dbPTM

A2MG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	A2MG_HUMAN
UniProt AC	P01023
Protein Name	Alpha-2-macroglobulin
Gene Name	A2M
Organism	Homo sapiens (Human).
Sequence Length	1474
Subcellular Localization	Secreted .
Protein Description	Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase..
Protein Sequence	MGKNKLLHPSLVLLLLVLLPTDASVSGKPQYMVLVPSLLHTETTEKGCVLLSYLNETVTVSASLESVRGNRSLFTDLEAENDVLHCVAFAVPKSSSNEEVMFLTVQVKGPTQEFKKRTTVMVKNEDSLVFVQTDKSIYKPGQTVKFRVVSMDENFHPLNELIPLVYIQDPKGNRIAQWQSFQLEGGLKQFSFPLSSEPFQGSYKVVVQKKSGGRTEHPFTVEEFVLPKFEVQVTVPKIITILEEEMNVSVCGLYTYGKPVPGHVTVSICRKYSDASDCHGEDSQAFCEKFSGQLNSHGCFYQQVKTKVFQLKRKEYEMKLHTEAQIQEEGTVVELTGRQSSEITRTITKLSFVKVDSHFRQGIPFFGQVRLVDGKGVPIPNKVIFIRGNEANYYSNATTDEHGLVQFSINTTNVMGTSLTVRVNYKDRSPCYGYQWVSEEHEEAHHTAYLVFSPSKSFVHLEPMSHELPCGHTQTVQAHYILNGGTLLGLKKLSFYYLIMAKGGIVRTGTHGLLVKQEDMKGHFSISIPVKSDIAPVARLLIYAVLPTGDVIGDSAKYDVENCLANKVDLSFSPSQSLPASHAHLRVTAAPQSVCALRAVDQSVLLMKPDAELSASSVYNLLPEKDLTGFPGPLNDQDNEDCINRHNVYINGITYTPVSSTNEKDMYSFLEDMGLKAFTNSKIRKPKMCPQLQQYEMHGPEGLRVGFYESDVMGRGHARLVHVEEPHTETVRKYFPETWIWDLVVVNSAGVAEVGVTVPDTITEWKAGAFCLSEDAGLGISSTASLRAFQPFFVELTMPYSVIRGEAFTLKATVLNYLPKCIRVSVQLEASPAFLAVPVEKEQAPHCICANGRQTVSWAVTPKSLGNVNFTVSAEALESQELCGTEVPSVPEHGRKDTVIKPLLVEPEGLEKETTFNSLLCPSGGEVSEELSLKLPPNVVEESARASVSVLGDILGSAMQNTQNLLQMPYGCGEQNMVLFAPNIYVLDYLNETQQLTPEIKSKAIGYLNTGYQRQLNYKHYDGSYSTFGERYGRNQGNTWLTAFVLKTFAQARAYIFIDEAHITQALIWLSQRQKDNGCFRSSGSLLNNAIKGGVEDEVTLSAYITIALLEIPLTVTHPVVRNALFCLESAWKTAQEGDHGSHVYTKALLAYAFALAGNQDKRKEVLKSLNEEAVKKDNSVHWERPQKPKAPVGHFYEPQAPSAEVEMTSYVLLAYLTAQPAPTSEDLTSATNIVKWITKQQNAQGGFSSTQDTVVALHALSKYGAATFTRTGKAAQVTIQSSGTFSSKFQVDNNNRLLLQQVSLPELPGEYSMKVTGEGCVYLQTSLKYNILPEKEEFPFALGVQTLPQTCDEPKAHTSFQISLSVSYTGSRSASNMAIVDVKMVSGFIPLKPTVKMLERSNHVSRTEVSSNHVLIYLDKVSNQTLSLFFTVLQDVPVRDLKPAIVKVYDYYETDEFAIAEYNAPCSKDLGNA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
26	O-linked_Glycosylation	LPTDASVSGKPQYMV CCCCCCCCCCCCEEE	38.31	OGP
55	N-linked_Glycosylation	CVLLSYLNETVTVSA EEEEEECCCEEEEEE	34.36	18638581
70	N-linked_Glycosylation	SLESVRGNRSLFTDL EEHHHCCCCCCCCCH	21.58	6203908
133	Phosphorylation	DSLVFVQTDKSIYKP CCEEEEEECCCCCCC	39.84	24505115
145	Glycation	YKPGQTVKFRVVSMD CCCCCEEEEEEEECC	30.73	-
191	Phosphorylation	EGGLKQFSFPLSSEP CCCEEEEECCCCCCC	24.38	26074081
195	Phosphorylation	KQFSFPLSSEPFQGS EEEECCCCCCCCCCE	32.66	26074081
196	Phosphorylation	QFSFPLSSEPFQGSY EEECCCCCCCCCCEE	57.90	26074081
202	Phosphorylation	SSEPFQGSYKVVVQK CCCCCCCEEEEEEEE	15.82	26074081
203	Phosphorylation	SEPFQGSYKVVVQKK CCCCCCEEEEEEEEC	18.02	26074081
211	Phosphorylation	KVVVQKKSGGRTEHP EEEEEECCCCCCCCC	54.22	26074081
215	Phosphorylation	QKKSGGRTEHPFTVE EECCCCCCCCCEEEE	41.75	26074081
247	N-linked_Glycosylation	TILEEEMNVSVCGLY HHCHHHCCEEEEEEE	26.62	16335952
254	Phosphorylation	NVSVCGLYTYGKPVP CEEEEEEEECCCCCC	5.34	28258704
255	Phosphorylation	VSVCGLYTYGKPVPG EEEEEEEECCCCCCC	30.73	28258704
272	Phosphorylation	TVSICRKYSDASDCH EEEEECCCCCHHHCC	7.76	24114839
273	Phosphorylation	VSICRKYSDASDCHG EEEECCCCCHHHCCC	29.72	24114839
276	Phosphorylation	CRKYSDASDCHGEDS ECCCCCHHHCCCCCH	45.84	24114839
283	Phosphorylation	SDCHGEDSQAFCEKF HHCCCCCHHHHHHHH	21.07	24114839
291	Phosphorylation	QAFCEKFSGQLNSHG HHHHHHHHCCCCCCC	36.38	28270605
296	Phosphorylation	KFSGQLNSHGCFYQQ HHHCCCCCCCCCHHH	29.83	28270605
299	S-palmitoylation	GQLNSHGCFYQQVKT CCCCCCCCCHHHHHH	2.10	29575903
301	Phosphorylation	LNSHGCFYQQVKTKV CCCCCCCHHHHHHHE	11.34	28270605
346	Phosphorylation	QSSEITRTITKLSFV CCHHHEEEEEEEEEE	25.09	46156069
382	Glycation	KGVPIPNKVIFIRGN CCCCCCCEEEEEECC	31.21	-
393	Phosphorylation	IRGNEANYYSNATTD EECCCCCCCCCCCCC	18.47	30576142
394	Phosphorylation	RGNEANYYSNATTDE ECCCCCCCCCCCCCC	8.68	24043423
395	Phosphorylation	GNEANYYSNATTDEH CCCCCCCCCCCCCCC	15.04	24043423
396	N-linked_Glycosylation	NEANYYSNATTDEHG CCCCCCCCCCCCCCC	25.78	6203908
398	Phosphorylation	ANYYSNATTDEHGLV CCCCCCCCCCCCCEE	38.74	30576142
399	Phosphorylation	NYYSNATTDEHGLVQ CCCCCCCCCCCCEEE	36.66	24043423
408	Phosphorylation	EHGLVQFSINTTNVM CCCEEEEEEECCCCC	9.61	24043423
410	N-linked_Glycosylation	GLVQFSINTTNVMGT CEEEEEEECCCCCCC	39.39	6203908
410	N-linked_Glycosylation	GLVQFSINTTNVMGT CEEEEEEECCCCCCC	39.39	16335952
411	Phosphorylation	LVQFSINTTNVMGTS EEEEEEECCCCCCCE	20.34	24043423
412	Phosphorylation	VQFSINTTNVMGTSL EEEEEECCCCCCCEE	22.71	24043423
417	Phosphorylation	NTTNVMGTSLTVRVN ECCCCCCCEEEEEEE	11.50	24043423
418	Phosphorylation	TTNVMGTSLTVRVNY CCCCCCCEEEEEEEE	19.13	24043423
420	Phosphorylation	NVMGTSLTVRVNYKD CCCCCEEEEEEEECC	13.16	24043423
425	Phosphorylation	SLTVRVNYKDRSPCY EEEEEEEECCCCCCC	16.06	30576142
431	S-palmitoylation	NYKDRSPCYGYQWVS EECCCCCCCCEEECC	4.31	29575903
497	Phosphorylation	LKKLSFYYLIMAKGG CCHHHHHHHHHCCCC	6.42	22817900
510	Phosphorylation	GGIVRTGTHGLLVKQ CCEEEEECCEEEEEC	16.50	26091039
543	Nitration	PVARLLIYAVLPTGD HHHHHHHHHHCCCCC	7.22	-
571	Phosphorylation	LANKVDLSFSPSQSL HCCCCCCCCCCCCCC	21.15	28270605
573	Phosphorylation	NKVDLSFSPSQSLPA CCCCCCCCCCCCCCC	21.92	28270605
575	O-linked_Glycosylation	VDLSFSPSQSLPASH CCCCCCCCCCCCCCC	31.07	OGP
575	Phosphorylation	VDLSFSPSQSLPASH CCCCCCCCCCCCCCC	31.07	28270605
577	Phosphorylation	LSFSPSQSLPASHAH CCCCCCCCCCCCCCE	40.43	28270605
581	Phosphorylation	PSQSLPASHAHLRVT CCCCCCCCCCEEEEE	21.19	28270605
588	O-linked_Glycosylation	SHAHLRVTAAPQSVC CCCEEEEECCCCCHH	15.63	OGP
593	Phosphorylation	RVTAAPQSVCALRAV EEECCCCCHHHHEEC	20.36	30206219
654	O-linked_Glycosylation	NVYINGITYTPVSST CEEECCEEEECCCCC	23.81	OGP
679	Phosphorylation	DMGLKAFTNSKIRKP HCCCHHHCCCCCCCC	43.36	20068231
695	Phosphorylation	MCPQLQQYEMHGPEG CCHHHHHCCHHCCCC	11.40	2035307
708	Nitration	EGLRVGFYESDVMGR CCEEEEEEECCCCCC	14.48	-
708	Phosphorylation	EGLRVGFYESDVMGR CCEEEEEEECCCCCC	14.48	28857561
710	Phosphorylation	LRVGFYESDVMGRGH EEEEEEECCCCCCCE	24.91	28857561
757	O-linked_Glycosylation	GVAEVGVTVPDTITE CEEEECEECCCCCCC	22.01	OGP
800	Nitration	FVELTMPYSVIRGEA EEEEECCCEEECCCC	12.54	-
817	Phosphorylation	LKATVLNYLPKCIRV EHHHHHHHHCCCEEE	21.88	25884760
820	Acetylation	TVLNYLPKCIRVSVQ HHHHHHCCCEEEEEE	39.43	-
861	Phosphorylation	QTVSWAVTPKSLGNV EEEEEEECCHHCCCC	19.77	110738701
869	N-linked_Glycosylation	PKSLGNVNFTVSAEA CHHCCCCEEEEEHHH	30.76	18638581
869	N-linked_Glycosylation	PKSLGNVNFTVSAEA CHHCCCCEEEEEHHH	30.76	16335952
885	O-linked_Glycosylation	ESQELCGTEVPSVPE HHCCCCCCCCCCCCC	32.58	OGP
898	Phosphorylation	PEHGRKDTVIKPLLV CCCCCCCCCEECEEE	27.45	23312004
914	Phosphorylation	PEGLEKETTFNSLLC CCCCCCCCCCCEEEC	47.99	29978859
915	Phosphorylation	EGLEKETTFNSLLCP CCCCCCCCCCEEECC	23.16	29978859
918	Phosphorylation	EKETTFNSLLCPSGG CCCCCCCEEECCCCC	20.66	29978859
923	Phosphorylation	FNSLLCPSGGEVSEE CCEEECCCCCCCCHH	59.44	28270605
928	Phosphorylation	CPSGGEVSEELSLKL CCCCCCCCHHHCCCC	22.50	28270605
932	Phosphorylation	GEVSEELSLKLPPNV CCCCHHHCCCCCCCH	27.09	28270605
943	Phosphorylation	PPNVVEESARASVSV CCCHHHHHHHHHHHH	15.00	29978859
991	N-linked_Glycosylation	IYVLDYLNETQQLTP EEEEHHHHCCCCCCH	44.00	6203908
991	N-linked_Glycosylation	IYVLDYLNETQQLTP EEEEHHHHCCCCCCH	44.00	6203908
1003	Glycation	LTPEIKSKAIGYLNT CCHHHHHHHHHHCCC	38.73	-
1007	Nitration	IKSKAIGYLNTGYQR HHHHHHHHCCCCCCE	7.23	-
1007	Phosphorylation	IKSKAIGYLNTGYQR HHHHHHHHCCCCCCE	7.23	30814465
1012	Phosphorylation	IGYLNTGYQRQLNYK HHHCCCCCCEECCCC	9.85	30803825
1021	Phosphorylation	RQLNYKHYDGSYSTF EECCCCCCCCCCCCH	20.18	28270605
1025	Phosphorylation	YKHYDGSYSTFGERY CCCCCCCCCCHHHHC	19.77	7348323
1026	Phosphorylation	KHYDGSYSTFGERYG CCCCCCCCCHHHHCC	20.96	28270605
1027	Phosphorylation	HYDGSYSTFGERYGR CCCCCCCCHHHHCCC	27.68	28270605
1082	Phosphorylation	KDNGCFRSSGSLLNN CCCCCCCCCCHHHHH	20.85	28270605
1083	Phosphorylation	DNGCFRSSGSLLNNA CCCCCCCCCHHHHHH	28.30	28270605
1085	Phosphorylation	GCFRSSGSLLNNAIK CCCCCCCHHHHHHHC	31.47	28270605
1147	Acetylation	HGSHVYTKALLAYAF CCCHHHHHHHHHHHH	21.25	7926677
1162	Acetylation	ALAGNQDKRKEVLKS HHHCCHHHHHHHHHH	56.45	21466224
1164	Acetylation	AGNQDKRKEVLKSLN HCCHHHHHHHHHHHC	58.89	7926687
1168	Acetylation	DKRKEVLKSLNEEAV HHHHHHHHHHCHHHH	59.06	7926697
1168	Glycation	DKRKEVLKSLNEEAV HHHHHHHHHHCHHHH	59.06	-
1169	Phosphorylation	KRKEVLKSLNEEAVK HHHHHHHHHCHHHHH	32.06	28258704
1264	Phosphorylation	ALHALSKYGAATFTR HHHHHHHHCCEEEEE	14.50	21130716
1270	Phosphorylation	KYGAATFTRTGKAAQ HHCCEEEEECCCEEE	23.98	21130716
1272	Phosphorylation	GAATFTRTGKAAQVT CCEEEEECCCEEEEE	39.72	21130716
1321	S-palmitoylation	MKVTGEGCVYLQTSL EEEECCCEEEEEEEE	1.26	29575903
1374	Phosphorylation	VSYTGSRSASNMAIV EEECCCCCCCCEEEE	37.43	20068231
1387	Phosphorylation	IVDVKMVSGFIPLKP EEEEEEECCCCCCCC	25.20	-
1395	Phosphorylation	GFIPLKPTVKMLERS CCCCCCCHHHHHHCC	31.04	-
1424	N-linked_Glycosylation	IYLDKVSNQTLSLFF EEEEECCCCEEEHHE	41.67	18514042
1424	N-linked_Glycosylation	IYLDKVSNQTLSLFF EEEEECCCCEEEHHE	41.67	17623646

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 A2MG_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of A2MG_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 A2MG_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATS1_HUMAN	ADAMTS1	physical	10373500
PAEP_HUMAN	PAEP	physical	11023837
LEP_HUMAN	LEP	physical	9724081
LCAT_HUMAN	LCAT	physical	11435418
NGF_HUMAN	NGF	physical	10681572
APOE_HUMAN	APOE	physical	9831625
IL10_HUMAN	IL10	physical	10714547
IL4_HUMAN	IL4	physical	10714547
APOE_HUMAN	APOE	physical	21163940
A4_HUMAN	APP	physical	21163940
NOS3_HUMAN	NOS3	physical	21163940
PAXI1_HUMAN	PAXIP1	physical	21163940
IFIT5_HUMAN	IFIT5	physical	21163940
TPPC5_HUMAN	TRAPPC5	physical	21163940
RNF32_HUMAN	RNF32	physical	21163940
PRAM_HUMAN	PRAM1	physical	21163940
SYFA_HUMAN	FARSA	physical	21163940
IFIT3_HUMAN	IFIT3	physical	21163940
OGA_HUMAN	MGEA5	physical	21163940
RHEB_HUMAN	RHEB	physical	21163940
PRDX2_HUMAN	PRDX2	physical	21163940
ECSIT_HUMAN	ECSIT	physical	21163940
ELAV3_HUMAN	ELAVL3	physical	21163940
EXOS1_HUMAN	EXOSC1	physical	21163940
GCDH_HUMAN	GCDH	physical	21163940
LONM_HUMAN	LONP1	physical	21163940
CP2C8_HUMAN	CYP2C8	physical	21163940
CP2CI_HUMAN	CYP2C18	physical	21163940
RD23A_HUMAN	RAD23A	physical	21163940
A2MG_HUMAN	A2M	physical	21163940
AP1M2_HUMAN	AP1M2	physical	21163940
SWAP1_HUMAN	SWSAP1	physical	21163940
CDC37_HUMAN	CDC37	physical	21163940
DNJB1_HUMAN	DNAJB1	physical	21163940
EVI5L_HUMAN	EVI5L	physical	21163940
FXL12_HUMAN	FBXL12	physical	21163940
FBXW4_HUMAN	FBXW4	physical	21163940
RAB3A_HUMAN	RAB3A	physical	21163940
RETN_HUMAN	RETN	physical	21163940
STALP_HUMAN	STAMBPL1	physical	21163940
NCDN_HUMAN	NCDN	physical	21163940
UMPS_HUMAN	UMPS	physical	21163940
LST8_HUMAN	MLST8	physical	21163940
ACTB_HUMAN	ACTB	physical	21163940
AT1A1_HUMAN	ATP1A1	physical	21163940
EGLN2_HUMAN	EGLN2	physical	21163940
ENOG_HUMAN	ENO2	physical	21163940
FIS1_HUMAN	FIS1	physical	21163940
IGSF8_HUMAN	IGSF8	physical	21163940
TBA1B_HUMAN	TUBA1B	physical	21163940
TYRO3_HUMAN	TYRO3	physical	21163940
TGM2_HUMAN	TGM2	physical	21988832
PZP_HUMAN	PZP	physical	28514442
HPLN3_HUMAN	HAPLN3	physical	28514442
CRAC1_HUMAN	CRTAC1	physical	28514442
METRN_HUMAN	METRN	physical	28514442
PTX3_HUMAN	PTX3	physical	28514442
PADC1_HUMAN	PRADC1	physical	28514442
LOXL1_HUMAN	LOXL1	physical	28514442
EOGT_HUMAN	EOGT	physical	28514442
GLT12_HUMAN	GALNT12	physical	28514442
FKB14_HUMAN	FKBP14	physical	28514442
METRL_HUMAN	METRNL	physical	28514442
DEFM_HUMAN	PDF	physical	28514442
PGLT1_HUMAN	POGLUT1	physical	28514442
EGFL7_HUMAN	EGFL7	physical	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 A2MG_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-396; ASN-991 AND ASN-1424,AND MASS SPECTROMETRY.	19159218 [Abstract]
"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-55; ASN-247; ASN-396;ASN-410; ASN-869; ASN-991 AND ASN-1424, AND MASS SPECTROMETRY.	16335952 [Abstract]
"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-869 AND ASN-1424, AND MASSSPECTROMETRY.	14760718 [Abstract]
"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-991.	12754519 [Abstract]
"Primary structure of human alpha 2-macroglobulin. V. The completestructure."; Sottrup-Jensen L., Stepanik T.M., Kristensen T., Wierzbicki D.M.,Jones C.M., Loenblad P.B., Magnusson S., Petersen T.E.; J. Biol. Chem. 259:8318-8327(1984). Cited for: PROTEIN SEQUENCE OF 24-1474, SUBUNIT, SUBCELLULAR LOCATION, TISSUESPECIFICITY, AND DISULFIDE BONDS.	6203908 [Abstract]
Thioester bond
Reference	PubMed
"Primary structure of human alpha 2-macroglobulin. V. The completestructure."; Sottrup-Jensen L., Stepanik T.M., Kristensen T., Wierzbicki D.M.,Jones C.M., Loenblad P.B., Magnusson S., Petersen T.E.; J. Biol. Chem. 259:8318-8327(1984). Cited for: PROTEIN SEQUENCE OF 24-1474, SUBUNIT, SUBCELLULAR LOCATION, TISSUESPECIFICITY, AND DISULFIDE BONDS.	6203908 [Abstract]