dbPTM

HXB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HXB2_HUMAN
UniProt AC	P14652
Protein Name	Homeobox protein Hox-B2
Gene Name	HOXB2
Organism	Homo sapiens (Human).
Sequence Length	356
Subcellular Localization	Nucleus.
Protein Description	Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis..
Protein Sequence	MNFEFEREIGFINSQPSLAECLTSFPAVLETFQTSSIKESTLIPPPPPFEQTFPSLQPGASTLQRPRSQKRAEDGPALPPPPPPPLPAAPPAPEFPWMKEKKSAKKPSQSATSPSPAASAVPASGVGSPADGLGLPEAGGGGARRLRTAYTNTQLLELEKEFHFNKYLCRPRRVEIAALLDLTERQVKVWFQNRRMKHKRQTQHREPPDGEPACPGALEDICDPAEEPAASPGGPSASRAAWEACCHPPEVVPGALSADPRPLAVRLEGAGASSPGCALRGAGGLEPGPLPEDVFSGRQDSPFLPDLNFFAADSCLQLSGGLSPSLQGSLDSPVPFSEEELDFFTSTLCAIDLQFP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
52	Phosphorylation	PPPPFEQTFPSLQPG CCCCHHHCCCCCCCC	30.25	22817900
55	Phosphorylation	PFEQTFPSLQPGAST CHHHCCCCCCCCCCC	35.13	22817900
119	Phosphorylation	TSPSPAASAVPASGV CCCCCCHHCCCCCCC	31.72	19007248
124	Phosphorylation	AASAVPASGVGSPAD CHHCCCCCCCCCCCC	28.13	19007248
148	Phosphorylation	GGARRLRTAYTNTQL CHHHHHHHCCCHHHH	28.71	-
150	Phosphorylation	ARRLRTAYTNTQLLE HHHHHHCCCHHHHHH	10.42	22210691
151	Phosphorylation	RRLRTAYTNTQLLEL HHHHHCCCHHHHHHH	29.35	22210691
153	Phosphorylation	LRTAYTNTQLLELEK HHHCCCHHHHHHHHH	16.88	-
273	Phosphorylation	RLEGAGASSPGCALR EEECCCCCCCCCCCC	35.83	23186163
274	Phosphorylation	LEGAGASSPGCALRG EECCCCCCCCCCCCC	25.44	25850435

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 HXB2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HXB2_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 HXB2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of HXB2_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 HXB2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-124, ANDMASS SPECTROMETRY.	19007248 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-52, AND MASSSPECTROMETRY.	18187866 [Abstract]