HPT_HUMAN - dbPTM
HPT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HPT_HUMAN
UniProt AC P00738
Protein Name Haptoglobin
Gene Name HP
Organism Homo sapiens (Human).
Sequence Length 406
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 Antimicrobial; 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.; 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 MSALGAVIALLLWGQLFAVDSGNDVTDIADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNDKKQWINKAVGDKLPECEADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNNEKQWINKAVGDKLPECEAVCGKPKNPANPVQRILGGHLDAKGSFPWQAKMVSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHPNYSQVDIGLIKLKQKVSVNERVMPICLPSKDYAEVGRVGYVSGWGRNANFKFTDHLKYVMLPVADQDQCIRHYEGSTVPEKKTPKSPVGVQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDLEEDTWYATGILSFDKSCAVAEYGVYVKVTSIQDWVQKTIAEN
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
21PhosphorylationGQLFAVDSGNDVTDI
HHHHCCCCCCCCHHC		32.6626657352
53GlycationHSVRYQCKNYYKLRT
EEHHHEECCEEEEEE		32.24-
53AcetylationHSVRYQCKNYYKLRT
EEHHHEECCEEEEEE		32.2427178108
55PhosphorylationVRYQCKNYYKLRTEG
HHHEECCEEEEEECC		6.35-
56PhosphorylationRYQCKNYYKLRTEGD
HHEECCEEEEEECCC		16.97-
57AcetylationYQCKNYYKLRTEGDG
HEECCEEEEEECCCC		22.5727178108
66PhosphorylationRTEGDGVYTLNDKKQ
EECCCCEEECCCHHH		15.84-
71AcetylationGVYTLNDKKQWINKA
CEEECCCHHHHHHHH		45.8727178108
72AcetylationVYTLNDKKQWINKAV
EEECCCHHHHHHHHH		54.4527178108
77AcetylationDKKQWINKAVGDKLP
CHHHHHHHHHHCCCC		35.0027178108
112AcetylationHSVRYQCKNYYKLRT
EEHHHEECCEEEEEE		32.2427178108
114PhosphorylationVRYQCKNYYKLRTEG
HHHEECCEEEEEECC		6.35-
115PhosphorylationRYQCKNYYKLRTEGD
HHEECCEEEEEECCC		16.97-
116AcetylationYQCKNYYKLRTEGDG
HEECCEEEEEECCCC		22.5727178108
125PhosphorylationRTEGDGVYTLNNEKQ
EECCCCEEECCCCCH		15.84-
131AcetylationVYTLNNEKQWINKAV
EEECCCCCHHHHHHH		53.7227178108
136AcetylationNEKQWINKAVGDKLP
CCCHHHHHHHHCCCC		35.0027178108
170AcetylationLGGHLDAKGSFPWQA
HCCCCCCCCCCCCCE		55.547666885
184N-linked_GlycosylationAKMVSHHNLTTGATL
EEECEECCCCCCCEE		33.3917623646
184N-linked_GlycosylationAKMVSHHNLTTGATL
EEECEECCCCCCCEE		33.3918514042
187O-linked_GlycosylationVSHHNLTTGATLINE
CEECCCCCCCEEECH		28.16OGP
207N-linked_GlycosylationTAKNLFLNHSENATA
HHHHHHHCCCCCCCH		29.3317623646
207N-linked_GlycosylationTAKNLFLNHSENATA
HHHHHHHCCCCCCCH		29.3318638581
211N-linked_GlycosylationLFLNHSENATAKDIA
HHHCCCCCCCHHHHH		45.6816740002
211N-linked_GlycosylationLFLNHSENATAKDIA
HHHCCCCCCCHHHHH		45.6818638581
241N-linked_GlycosylationEKVVLHPNYSQVDIG
EEEEECCCCCCCCEE		38.0419838169
241N-linked_GlycosylationEKVVLHPNYSQVDIG
EEEEECCCCCCCCEE		38.0418514042
242PhosphorylationKVVLHPNYSQVDIGL
EEEECCCCCCCCEEE		12.6326270265
243PhosphorylationVVLHPNYSQVDIGLI
EEECCCCCCCCEEEE		30.3026270265
251UbiquitinationQVDIGLIKLKQKVSV
CCCEEEEEEECCCCC		55.46-
266S-nitrosylationNERVMPICLPSKDYA
CCCEECEECCCCCCE		3.6425040305
269PhosphorylationVMPICLPSKDYAEVG
EECEECCCCCCEEEC		25.8024719451
272PhosphorylationICLPSKDYAEVGRVG
EECCCCCCEEECCEE		14.38-
280PhosphorylationAEVGRVGYVSGWGRN
EEECCEEEECCCCCC		6.6521253578
298PhosphorylationKFTDHLKYVMLPVAD
CCCCCCEEEEEEECC		9.4624114839
309S-nitrosylationPVADQDQCIRHYEGS
EECCHHHHHHHCCCC		3.8725040305
316PhosphorylationCIRHYEGSTVPEKKT
HHHHCCCCCCCCCCC		17.8128270605
317O-linked_GlycosylationIRHYEGSTVPEKKTP
HHHCCCCCCCCCCCC		51.44OGP
317PhosphorylationIRHYEGSTVPEKKTP
HHHCCCCCCCCCCCC		51.4428270605
321GlycationEGSTVPEKKTPKSPV
CCCCCCCCCCCCCCC		56.74-
321AcetylationEGSTVPEKKTPKSPV
CCCCCCCCCCCCCCC		56.747683315
323PhosphorylationSTVPEKKTPKSPVGV
CCCCCCCCCCCCCCC		47.2023312004
326PhosphorylationPEKKTPKSPVGVQPI
CCCCCCCCCCCCHHC		26.4824719451
340S-nitrosylationILNEHTFCAGMSKYQ
CCCCCEEEECCCCCC		3.1725040305
381S-nitrosylationILSFDKSCAVAEYGV
EEEECCCCEEEECEE		4.3225040305
386PhosphorylationKSCAVAEYGVYVKVT
CCCEEEECEEEEEEE		11.36-
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HPT_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 HPT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HBB_HUMANHBBphysical
7378053
TGM2_HUMANTGM2physical
21988832
RL11_HUMANRPL11physical
21988832
LAMC3_HUMANLAMC3physical
21988832
SMAD3_HUMANSMAD3physical
21988832
TBL1X_HUMANTBL1Xphysical
21988832
P63_HUMANTP63physical
21988832
WASL_HUMANWASLphysical
21988832
MVP_HUMANMVPphysical
21988832
APOA1_HUMANAPOA1physical
15533931
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614081Anhaptoglobinemia (AHP)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HPT_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Enrichment of glycopeptides for glycan structure and attachment siteidentification.";
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,Brinkmalm G., Larson G.;
Nat. Methods 6:809-811(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-241, CARBOHYDRATESTRUCTURE, AND MASS SPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184; ASN-207; ASN-211 ANDASN-241, AND MASS SPECTROMETRY.
"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry.";
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.;
J. Proteome Res. 5:1493-1503(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-207 AND ASN-211, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184; ASN-207; ASN-211 ANDASN-241, AND MASS SPECTROMETRY.
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184; ASN-207; ASN-211 ANDASN-241, AND MASS SPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-207 AND ASN-241.

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