PAPP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PAPP1_HUMAN
• UniProt AC: Q13219
• Protein Name: Pappalysin-1
• Gene Name: PAPPA
• Organism: Homo sapiens (Human).
• Sequence Length: 1627
• Subcellular Localization: Secreted .
• Protein Description: Metalloproteinase which specifically cleaves IGFBP-4 and IGFBP-5, resulting in release of bound IGF. Cleavage of IGFBP-4 is dramatically enhanced by the presence of IGF, whereas cleavage of IGFBP-5 is slightly inhibited by the presence of IGF..
• Protein Sequence: MRLWSWVLHLGLLSAALGCGLAERPRRARRDPRAGRPPRPAAGPATCATRAARGRRASPPPPPPPGGAWEAVRVPRRRQQREARGATEEPSPPSRALYFSGRGEQLRLRADLELPRDAFTLQVWLRAEGGQRSPAVITGLYDKCSYISRDRGWVVGIHTISDQDNKDPRYFFSLKTDRARQVTTINAHRSYLPGQWVYLAATYDGQFMKLYVNGAQVATSGEQVGGIFSPLTQKCKVLMLGGSALNHNYRGYIEHFSLWKVARTQREILSDMETHGAHTALPQLLLQENWDNVKHAWSPMKDGSSPKVEFSNAHGFLLDTSLEPPLCGQTLCDNTEVIASYNQLSSFRQPKVVRYRVVNLYEDDHKNPTVTREQVDFQHHQLAEAFKQYNISWELDVLEVSNSSLRRRLILANCDISKIGDENCDPECNHTLTGHDGGDCRHLRHPAFVKKQHNGVCDMDCNYERFNFDGGECCDPEITNVTQTCFDPDSPHRAYLDVNELKNILKLDGSTHLNIFFAKSSEEELAGVATWPWDKEALMHLGGIVLNPSFYGMPGHTHTMIHEIGHSLGLYHVFRGISEIQSCSDPCMETEPSFETGDLCNDTNPAPKHKSCGDPGPGNDTCGFHSFFNTPYNNFMSYADDDCTDSFTPNQVARMHCYLDLVYQGWQPSRKPAPVALAPQVLGHTTDSVTLEWFPPIDGHFFERELGSACHLCLEGRILVQYASNASSPMPCSPSGHWSPREAEGHPDVEQPCKSSVRTWSPNSAVNPHTVPPACPEPQGCYLELEFLYPLVPESLTIWVTFVSTDWDSSGAVNDIKLLAVSGKNISLGPQNVFCDVPLTIRLWDVGEEVYGIQIYTLDEHLEIDAAMLTSTADTPLCLQCKPLKYKVVRDPPLQMDVASILHLNRKFVDMDLNLGSVYQYWVITISGTEESEPSPAVTYIHGSGYCGDGIIQKDQGEQCDDMNKINGDGCSLFCRQEVSFNCIDEPSRCYFHDGDGVCEEFEQKTSIKDCGVYTPQGFLDQWASNASVSHQDQQCPGWVIIGQPAASQVCRTKVIDLSEGISQHAWYPCTISYPYSQLAQTTFWLRAYFSQPMVAAAVIVHLVTDGTYYGDQKQETISVQLLDTKDQSHDLGLHVLSCRNNPLIIPVVHDLSQPFYHSQAVRVSFSSPLVAISGVALRSFDNFDPVTLSSCQRGETYSPAEQSCVHFACEKTDCPELAVENASLNCSSSDRYHGAQCTVSCRTGYVLQIRRDDELIKSQTGPSVTVTCTEGKWNKQVACEPVDCSIPDHHQVYAASFSCPEGTTFGSQCSFQCRHPAQLKGNNSLLTCMEDGLWSFPEALCELMCLAPPPVPNADLQTARCRENKHKVGSFCKYKCKPGYHVPGSSRKSKKRAFKTQCTQDGSWQEGACVPVTCDPPPPKFHGLYQCTNGFQFNSECRIKCEDSDASQGLGSNVIHCRKDGTWNGSFHVCQEMQGQCSVPNELNSNLKLQCPDGYAIGSECATSCLDHNSESIILPMNVTVRDIPHWLNPTRVERVVCTAGLKWYPHPALIHCVKGCEPFMGDNYCDAINNRAFCNYDGGDCCTSTVKTKKVTPFPMSCDLQGDCACRDPQAQEHSRKDLRGYSHG

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
100	Phosphorylation	PSRALYFSGRGEQLR CCCEEEECCCCCEEE	17.64	-
133	Phosphorylation	RAEGGQRSPAVITGL HHCCCCCCCCEEEEC	14.88	24719451
141	Phosphorylation	PAVITGLYDKCSYIS CCEEEECCCHHCEEE	18.07	24719451
145	Phosphorylation	TGLYDKCSYISRDRG EECCCHHCEEECCCC	31.10	24719451
390	N-linked_Glycosylation	AEAFKQYNISWELDV HHHHHHCCCEEEEEE	21.23	UniProtKB CARBOHYD
402	N-linked_Glycosylation	LDVLEVSNSSLRRRL EEEEEECCHHHHHHH	40.57	12421832
402	N-linked_Glycosylation	LDVLEVSNSSLRRRL EEEEEECCHHHHHHH	40.57	12421832
429	N-linked_Glycosylation	ENCDPECNHTLTGHD CCCCCCCCCCCCCCC	29.53	12421832
429	N-linked_Glycosylation	ENCDPECNHTLTGHD CCCCCCCCCCCCCCC	29.53	12421832
450	Ubiquitination	LRHPAFVKKQHNGVC CCCCCHHCCCCCCCC	40.02	-
480	N-linked_Glycosylation	CCDPEITNVTQTCFD CCCHHHCCEEEECCC	40.26	12421832
480	N-linked_Glycosylation	CCDPEITNVTQTCFD CCCHHHCCEEEECCC	40.26	12421832
601	N-linked_Glycosylation	FETGDLCNDTNPAPK CCCCCCCCCCCCCCC	67.45	12421832
601	N-linked_Glycosylation	FETGDLCNDTNPAPK CCCCCCCCCCCCCCC	67.45	12421832
619	N-linked_Glycosylation	CGDPGPGNDTCGFHS CCCCCCCCCCCCCCC	44.55	12421832
619	N-linked_Glycosylation	CGDPGPGNDTCGFHS CCCCCCCCCCCCCCC	44.55	12421832
658	Phosphorylation	QVARMHCYLDLVYQG HHHHHHHHHHHHHCC	6.64	22817900
725	N-linked_Glycosylation	ILVQYASNASSPMPC EEEEECCCCCCCCCC	35.35	12421832
725	N-linked_Glycosylation	ILVQYASNASSPMPC EEEEECCCCCCCCCC	35.35	12421832
739	Phosphorylation	CSPSGHWSPREAEGH CCCCCCCCCCCCCCC	14.38	24719451
825	N-linked_Glycosylation	LLAVSGKNISLGPQN EEEECCCCCCCCCCC	32.38	UniProtKB CARBOHYD
825	N-linked_Glycosylation	LLAVSGKNISLGPQN EEEECCCCCCCCCCC	32.38	12421832
886	Phosphorylation	LQCKPLKYKVVRDPP ECCCCCCEEEECCCC	19.39	22210691
917	Phosphorylation	DMDLNLGSVYQYWVI CCCCCCCCEEEEEEE	22.33	-
1026	N-linked_Glycosylation	FLDQWASNASVSHQD HHHHHHHCCCCCCCC	28.61	12421832
1026	N-linked_Glycosylation	FLDQWASNASVSHQD HHHHHHHCCCCCCCC	28.61	12421832
1105	Phosphorylation	AVIVHLVTDGTYYGD HHEEEHHCCCCCCCC	34.76	25332170
1109	Phosphorylation	HLVTDGTYYGDQKQE EHHCCCCCCCCCCCE	15.81	25332170
1110	Phosphorylation	LVTDGTYYGDQKQET HHCCCCCCCCCCCEE	17.67	25332170
1222	N-linked_Glycosylation	CPELAVENASLNCSS CCHHHCCCCCCCCCC	28.38	UniProtKB CARBOHYD
1226	N-linked_Glycosylation	AVENASLNCSSSDRY HCCCCCCCCCCCCCC	22.56	12421832
1226	N-linked_Glycosylation	AVENASLNCSSSDRY HCCCCCCCCCCCCCC	22.56	12421832
1270	Phosphorylation	PSVTVTCTEGKWNKQ CCEEEEECCCCCCCE	38.11	24667141
1323	N-linked_Glycosylation	HPAQLKGNNSLLTCM CCHHHCCCCCEEEEC	33.07	12421832
1323	N-linked_Glycosylation	HPAQLKGNNSLLTCM CCHHHCCCCCEEEEC	33.07	12421832
1381	Phosphorylation	KYKCKPGYHVPGSSR CCCCCCCCCCCCCCC	14.26	-
1465	N-linked_Glycosylation	CRKDGTWNGSFHVCQ EECCCCCCCCEEECH	35.75	UniProtKB CARBOHYD
1519	N-linked_Glycosylation	ESIILPMNVTVRDIP CEEEEECCEEECCCC	25.11	12421832
1519	N-linked_Glycosylation	ESIILPMNVTVRDIP CEEEEECCEEECCCC	25.11	12421832

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PAPP1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PAPP1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PAPP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PRG2_HUMAN	PRG2	physical	10913121
PRG2_HUMAN	PRG2	physical	12421832
PRG2_HUMAN	PRG2	physical	7685339

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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Complex of pregnancy-associated plasma protein-A and the proform ofeosinophil major basic protein. Disulfide structure and carbohydrateattachment sites.";
Overgaard M.T., Sorensen E.S., Stachowiak D., Boldt H.B.,Kristensen L., Sottrup-Jensen L., Oxvig C.;
J. Biol. Chem. 278:2106-2117(2003).
Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-402; ASN-429; ASN-480;ASN-601; ASN-619; ASN-725; ASN-1026; ASN-1226; ASN-1323 AND ASN-1519,AND DISULFIDE BONDS.
PubMed: 12421832