PROZ_HUMAN - dbPTM
PROZ_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PROZ_HUMAN
UniProt AC P22891
Protein Name Vitamin K-dependent protein Z
Gene Name PROZ
Organism Homo sapiens (Human).
Sequence Length 400
Subcellular Localization Secreted.
Protein Description Appears to assist hemostasis by binding thrombin and promoting its association with phospholipid vesicles. Inhibits activity of the coagulation protease factor Xa in the presence of SERPINA10, calcium and phospholipids..
Protein Sequence MAGCVPLLQGLVLVLALHRVEPSVFLPASKANDVLVRWKRAGSYLLEELFEGNLEKECYEEICVYEEAREVFENEVVTDEFWRRYKGGSPCISQPCLHNGSCQDSIWGYTCTCSPGYEGSNCELAKNECHPERTDGCQHFCLPGQESYTCSCAQGYRLGEDHKQCVPHDQCACGVLTSEKRAPDLQDLPWQVKLTNSEGKDFCGGVIIRENFVLTTAKCSLLHRNITVKTYFNRTSQDPLMIKITHVHVHMRYDADAGENDLSLLELEWPIQCPGAGLPVCTPEKDFAEHLLIPRTRGLLSGWARNGTDLGNSLTTRPVTLVEGEECGQVLNVTVTTRTYCERSSVAAMHWMDGSVVTREHRGSWFLTGVLGSQPVGGQAHMVLVTKVSRYSLWFKQIMN
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
474-carboxyglutamateRAGSYLLEELFEGNL
HHHHHHHHHHHCCCC
50.49-
47Gamma-carboxyglutamic_acidRAGSYLLEELFEGNL
HHHHHHHHHHHCCCC
50.492244898
47Gamma-carboxyglutamic_acidRAGSYLLEELFEGNL
HHHHHHHHHHHCCCC
50.492244898
484-carboxyglutamateAGSYLLEELFEGNLE
HHHHHHHHHHCCCCC
59.74-
48Gamma-carboxyglutamic_acidAGSYLLEELFEGNLE
HHHHHHHHHHCCCCC
59.742244898
48Gamma-carboxyglutamic_acidAGSYLLEELFEGNLE
HHHHHHHHHHCCCCC
59.742244898
51Gamma-carboxyglutamic_acidYLLEELFEGNLEKEC
HHHHHHHCCCCCHHH
60.852244898
514-carboxyglutamateYLLEELFEGNLEKEC
HHHHHHHCCCCCHHH
60.85-
51Gamma-carboxyglutamic_acidYLLEELFEGNLEKEC
HHHHHHHCCCCCHHH
60.852244898
554-carboxyglutamateELFEGNLEKECYEEI
HHHCCCCCHHHHHHH
51.30-
55Gamma-carboxyglutamic_acidELFEGNLEKECYEEI
HHHCCCCCHHHHHHH
51.302244898
55Gamma-carboxyglutamic_acidELFEGNLEKECYEEI
HHHCCCCCHHHHHHH
51.302244898
57Gamma-carboxyglutamic_acidFEGNLEKECYEEICV
HCCCCCHHHHHHHHH
32.722244898
57Gamma-carboxyglutamic_acidFEGNLEKECYEEICV
HCCCCCHHHHHHHHH
32.722244898
574-carboxyglutamateFEGNLEKECYEEICV
HCCCCCHHHHHHHHH
32.72-
60Gamma-carboxyglutamic_acidNLEKECYEEICVYEE
CCCHHHHHHHHHHHH
53.172244898
60Gamma-carboxyglutamic_acidNLEKECYEEICVYEE
CCCHHHHHHHHHHHH
53.172244898
604-carboxyglutamateNLEKECYEEICVYEE
CCCHHHHHHHHHHHH
53.17-
614-carboxyglutamateLEKECYEEICVYEEA
CCHHHHHHHHHHHHH
18.40-
61Gamma-carboxyglutamic_acidLEKECYEEICVYEEA
CCHHHHHHHHHHHHH
18.402244898
61Gamma-carboxyglutamic_acidLEKECYEEICVYEEA
CCHHHHHHHHHHHHH
18.402244898
66Gamma-carboxyglutamic_acidYEEICVYEEAREVFE
HHHHHHHHHHHHHHH
25.452244898
664-carboxyglutamateYEEICVYEEAREVFE
HHHHHHHHHHHHHHH
25.45-
66Gamma-carboxyglutamic_acidYEEICVYEEAREVFE
HHHHHHHHHHHHHHH
25.452244898
67Gamma-carboxyglutamic_acidEEICVYEEAREVFEN
HHHHHHHHHHHHHHC
35.032244898
67Gamma-carboxyglutamic_acidEEICVYEEAREVFEN
HHHHHHHHHHHHHHC
35.032244898
674-carboxyglutamateEEICVYEEAREVFEN
HHHHHHHHHHHHHHC
35.03-
70Gamma-carboxyglutamic_acidCVYEEAREVFENEVV
HHHHHHHHHHHCCCC
59.622244898
70Gamma-carboxyglutamic_acidCVYEEAREVFENEVV
HHHHHHHHHHHCCCC
59.622244898
704-carboxyglutamateCVYEEAREVFENEVV
HHHHHHHHHHHCCCC
59.62-
734-carboxyglutamateEEAREVFENEVVTDE
HHHHHHHHCCCCCHH
58.62-
73Gamma-carboxyglutamic_acidEEAREVFENEVVTDE
HHHHHHHHCCCCCHH
58.622244898
73Gamma-carboxyglutamic_acidEEAREVFENEVVTDE
HHHHHHHHCCCCCHH
58.622244898
754-carboxyglutamateAREVFENEVVTDEFW
HHHHHHCCCCCHHHH
31.03-
75Gamma-carboxyglutamic_acidAREVFENEVVTDEFW
HHHHHHCCCCCHHHH
31.032244898
75Gamma-carboxyglutamic_acidAREVFENEVVTDEFW
HHHHHHCCCCCHHHH
31.032244898
804-carboxyglutamateENEVVTDEFWRRYKG
HCCCCCHHHHHHHCC
37.43-
80Gamma-carboxyglutamic_acidENEVVTDEFWRRYKG
HCCCCCHHHHHHHCC
37.432244898
80Gamma-carboxyglutamic_acidENEVVTDEFWRRYKG
HCCCCCHHHHHHHCC
37.432244898
93O-linked_GlycosylationKGGSPCISQPCLHNG
CCCCCCCCCCCCCCC
34.482511201
93O-linked_GlycosylationKGGSPCISQPCLHNG
CCCCCCCCCCCCCCC
34.482511201
99N-linked_GlycosylationISQPCLHNGSCQDSI
CCCCCCCCCCCCCCC
30.9920427285
104HydroxylationLHNGSCQDSIWGYTC
CCCCCCCCCCCEEEE
46.55-
220PhosphorylationVLTTAKCSLLHRNIT
EEEECCHHHHCCCEE
33.00-
225N-linked_GlycosylationKCSLLHRNITVKTYF
CHHHHCCCEEEEEEE
24.4420427285
233N-linked_GlycosylationITVKTYFNRTSQDPL
EEEEEEECCCCCCCE
35.5919528533
301PhosphorylationPRTRGLLSGWARNGT
HHHCCCHHHHHCCCC
37.0124043423
306N-linked_GlycosylationLLSGWARNGTDLGNS
CHHHHHCCCCCCCCC
50.39UniProtKB CARBOHYD
308PhosphorylationSGWARNGTDLGNSLT
HHHHCCCCCCCCCCC
31.4424043423
313PhosphorylationNGTDLGNSLTTRPVT
CCCCCCCCCCCCCEE
25.8724043423
315PhosphorylationTDLGNSLTTRPVTLV
CCCCCCCCCCCEEEE
22.1524043423
316PhosphorylationDLGNSLTTRPVTLVE
CCCCCCCCCCEEEEC
37.9624043423
332N-linked_GlycosylationEECGQVLNVTVTTRT
CCCCCEEEEEEECCC
28.6720427285
344PhosphorylationTRTYCERSSVAAMHW
CCCEECCCCCEEEEE
13.58-
345PhosphorylationRTYCERSSVAAMHWM
CCEECCCCCEEEEEC
23.23-

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 PROZ_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PROZ_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 PROZ_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FOXG1_HUMANFOXG1physical
28514442
INT6_HUMANINTS6physical
28514442
ATP23_HUMANXRCC6BP1physical
28514442
FOXF2_HUMANFOXF2physical
28514442
SI1L2_HUMANSIPA1L2physical
28514442
SDF2L_HUMANSDF2L1physical
28514442
SIK2_HUMANSIK2physical
28514442
MP2K7_HUMANMAP2K7physical
28514442
CDC6_HUMANCDC6physical
28514442
SENP1_HUMANSENP1physical
28514442
RICTR_HUMANRICTORphysical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
TYW3_HUMANTYW3physical
28514442
MELK_HUMANMELKphysical
28514442
EGFL7_HUMANEGFL7physical
28514442
TBB8_HUMANTUBB8physical
28514442
SELN_HUMANSEPN1physical
28514442
KANK2_HUMANKANK2physical
28514442
GNL3L_HUMANGNL3Lphysical
28514442
MLF1_HUMANMLF1physical
28514442
ACOT9_HUMANACOT9physical
28514442
ETV3_HUMANETV3physical
28514442
GRP78_HUMANHSPA5physical
28514442
DNJB9_HUMANDNAJB9physical
28514442
HIG1A_HUMANHIGD1Aphysical
28514442
TBB3_HUMANTUBB3physical
28514442
N42L2_HUMANN4BP2L2physical
28514442
BCD1_HUMANZNHIT6physical
28514442
ARVC_HUMANARVCFphysical
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 PROZ_HUMAN

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Related Literatures of Post-Translational Modification

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