dbPTM

AMBP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AMBP_HUMAN
UniProt AC	P02760
Protein Name	Protein AMBP
Gene Name	AMBP
Organism	Homo sapiens (Human).
Sequence Length	352
Subcellular Localization	Secreted.
Protein Description	Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization.; Trypstatin is a trypsin inhibitor..
Protein Sequence	MRSLGALLLLLSACLAVSAGPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIMDRMTVSTLVLGEGATEAEISMTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIFTMADRGECVPGEQEPEPILIPRVRRAVLPQEEEGSGGGQLVTEVTKKEDSCQLGYSAGPCMGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTCRTVAACNLPIVRGPCRAFIQLWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVPGDGDEELLRFSN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
24	O-linked_Glycosylation	VSAGPVPTPPDNIQV HHCCCCCCCCCCCEE	47.92	6198962
24	O-linked_Glycosylation	VSAGPVPTPPDNIQV HHCCCCCCCCCCCEE	47.92	1694784
36	N-linked_Glycosylation	IQVQENFNISRIYGK CEEECCCEEEHEECC	42.80	1694784
36	N-linked_Glycosylation	IQVQENFNISRIYGK CEEECCCEEEHEECC	42.80	1694784
64	Phosphorylation	KKIMDRMTVSTLVLG HHHHHHCCCEEEEEC	16.52	25954137
66	Phosphorylation	IMDRMTVSTLVLGEG HHHHCCCEEEEECCC	13.57	68723839
67	Phosphorylation	MDRMTVSTLVLGEGA HHHCCCEEEEECCCC	19.29	25954137
75	Phosphorylation	LVLGEGATEAEISMT EEECCCCCEEEEEEC	46.73	68728509
80	Phosphorylation	GATEAEISMTSTRWR CCCEEEEEECCCCCH	13.91	25954137
82	Phosphorylation	TEAEISMTSTRWRKG CEEEEEECCCCCHHC	21.84	29083192
83	Phosphorylation	EAEISMTSTRWRKGV EEEEEECCCCCHHCC	13.82	22210691
84	Phosphorylation	AEISMTSTRWRKGVC EEEEECCCCCHHCCC	25.69	29083192
94	O-linked_Glycosylation	RKGVCEETSGAYEKT HHCCCCCCCCCEEEE	15.35	OGP
95	Phosphorylation	KGVCEETSGAYEKTD HCCCCCCCCCEEEEC	25.38	29759185
95	O-linked_Glycosylation	KGVCEETSGAYEKTD HCCCCCCCCCEEEEC	25.38	OGP
115	N-linked_Glycosylation	LYHKSKWNITMESYV EEEECCEEEEEEEEE	24.48	1694784
115	N-linked_Glycosylation	LYHKSKWNITMESYV EEEECCEEEEEEEEE	24.48	22171320
215	O-linked_Glycosylation	LPQEEEGSGGGQLVT CCCCCCCCCCCEEEE	37.23	7682553
230	Phosphorylation	EVTKKEDSCQLGYSA EEEECCCCCCCCCCC	12.59	24505115
236	Phosphorylation	DSCQLGYSAGPCMGM CCCCCCCCCCCCCCC	25.58	24505115
250	N-linked_Glycosylation	MTSRYFYNGTSMACE CCEEEEECCCCCEEE	37.05	22171320
317	Phosphorylation	GKCVLFPYGGCQGNG CEEEEECCCCCCCCC	20.86	24505115
351	Phosphorylation	DEELLRFSN------ CHHHHCCCC------	34.88	29759185

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 AMBP_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
215	S	Sulfation		1898736
O-linkage of the glycosaminoglycan, chondroitin sulfate, at Ser-215 allows cross-linking between the three polypeptide chains.

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 AMBP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AMBP_HUMAN	AMBP	physical	11883904
FINC_HUMAN	FN1	physical	7519849
A2MG_HUMAN	A2M	physical	7519849
A2MG_HUMAN	A2M	physical	1697852
AMBP_HUMAN	AMBP	physical	9183005
ALBU_HUMAN	ALB	physical	9183005
CD79A_HUMAN	CD79A	physical	9183005
COX8A_HUMAN	COX8A	physical	21988832
ENOA_HUMAN	ENO1	physical	21988832
STAT3_HUMAN	STAT3	physical	21988832
DAAM1_HUMAN	DAAM1	physical	21988832
FHL3_HUMAN	FHL3	physical	25416956

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 AMBP_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD."; Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; Mol. Cell. Proteomics 0:0-0(2011). Cited for: GLYCOSYLATION AT ASN-115 AND ASN-250, STRUCTURE OF CARBOHYDRATES, ANDMASS SPECTROMETRY.	22171320 [Abstract]
"Location and characterization of the three carbohydrate prostheticgroups of human protein HC."; Escribano J., Lopex-Otin C., Hjerpe A., Grubb A.O., Mendez E.; FEBS Lett. 266:167-170(1990). Cited for: GLYCOSYLATION AT THR-24; ASN-36 AND ASN-115, AND STRUCTURE OFCARBOHYDRATES.	1694784 [Abstract]
"Kunitz-type proteinase inhibitors derived by limited proteolysis ofthe inter-alpha-trypsin inhibitor, V. Attachments of carbohydrates inthe human urinary trypsin inhibitor isolated by affinitychromatography."; Hochstrasser K., Schoenberger O.L., Rossmanith I., Wachter E.; Hoppe-Seyler's Z. Physiol. Chem. 362:1357-1362(1981). Cited for: GLYCOSYLATION AT SER-215 AND ASN-250, AND STRUCTURE OF CARBOHYDRATES.	6171497 [Abstract]
O-linked Glycosylation
Reference	PubMed
"Location and characterization of the three carbohydrate prostheticgroups of human protein HC."; Escribano J., Lopex-Otin C., Hjerpe A., Grubb A.O., Mendez E.; FEBS Lett. 266:167-170(1990). Cited for: GLYCOSYLATION AT THR-24; ASN-36 AND ASN-115, AND STRUCTURE OFCARBOHYDRATES.	1694784 [Abstract]
"Kunitz-type proteinase inhibitors derived by limited proteolysis ofthe inter-alpha-trypsin inhibitor, V. Attachments of carbohydrates inthe human urinary trypsin inhibitor isolated by affinitychromatography."; Hochstrasser K., Schoenberger O.L., Rossmanith I., Wachter E.; Hoppe-Seyler's Z. Physiol. Chem. 362:1357-1362(1981). Cited for: GLYCOSYLATION AT SER-215 AND ASN-250, AND STRUCTURE OF CARBOHYDRATES.	6171497 [Abstract]
"Presence of the protein-glycosaminoglycan-protein covalent cross-linkin the inter-alpha-inhibitor-related proteinase inhibitor heavy chain2/bikunin."; Enghild J.J., Salvesen G., Thoegersen I.B., Valnickova Z., Pizzo S.V.,Hefta S.A.; J. Biol. Chem. 268:8711-8716(1993). Cited for: PROTEIN SEQUENCE OF 206-223, GLYCOSYLATION AT SER-215, AND CROSS-LINKSITE TO HC2.	7682553 [Abstract]
"Chondroitin 4-sulfate covalently cross-links the chains of the humanblood protein pre-alpha-inhibitor."; Enghild J.J., Salvesen G., Hefta S.A., Thoegersen I.B., Rutherfurd S.,Pizzo S.V.; J. Biol. Chem. 266:747-751(1991). Cited for: PROTEIN SEQUENCE OF 206-223, GLYCOSYLATION AT SER-215, AND CROSS-LINKSITE TO HC3.	1898736 [Abstract]

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