dbPTM

HPT_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HPT_MOUSE
UniProt AC	Q61646
Protein Name	Haptoglobin
Gene Name	Hp
Organism	Mus musculus (Mouse).
Sequence Length	347
Subcellular Localization	Secreted.
Protein Description	As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an antioxidant, has antibacterial activity and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidely cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation pathway (By similarity).; Uncleaved haptoglogin, also known as zonulin, plays a role in intestinal permeability, allowing intercellular tight junction disassembly, and controlling the equilibrium between tolerance and immunity to non-self antigens..
Protein Sequence	MRALGAVVTLLLWGQLFAVELGNDAMDFEDDSCPKPPEIANGYVEHLVRYRCRQFYRLRAEGDGVYTLNDEKQWVNTVAGEKLPECEAVCGKPKHPVDQVQRIIGGSMDAKGSFPWQAKMISRHGLTTGATLISDQWLLTTAKNLFLNHSETASAKDITPTLTLYVGKNQLVEIEKVVLHPNHSVVDIGLIKLKQRVLVTERVMPICLPSKDYIAPGRVGYVSGWGRNANFRFTDRLKYVMLPVADQDKCVVHYENSTVPEKKNLTSPVGVQPILNEHTFCAGLTKYQEDTCYGDAGSAFAIHDMEEDTWYAAGILSFDKSCAVAEYGVYVRATDLKDWVQETMAKN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
66	Nitration	RAEGDGVYTLNDEKQ EECCCCEEECCCCCE	15.84	-
77	Phosphorylation	DEKQWVNTVAGEKLP CCCEEEEECCCCCCC	11.34	28418008
111	Acetylation	IGGSMDAKGSFPWQA HCCCCCCCCCCHHHH	51.31	7666897
111	Ubiquitination	IGGSMDAKGSFPWQA HCCCCCCCCCCHHHH	51.31	-
113	Phosphorylation	GSMDAKGSFPWQAKM CCCCCCCCCHHHHHH	27.68	28059163
119	Ubiquitination	GSFPWQAKMISRHGL CCCHHHHHHHHHCCC	22.97	-
148	N-linked_Glycosylation	TAKNLFLNHSETASA HHHHHHHCCCCCCCC	29.33	16944957
182	N-linked_Glycosylation	EKVVLHPNHSVVDIG EEEEECCCCCEEEEE	29.35	16944957
207	S-palmitoylation	TERVMPICLPSKDYI EECEECCCCCCCCCC	3.64	26165157
256	N-linked_Glycosylation	KCVVHYENSTVPEKK CEEEEECCCCCCCCC	35.50	16944957
264	N-linked_Glycosylation	STVPEKKNLTSPVGV CCCCCCCCCCCCCCC	60.67	-

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 HPT_MOUSE !!

Functions of PTM Sites

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

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of HPT_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Proteome-wide characterization of N-glycosylation events by diagonalchromatography."; Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.; J. Proteome Res. 5:2438-2447(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-148; ASN-182 AND ASN-256,AND MASS SPECTROMETRY.	16944957 [Abstract]