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Protein

Pregnancy zone protein

Gene

PZP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. endopeptidase inhibitor activity Source: UniProtKB
  2. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

GO - Biological processi

  1. female pregnancy Source: UniProtKB
  2. negative regulation of endopeptidase activity Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI39.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Pregnancy zone protein
Alternative name(s):
C3 and PZP-like alpha-2-macroglobulin domain-containing protein 6
Gene namesi
Name:PZP
Synonyms:CPAMD6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:9750. PZP.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProtKB
  2. extracellular region Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Add
BLAST
Chaini26 – 14821457Pregnancy zone proteinPRO_0000000063Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi24 – 241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi54 – 541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi69 – 691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi246 – 2461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi392 – 3921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi406 – 4061N-linked (GlcNAc...)1 Publication
Glycosylationi753 – 7531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi875 – 8751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi932 – 9321N-linked (GlcNAc...)1 Publication
Cross-linki978 ↔ 981Isoglutamyl cysteine thioester (Cys-Gln)
Glycosylationi997 – 9971N-linked (GlcNAc...)2 Publications
Glycosylationi1430 – 14301N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Thioester bond

Proteomic databases

MaxQBiP20742.
PaxDbiP20742.
PRIDEiP20742.

PTM databases

PhosphoSiteiP20742.

Expressioni

Tissue specificityi

Plasma. Prominent constituent of late-pregnancy sera.

Gene expression databases

BgeeiP20742.
ExpressionAtlasiP20742. baseline and differential.
GenevestigatoriP20742.

Organism-specific databases

HPAiHPA041403.
HPA041471.

Interactioni

Subunit structurei

Homotetramer, which consists of two pairs of disulfide-linked chains.

Protein-protein interaction databases

STRINGi9606.ENSP00000261336.

Structurei

3D structure databases

ProteinModelPortaliP20742.
SMRiP20742. Positions 126-226, 1346-1474.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni685 – 73551Bait regionAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Bait region, Signal

Phylogenomic databases

eggNOGiCOG2373.
GeneTreeiENSGT00760000118982.
HOGENOMiHOG000220939.
HOVERGENiHBG000039.
InParanoidiP20742.
OMAiWIWELVA.
OrthoDBiEOG7DJSKB.
PhylomeDBiP20742.
TreeFamiTF313285.

Family and domain databases

Gene3Di1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProiIPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR014756. Ig_E-set.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR010916. TonB_box_CS.
[Graphical view]
PfamiPF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF10569. Thiol-ester_cl. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P20742-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRKDRLLHLC LVLLLILLSA SDSNSTEPQY MVLVPSLLHT EAPKKGCVLL
60 70 80 90 100
SHLNETVTVS ASLESGRENR SLFTDLVAEK DLFHCVSFTL PRISASSEVA
110 120 130 140 150
FLSIQIKGPT QDFRKRNTVL VLNTQSLVFV QTDKPMYKPG QTVRFRVVSV
160 170 180 190 200
DENFRPRNEL IPLIYLENPR RNRIAQWQSL KLEAGINQLS FPLSSEPIQG
210 220 230 240 250
SYRVVVQTES GGRIQHPFTV EEFVLPKFEV KVQVPKIISI MDEKVNITVC
260 270 280 290 300
GEYTYGKPVP GLATVSLCRK LSRVLNCDKQ EVCEEFSQQL NSNGCITQQV
310 320 330 340 350
HTKMLQITNT GFEMKLRVEA RIREEGTDLE VTANRISEIT NIVSKLKFVK
360 370 380 390 400
VDSHFRQGIP FFAQVLLVDG KGVPIPNKLF FISVNDANYY SNATTNEQGL
410 420 430 440 450
AQFSINTTSI SVNKLFVRVF TVHPNLCFHY SWVAEDHQGA QHTANRVFSL
460 470 480 490 500
SGSYIHLEPV AGTLPCGHTE TITAHYTLNR QAMGELSELS FHYLIMAKGV
510 520 530 540 550
IVRSGTHTLP VESGDMKGSF ALSFPVESDV APIARMFIFA ILPDGEVVGD
560 570 580 590 600
SEKFEIENCL ANKVDLSFSP AQSPPASHAH LQVAAAPQSL CALRAVDQSV
610 620 630 640 650
LLMKPEAELS VSSVYNLLTV KDLTNFPDNV DQQEEEQGHC PRPFFIHNGA
660 670 680 690 700
IYVPLSSNEA DIYSFLKGMG LKVFTNSKIR KPKSCSVIPS VSAGAVGQGY
710 720 730 740 750
YGAGLGVVER PYVPQLGTYN VIPLNNEQSS GPVPETVRSY FPETWIWELV
760 770 780 790 800
AVNSSGVAEV GVTVPDTITE WKAGAFCLSE DAGLGISSTA SLRAFQPFFV
810 820 830 840 850
ELTMPYSVIR GEVFTLKATV LNYLPKCIRV SVQLKASPAF LASQNTKGEE
860 870 880 890 900
SYCICGNERQ TLSWTVTPKT LGNVNFSVSA EAMQSLELCG NEVVEVPEIK
910 920 930 940 950
RKDTVIKTLL VEAEGIEQEK TFSSMTCASG ANVSEQLSLK LPSNVVKESA
960 970 980 990 1000
RASFSVLGDI LGSAMQNIQN LLQMPYGCGE QNMVLFAPNI YVLNYLNETQ
1010 1020 1030 1040 1050
QLTQEIKAKA VGYLITGYQR QLNYKHQDGS YSTFGERYGR NQGNTWLTAF
1060 1070 1080 1090 1100
VLKTFAQARS YIFIDEAHIT QSLTWLSQMQ KDNGCFRSSG SLLNNAIKGG
1110 1120 1130 1140 1150
VEDEATLSAY VTIALLEIPL PVTNPIVRNA LFCLESAWNV AKEGTHGSHV
1160 1170 1180 1190 1200
YTKALLAYAF SLLGKQNQNR EILNSLDKEA VKEDNLVHWE RPQRPKAPVG
1210 1220 1230 1240 1250
HLYQTQAPSA EVEMTSYVLL AYLTAQPAPT SGDLTSATNI VKWIMKQQNA
1260 1270 1280 1290 1300
QGGFSSTQDT VVALHALSRY GAATFTRTEK TAQVTVQDSQ TFSTNFQVDN
1310 1320 1330 1340 1350
NNLLLLQQIS LPELPGEYVI TVTGERCVYL QTSMKYNILP EKEDSPFALK
1360 1370 1380 1390 1400
VQTVPQTCDG HKAHTSFQIS LTISYTGNRP ASNMVIVDVK MVSGFIPLKP
1410 1420 1430 1440 1450
TVKMLERSSS VSRTEVSNNH VLIYVEQVTN QTLSFSFMVL QDIPVGDLKP
1460 1470 1480
AIVKVYDYYE TDESVVAEYI APCSTDTEHG NV
Length:1,482
Mass (Da):163,863
Last modified:December 15, 2009 - v4
Checksum:iFA89A47458C4A18B
GO
Isoform 2 (identifier: P20742-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-131: Missing.
     132-142: TDKPMYKPGQT → MSESYRRTTFP
     830-912: Missing.

Note: No experimental confirmation available.

Show »
Length:1,268
Mass (Da):140,368
Checksum:i8D3255FD5698667E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti753 – 7531N → Q AA sequence (PubMed:2476433)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti379 – 3791L → V.
Corresponds to variant rs12230214 [ dbSNP | Ensembl ].
VAR_034429
Natural varianti691 – 6911V → M.1 Publication
Corresponds to variant rs3213832 [ dbSNP | Ensembl ].
VAR_021845
Natural varianti813 – 8131V → A.
Corresponds to variant rs2277413 [ dbSNP | Ensembl ].
VAR_020005
Natural varianti857 – 8571N → S.1 Publication
Corresponds to variant rs3213831 [ dbSNP | Ensembl ].
VAR_060733
Natural varianti1003 – 10031T → M.
Corresponds to variant rs57006764 [ dbSNP | Ensembl ].
VAR_060982
Natural varianti1128 – 11281R → H in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036235
Natural varianti1205 – 12051T → P.1 Publication
Corresponds to variant rs2377741 [ dbSNP | Ensembl ].
VAR_060734
Natural varianti1443 – 14431I → N.
Corresponds to variant rs10842971 [ dbSNP | Ensembl ].
VAR_024358

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 131131Missing in isoform 2. 1 PublicationVSP_030862Add
BLAST
Alternative sequencei132 – 14211TDKPMYKPGQT → MSESYRRTTFP in isoform 2. 1 PublicationVSP_030863Add
BLAST
Alternative sequencei830 – 91283Missing in isoform 2. 1 PublicationVSP_030864Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54380 mRNA. Translation: CAA38255.1.
AC010175 Genomic DNA. No translation available.
BC111756 mRNA. Translation: AAI11757.1.
X51541 Genomic DNA. Translation: CAA35919.1.
M24416 Genomic DNA. Translation: AAA60234.1.
CCDSiCCDS8600.1. [P20742-1]
PIRiS13495.
S29738.
UniGeneiHs.707491.

Genome annotation databases

EnsembliENST00000261336; ENSP00000261336; ENSG00000126838. [P20742-1]
UCSCiuc001qvl.3. human. [P20742-1]
uc009zgl.3. human. [P20742-2]

Polymorphism databases

DMDMi281185515.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54380 mRNA. Translation: CAA38255.1.
AC010175 Genomic DNA. No translation available.
BC111756 mRNA. Translation: AAI11757.1.
X51541 Genomic DNA. Translation: CAA35919.1.
M24416 Genomic DNA. Translation: AAA60234.1.
CCDSiCCDS8600.1. [P20742-1]
PIRiS13495.
S29738.
UniGeneiHs.707491.

3D structure databases

ProteinModelPortaliP20742.
SMRiP20742. Positions 126-226, 1346-1474.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000261336.

Protein family/group databases

MEROPSiI39.003.

PTM databases

PhosphoSiteiP20742.

Polymorphism databases

DMDMi281185515.

Proteomic databases

MaxQBiP20742.
PaxDbiP20742.
PRIDEiP20742.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261336; ENSP00000261336; ENSG00000126838. [P20742-1]
UCSCiuc001qvl.3. human. [P20742-1]
uc009zgl.3. human. [P20742-2]

Organism-specific databases

GeneCardsiGC12M009301.
H-InvDBHIX0036869.
HGNCiHGNC:9750. PZP.
HPAiHPA041403.
HPA041471.
MIMi176420. gene.
neXtProtiNX_P20742.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2373.
GeneTreeiENSGT00760000118982.
HOGENOMiHOG000220939.
HOVERGENiHBG000039.
InParanoidiP20742.
OMAiWIWELVA.
OrthoDBiEOG7DJSKB.
PhylomeDBiP20742.
TreeFamiTF313285.

Miscellaneous databases

PROiP20742.
SOURCEiSearch...

Gene expression databases

BgeeiP20742.
ExpressionAtlasiP20742. baseline and differential.
GenevestigatoriP20742.

Family and domain databases

Gene3Di1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProiIPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR014756. Ig_E-set.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR010916. TonB_box_CS.
[Graphical view]
PfamiPF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF10569. Thiol-ester_cl. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of pregnancy zone protein. Molecular cloning of a full-length PZP cDNA clone by the polymerase chain reaction."
    Devriendt K., van den Berghe H., Cassiman J.-J., Marynen P.
    Biochim. Biophys. Acta 1088:95-103(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-857.
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT PRO-1205.
  4. "Alpha-macroglobulin domain structure studied by specific limited proteolysis."
    Thomsen N.K., Sottrup-Jensen L.
    Arch. Biochem. Biophys. 300:327-334(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-37; 222-230; 720-733; 896-902; 1003-1008; 1056-1061; 1184-1193; 1197-1224; 1277-1286 AND 1336-1344 (ISOFORM 1).
  5. "A genetic polymorphism in a functional domain of human pregnancy zone protein: the bait region. Genomic structure of the bait domains of human pregnancy zone protein and alpha 2 macroglobulin."
    Marynen P., Devriendt K., van den Berghe H., Cassiman J.-J.
    FEBS Lett. 262:349-352(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 668-753, VARIANT MET-691.
    Tissue: Placenta.
  6. "The alpha-macroglobulin bait region. Sequence diversity and localization of cleavage sites for proteinases in five mammalian alpha-macroglobulins."
    Sottrup-Jensen L., Sand O., Kristensen L., Fey G.H.
    J. Biol. Chem. 264:15781-15789(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 670-759.
  7. "Characterization of human pregnancy zone protein. Comparison with human alpha 2-macroglobulin."
    Sand O., Folkersen J., Westergaard J.G., Sottrup-Jensen L.
    J. Biol. Chem. 260:15723-15735(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 974-983.
  8. "A cluster of alpha 2-macroglobulin-related genes (alpha 2 M) on human chromosome 12p: cloning of the pregnancy-zone protein gene and an alpha 2M pseudogene."
    Devriendt K., Zhang J., van Leuven F., van den Berghe H., Cassiman J.-J., Marynen P.
    Gene 81:325-334(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1259-1461.
  9. "Pregnancy zone protein, a proteinase-binding macroglobulin. Interactions with proteinases and methylamine."
    Christensen U., Simonsen M., Harrit N., Sottrup-Jensen L.
    Biochemistry 28:9324-9331(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PROTEINASES AND METHYLAMINE.
  10. "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) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406; ASN-932; ASN-997 AND ASN-1430.
    Tissue: Plasma.
  11. "Glycoproteomics analysis of human liver tissue by combination of multiple 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-997.
    Tissue: Liver.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-1128.

Entry informationi

Entry nameiPZP_HUMAN
AccessioniPrimary (citable) accession number: P20742
Secondary accession number(s): A6ND27
, Q15273, Q2NKL2, Q7M4N7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: December 15, 2009
Last modified: January 7, 2015
This is version 136 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.