PZP_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PZP_MOUSE
• UniProt AC: Q61838
• Protein Name: Pregnancy zone protein
• Gene Name: Pzp
• Organism: Mus musculus (Mouse).
• Sequence Length: 1495
• 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: MRRNQLPTPAFLLLFLLLPRDATTATAKPQYVVLVPSEVYSGVPEKACVSLNHVNETVMLSLTLEYAMQQTKLLTDQAVDKDSFYCSPFTISGSPLPYTFITVEIKGPTQRFIKKKSIQIIKAESPVFVQTDKPIYKPGQIVKFRVVSVDISFRPLNETFPVVYIETPKRNRIFQWQNIHLAGGLHQLSFPLSVEPALGIYKVVVQKDSGKKIEHSFEVKEYVLPKFEVIIKMQKTMAFLEEELPITACGVYTYGKPVPGLVTLRVCRKYSRYRSTCHNQNSMSICEEFSQQADDKGCFRQVVKTKVFQLRQKGHDMKIEVEAKIKEEGTGIELTGIGSCEIANALSKLKFTKVNTNYRPGLPFSGQVLLVDEKGKPIPNKNITSVVSPLGYLSIFTTDEHGLANISIDTSNFTAPFLRVVVTYKQNHVCYDNWWLDEFHTQADHSATLVFSPSQSYIQLELVFGTLACGQTQEIRIHYLLNEDIMKNEKDLTFYYLIKARGSIFNLGSHVLSLEQGNMKGVFSLPIQVEPGMAPEAQLLIYAILPNEELVADAQNFEIEKCFANKVNLSFPSAQSLPASDTHLKVKAAPLSLCALTAVDQSVLLLKPEAKLSPQSIYNLLPGKTVQGAFFGVPVYKDHENCISGEDITHNGIVYTPKHSLGDNDAHSIFQSVGINIFTNSKIHKPRFCQEFQHYPAMGGVAPQALAVAASGPGSSFRAMGVPMMGLDYSDEINQVVEVRETVRKYFPETWIWDLVPLDVSGDGELAVKVPDTITEWKASAFCLSGTTGLGLSSTISLQAFQPFFLELTLPYSVVRGEAFTLKATVLNYMSHCIQIRVDLEISPDFLAVPVGGHENSHCICGNERKTVSWAVTPKSLGEVNFTATAEALQSPELCGNKLTEVPALVHKDTVVKSVIVEPEGIEKEQTYNTLLCPQDTELQDNWSLELPPNVVEGSARATHSVLGDILGSAMQNLQNLLQMPYGCGEQNMVLFVPNIYVLNYLNETQQLTEAIKSKAINYLISGYQRQLNYQHSDGSYSTFGNHGGGNTPGNTWLTAFVLKAFAQAQSHIFIEKTHITNAFNWLSMKQKENGCFQQSGYLLNNAMKGGVDDEVTLSAYITIALLEMPLPVTHSAVRNALFCLETAWASISQSQESHVYTKALLAYAFALAGNKAKRSELLESLNKDAVKEEDSLHWQRPGDVQKVKALSFYQPRAPSAEVEMTAYVLLAYLTSESSRPTRDLSSSDLSTASKIVKWISKQQNSHGGFSSTQDTVVALQALSKYGAATFTRSQKEVLVTIESSGTFSKTFHVNSGNRLLLQEVRLPDLPGNYVTKGSGSGCVYLQTSLKYNILPVADGKAPFALQVNTLPLNFDKAGDHRTFQIRINVSYTGERPSSNMVIVDVKMVSGFIPMKPSVKKLQDQPNIQRTEVNTNHVLIYIEKLTNQTLGFSFAVEQDIPVKNLKPAPIKVYDYYETDEFTVEEYSAPFSDGSEQGNA

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
55	N-linked_Glycosylation	CVSLNHVNETVMLSL EEECCCCCCHHHHHH		-
61	Phosphorylation	VNETVMLSLTLEYAM CCCHHHHHHHHHHHH		21183079
63	Phosphorylation	ETVMLSLTLEYAMQQ CHHHHHHHHHHHHHH		22817900
71	Phosphorylation	LEYAMQQTKLLTDQA HHHHHHHCCCCCCCC		22817900
109	Phosphorylation	TVEIKGPTQRFIKKK EEEEECCCHHEEEEC		-
157	N-linked_Glycosylation	DISFRPLNETFPVVY EEEECCCCCCCCEEE		16944957
324	Ubiquitination	MKIEVEAKIKEEGTG CEEEEEEEEECCCCC		-
353	Ubiquitination	LSKLKFTKVNTNYRP HHHCCCEECCCCCCC		-
382	N-linked_Glycosylation	GKPIPNKNITSVVSP CCCCCCCCCCCEEEC		-
405	N-linked_Glycosylation	TDEHGLANISIDTSN ECCCCCEEEEEECCC		16944957
412	N-linked_Glycosylation	NISIDTSNFTAPFLR EEEEECCCCCCCEEE		16944957
568	N-linked_Glycosylation	KCFANKVNLSFPSAQ HHHCCCCCCCCCCCC		17330941
594	S-palmitoylation	KAAPLSLCALTAVDQ CCCCHHHHHHHHCCC		28526873
644	Phosphorylation	KDHENCISGEDITHN CCCCCCCCCCCCCCC		25521595
649	Phosphorylation	CISGEDITHNGIVYT CCCCCCCCCCCEEEC		27742792
711	Phosphorylation	QALAVAASGPGSSFR HHHHHHHCCCCCCHH		23984901
715	Phosphorylation	VAASGPGSSFRAMGV HHHCCCCCCHHHCCC		23984901
716	Phosphorylation	AASGPGSSFRAMGVP HHCCCCCCHHHCCCC		23984901
866	Ubiquitination	CICGNERKTVSWAVT EECCCCCCEEEEEEC		-
881	N-linked_Glycosylation	PKSLGEVNFTATAEA CCCCCCCEEEEEHHH		17330941
914	Phosphorylation	HKDTVVKSVIVEPEG CCCCEEEEEEECCCC		29109428
942	N-linked_Glycosylation	QDTELQDNWSLELPP CCCCCCCCCEEECCC		-
1003	N-linked_Glycosylation	IYVLNYLNETQQLTE EEEHHCCCHHHHHHH		16944957
1015	Ubiquitination	LTEAIKSKAINYLIS HHHHHHHHHHHHHHH		-
1019	Nitration	IKSKAINYLISGYQR HHHHHHHHHHHHHHH		-
1024	Nitration	INYLISGYQRQLNYQ HHHHHHHHHHHCCCC		-
1088	Ubiquitination	NWLSMKQKENGCFQQ HHHHHHCHHCCCCHH		-
1184	Ubiquitination	ELLESLNKDAVKEED HHHHHHCHHCCCHHH		-
1205	Ubiquitination	PGDVQKVKALSFYQP CCCCCEEEEEEEECC		-
1242	Phosphorylation	SRPTRDLSSSDLSTA CCCCCCCCCCHHHHH		23984901
1243	Phosphorylation	RPTRDLSSSDLSTAS CCCCCCCCCHHHHHH		23984901
1258	Ubiquitination	KIVKWISKQQNSHGG HHHHHHHHCCCCCCC		-
1281	Ubiquitination	VALQALSKYGAATFT HHHHHHHHHCCEEEE		-
1282	Phosphorylation	ALQALSKYGAATFTR HHHHHHHHCCEEEEC		-
1286	Phosphorylation	LSKYGAATFTRSQKE HHHHCCEEEECCCCE		-
1288	Phosphorylation	KYGAATFTRSQKEVL HHCCEEEECCCCEEE		-
1290	Phosphorylation	GAATFTRSQKEVLVT CCEEEECCCCEEEEE		-
1330	Nitration	LPDLPGNYVTKGSGS CCCCCCCEEECCCCC		-
1385	N-linked_Glycosylation	RTFQIRINVSYTGER CEEEEEEEEEECCCC		16944957
1443	N-linked_Glycosylation	IYIEKLTNQTLGFSF EEEEEHHCCCCCEEE		16944957

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of PZP_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.