phosphorylation	RSVGDGETVEFDVVE HHCCCCCEEEEEEEE	30.75	30266825
158	Phosphorylation	GEKGAEATNVTGPGG CCCCCEEECCCCCCC	23.02	24719451
161	Phosphorylation	GAEATNVTGPGGVPV CCEEECCCCCCCCCC	39.46	24719451
189	Phosphorylation	RFIPRPPSVAPPPMV CCCCCCCCCCCCCEE	33.33	25849741
201	Phosphorylation	PMVAEIPSAGTGPGS CEEEECCCCCCCCCC	45.02	26074081
204	Phosphorylation	AEIPSAGTGPGSKGE EECCCCCCCCCCCCC	39.66	26074081
208	Phosphorylation	SAGTGPGSKGERAED CCCCCCCCCCCCCCC	40.39	26074081
250	Phosphorylation	QQQPIEGTDRVEPKE CCCCCCCCCCCCCCC	14.08	-
324	Phosphorylation	QRPRNRPYFQRRRQQ CCCCCCHHHHHHHHC	14.76	-

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
115	T	Phosphorylation	Kinase	CHEK1	O14757	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of YBOX2_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 YBOX2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of YBOX2_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 YBOX2_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-116, AND MASS SPECTROMETRY.	19608861 [Abstract]