HEMO_HUMAN - dbPTM
HEMO_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HEMO_HUMAN
UniProt AC P02790
Protein Name Hemopexin
Gene Name HPX
Organism Homo sapiens (Human).
Sequence Length 462
Subcellular Localization Secreted.
Protein Description Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation..
Protein Sequence MARVLGAPVALGLWSLCWSLAIATPLPPTSAHGNVAEGETKPDPDVTERCSDGWSFDATTLDDNGTMLFFKGEFVWKSHKWDRELISERWKNFPSPVDAAFRQGHNSVFLIKGDKVWVYPPEKKEKGYPKLLQDEFPGIPSPLDAAVECHRGECQAEGVLFFQGDREWFWDLATGTMKERSWPAVGNCSSALRWLGRYYCFQGNQFLRFDPVRGEVPPRYPRDVRDYFMPCPGRGHGHRNGTGHGNSTHHGPEYMRCSPHLVLSALTSDNHGATYAFSGTHYWRLDTSRDGWHSWPIAHQWPQGPSAVDAAFSWEEKLYLVQGTQVYVFLTKGGYTLVSGYPKRLEKEVGTPHGIILDSVDAAFICPGSSRLHIMAGRRLWWLDLKSGAQATWTELPWPHEKVDGALCMEKSLGPNSCSANGPGLYLIHGPNLYCYSDVEKLNAAKALPQPQNVTSLLGCTH
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
19PhosphorylationGLWSLCWSLAIATPL
HHHHHHHHHHHCCCC		13.6124505115
24O-linked_GlycosylationCWSLAIATPLPPTSA
HHHHHHCCCCCCCCC		21.176510521
24O-linked_GlycosylationCWSLAIATPLPPTSA
HHHHHHCCCCCCCCC		21.1719838169
29O-linked_GlycosylationIATPLPPTSAHGNVA
HCCCCCCCCCCCCCC		36.2823234360
29PhosphorylationIATPLPPTSAHGNVA
HCCCCCCCCCCCCCC		36.2824505115
30O-linked_GlycosylationATPLPPTSAHGNVAE
CCCCCCCCCCCCCCC		24.84OGP
30PhosphorylationATPLPPTSAHGNVAE
CCCCCCCCCCCCCCC		24.8424505115
40O-linked_GlycosylationGNVAEGETKPDPDVT
CCCCCCCCCCCCCCC		59.75OGP
47O-linked_GlycosylationTKPDPDVTERCSDGW
CCCCCCCCCCCCCCC		25.70OGP
64N-linked_GlycosylationDATTLDDNGTMLFFK
ECEEECCCCCEEEEE		47.7218638581
64N-linked_GlycosylationDATTLDDNGTMLFFK
ECEEECCCCCEEEEE		47.7219838169
77AcetylationFKGEFVWKSHKWDRE
EECEEEECCCCHHHH		37.0627178108
115GlycationVFLIKGDKVWVYPPE
EEEEECCEEEECCHH		46.82-
141PhosphorylationDEFPGIPSPLDAAVE
CCCCCCCCCCHHHEE		35.8524505115
174PhosphorylationEWFWDLATGTMKERS
EEEEECCCCCCCCCC		40.2524505115
176PhosphorylationFWDLATGTMKERSWP
EEECCCCCCCCCCCC		22.2524505115
187N-linked_GlycosylationRSWPAVGNCSSALRW
CCCCCCCCHHHHHHH		18.8515084671
187N-linked_GlycosylationRSWPAVGNCSSALRW
CCCCCCCCHHHHHHH		18.8515084671
200S-nitrosylationRWLGRYYCFQGNQFL
HHHHHEEEECCCEEE		1.2025040305
220PhosphorylationRGEVPPRYPRDVRDY
CCCCCCCCCCCHHHH		14.37-
227NitrationYPRDVRDYFMPCPGR
CCCCHHHHCCCCCCC		7.39-
240N-linked_GlycosylationGRGHGHRNGTGHGNS
CCCCCCCCCCCCCCC		46.8617623646
240N-linked_GlycosylationGRGHGHRNGTGHGNS
CCCCCCCCCCCCCCC		46.866371807
246N-linked_GlycosylationRNGTGHGNSTHHGPE
CCCCCCCCCCCCCCC		37.756371807
246N-linked_GlycosylationRNGTGHGNSTHHGPE
CCCCCCCCCCCCCCC		37.7518638581
319PhosphorylationFSWEEKLYLVQGTQV
CCCCEEEEEEECCEE		18.8525072903
324PhosphorylationKLYLVQGTQVYVFLT
EEEEEECCEEEEEEE		9.5825072903
327PhosphorylationLVQGTQVYVFLTKGG
EEECCEEEEEEECCC		3.9125072903
331PhosphorylationTQVYVFLTKGGYTLV
CEEEEEEECCCEEEE		19.0425072903
335NitrationVFLTKGGYTLVSGYP
EEEECCCEEEEECCC		12.93-
341PhosphorylationGYTLVSGYPKRLEKE
CEEEEECCCHHHHHH		9.70-
351O-linked_GlycosylationRLEKEVGTPHGIILD
HHHHHHCCCCEEEEE		19.79OGP
366S-nitrosylationSVDAAFICPGSSRLH
CCCEEEECCCCCEEE		2.2325040305
386AcetylationRLWWLDLKSGAQATW
EEEEEECCCCCEEEE		46.657695101
432N-linked_GlycosylationLYLIHGPNLYCYSDV
EEEEECCCEEECCCH		48.516371807
437PhosphorylationGPNLYCYSDVEKLNA
CCCEEECCCHHHHHH		31.4524505115
453N-linked_GlycosylationKALPQPQNVTSLLGC
HCCCCCCCHHHHCCC		45.8015084671
453N-linked_GlycosylationKALPQPQNVTSLLGC
HCCCCCCCHHHHCCC		45.8015084671
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 HEMO_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
24TGlycosylation

6371807
29TGlycosylation

23234360
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 HEMO_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P63_HUMANTP63physical
21988832
ATS1_HUMANADAMTS1physical
26186194
GLT12_HUMANGALNT12physical
26186194
GLT12_HUMANGALNT12physical
28514442
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 HEMO_HUMAN

loading...

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 THR-24; ASN-64; ASN-187 ANDASN-453, STRUCTURE OF CARBOHYDRATES, 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-187 AND ASN-453, AND MASSSPECTROMETRY.
"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-187 AND ASN-453, 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-64 AND ASN-187, AND MASSSPECTROMETRY.
"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-187; ASN-240 AND ASN-246,AND MASS SPECTROMETRY.
"A proteomic analysis of human bile.";
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
Mol. Cell. Proteomics 3:715-728(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187 AND ASN-453, AND MASSSPECTROMETRY.
"Structure of human hemopexin: O-glycosyl and N-glycosyl sites andunusual clustering of tryptophan residues.";
Takahashi N., Takahashi Y., Putnam F.W.;
Proc. Natl. Acad. Sci. U.S.A. 81:2021-2025(1984).
Cited for: PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION AT THR-24; ASN-64; ASN-64;ASN-187; ASN-240; ASN-246 AND ASN-453.
"Amino acid sequence of the N-terminal region of human hemopexin.";
Frantikova V., Borvak J., Kluh I., Moravek L.;
FEBS Lett. 178:213-216(1984).
Cited for: PROTEIN SEQUENCE OF 24-255.
O-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 THR-24; ASN-64; ASN-187 ANDASN-453, STRUCTURE OF CARBOHYDRATES, AND MASS SPECTROMETRY.
"Structure of human hemopexin: O-glycosyl and N-glycosyl sites andunusual clustering of tryptophan residues.";
Takahashi N., Takahashi Y., Putnam F.W.;
Proc. Natl. Acad. Sci. U.S.A. 81:2021-2025(1984).
Cited for: PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION AT THR-24; ASN-64; ASN-64;ASN-187; ASN-240; ASN-246 AND ASN-453.
"Amino acid sequence of the N-terminal region of human hemopexin.";
Frantikova V., Borvak J., Kluh I., Moravek L.;
FEBS Lett. 178:213-216(1984).
Cited for: PROTEIN SEQUENCE OF 24-255.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory