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Q13219

- PAPP1_HUMAN

UniProt

Q13219 - PAPP1_HUMAN

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Protein

Pappalysin-1

Gene

PAPPA

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

Functioni

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.3 Publications

Catalytic activityi

Cleavage of the 135-Met-|-Lys-136 bond in insulin-like growth factor binding protein (IGFBP)-4, and the 143-Ser-|-Lys-144 bond in IGFBP-5.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

Inhibited by complexation with the proform of PRG2.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi562 – 5621Zinc; catalyticPROSITE-ProRule annotation
Active sitei563 – 5631PROSITE-ProRule annotation
Metal bindingi566 – 5661Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi572 – 5721Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. endopeptidase activity Source: Ensembl
  2. metallopeptidase activity Source: UniProtKB
  3. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cell differentiation Source: InterPro
  2. cellular protein metabolic process Source: Reactome
  3. female pregnancy Source: UniProtKB
  4. response to follicle-stimulating hormone Source: Ensembl
  5. response to glucocorticoid Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000119398-MONOMER.
ReactomeiREACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Protein family/group databases

MEROPSiM43.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Pappalysin-1 (EC:3.4.24.79)
Alternative name(s):
Insulin-like growth factor-dependent IGF-binding protein 4 protease
Short name:
IGF-dependent IGFBP-4 protease
Short name:
IGFBP-4ase
Pregnancy-associated plasma protein A
Short name:
PAPP-A
Gene namesi
Name:PAPPA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:8602. PAPPA.

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: Ensembl
  3. membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32935.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Propeptidei23 – 80582 PublicationsPRO_0000029245Add
BLAST
Chaini81 – 16271547Pappalysin-1PRO_0000029246Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi144 ↔ 2351 PublicationPROSITE-ProRule annotation
Disulfide bondi327 ↔ 6221 PublicationPROSITE-ProRule annotation
Disulfide bondi332 ↔ 6571 PublicationPROSITE-ProRule annotation
Glycosylationi390 – 3901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi402 – 4021N-linked (GlcNAc...)1 Publication
Disulfide bondi414 ↔ 4281 PublicationPROSITE-ProRule annotation
Disulfide bondi424 ↔ 4401 PublicationPROSITE-ProRule annotation
Glycosylationi429 – 4291N-linked (GlcNAc...)1 Publication
Disulfide bondi457 ↔ 4731 PublicationPROSITE-ProRule annotation
Disulfide bondi461 – 461Interchain (with C-51 in PRG2 proform)1 PublicationPROSITE-ProRule annotation
Disulfide bondi474 ↔ 4851 PublicationPROSITE-ProRule annotation
Glycosylationi480 – 4801N-linked (GlcNAc...)1 Publication
Disulfide bondi583 ↔ 600Or C-583 with C-6121 PublicationPROSITE-ProRule annotation
Disulfide bondi587 ↔ 612Or C-587 with C-6001 PublicationPROSITE-ProRule annotation
Glycosylationi601 – 6011N-linked (GlcNAc...)1 Publication
Glycosylationi619 – 6191N-linked (GlcNAc...)1 Publication
Disulfide bondi710 ↔ 8781 PublicationPROSITE-ProRule annotation
Disulfide bondi713 ↔ 8811 PublicationPROSITE-ProRule annotation
Glycosylationi725 – 7251N-linked (GlcNAc...)1 Publication
Disulfide bondi732 – 732Interchain (with C-169 in PRG2 proform)1 PublicationPROSITE-ProRule annotation
Disulfide bondi753 ↔ 8351 PublicationPROSITE-ProRule annotation
Disulfide bondi775 ↔ 7811 PublicationPROSITE-ProRule annotation
Glycosylationi825 – 8251N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi947 ↔ 9751 PublicationPROSITE-ProRule annotation
Disulfide bondi960 ↔ 9711 PublicationPROSITE-ProRule annotation
Disulfide bondi983 ↔ 9901 PublicationPROSITE-ProRule annotation
Disulfide bondi999 ↔ 10111 PublicationPROSITE-ProRule annotation
Glycosylationi1026 – 10261N-linked (GlcNAc...)1 Publication
Disulfide bondi1036 ↔ 10701 PublicationPROSITE-ProRule annotation
Disulfide bondi1051 ↔ 11391 PublicationPROSITE-ProRule annotation
Disulfide bondi1192 ↔ 12051 PublicationPROSITE-ProRule annotation
Disulfide bondi1210 – 1210Interchain1 PublicationPROSITE-ProRule annotation
Disulfide bondi1215 ↔ 12691 PublicationPROSITE-ProRule annotation
Glycosylationi1222 – 12221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1226 – 12261N-linked (GlcNAc...)1 Publication
Disulfide bondi1227 ↔ 12381 PublicationPROSITE-ProRule annotation
Disulfide bondi1242 ↔ 12801 PublicationPROSITE-ProRule annotation
Disulfide bondi1285 ↔ 13291 PublicationPROSITE-ProRule annotation
Disulfide bondi1300 ↔ 13101 PublicationPROSITE-ProRule annotation
Disulfide bondi1314 ↔ 13421 PublicationPROSITE-ProRule annotation
Glycosylationi1323 – 13231N-linked (GlcNAc...)1 Publication
Disulfide bondi1346 ↔ 13991 PublicationPROSITE-ProRule annotation
Disulfide bondi1362 ↔ 13731 PublicationPROSITE-ProRule annotation
Disulfide bondi1377 ↔ 14101 PublicationPROSITE-ProRule annotation
Disulfide bondi1415 ↔ 14581 PublicationPROSITE-ProRule annotation
Disulfide bondi1428 ↔ 14381 PublicationPROSITE-ProRule annotation
Disulfide bondi1442 ↔ 14711 PublicationPROSITE-ProRule annotation
Glycosylationi1465 – 14651N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1478 ↔ 15391 PublicationPROSITE-ProRule annotation
Disulfide bondi1492 ↔ 15021 PublicationPROSITE-ProRule annotation
Disulfide bondi1506 ↔ 15541 PublicationPROSITE-ProRule annotation
Glycosylationi1519 – 15191N-linked (GlcNAc...)1 Publication
Disulfide bondi1558 ↔ 15761 PublicationPROSITE-ProRule annotation

Post-translational modificationi

There appear to be no free sulfhydryl groups.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ13219.
PRIDEiQ13219.

PTM databases

PhosphoSiteiQ13219.

Miscellaneous databases

PMAP-CutDBQ13219.

Expressioni

Tissue specificityi

High levels in placenta and pregnancy serum. In placenta, expressed in X cells in septa and anchoring villi, and in syncytiotrophoblasts in the chorionic villi. Lower levels are found in a variety of other tissues including kidney, myometrium, endometrium, ovaries, breast, prostate, bone marrow, colon, fibroblasts and osteoblasts.4 Publications

Developmental stagei

Present in serum and placenta during pregnancy; levels increase throughout pregnancy.2 Publications

Inductioni

By 8-bromoadenosine-3',5'-phosphate.1 Publication

Gene expression databases

BgeeiQ13219.
CleanExiHS_PAPPA.
ExpressionAtlasiQ13219. baseline and differential.
GenevestigatoriQ13219.

Organism-specific databases

HPAiCAB016724.
HPA001667.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. In pregnancy serum, predominantly found as a disulfide-linked 2:2 heterotetramer with the proform of PRG2.3 Publications

Protein-protein interaction databases

BioGridi111104. 8 interactions.
IntActiQ13219. 7 interactions.
MINTiMINT-1193478.
STRINGi9606.ENSP00000330658.

Structurei

3D structure databases

ProteinModelPortaliQ13219.
SMRiQ13219. Positions 543-660, 1191-1506.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1213 – 128270Sushi 1PROSITE-ProRule annotationAdd
BLAST
Domaini1283 – 134462Sushi 2PROSITE-ProRule annotationAdd
BLAST
Domaini1345 – 141268Sushi 3PROSITE-ProRule annotationAdd
BLAST
Domaini1413 – 147361Sushi 4PROSITE-ProRule annotationAdd
BLAST
Domaini1476 – 155681Sushi 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni272 – 583312MetalloproteaseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi24 – 8461Arg-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M43B family.Curated
Contains 5 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiNOG128309.
GeneTreeiENSGT00390000009007.
HOGENOMiHOG000067833.
HOVERGENiHBG053501.
InParanoidiQ13219.
KOiK07762.
OMAiGIQIYTL.
OrthoDBiEOG7HB58B.
PhylomeDBiQ13219.
TreeFamiTF331636.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.40.390.10. 3 hits.
InterProiIPR013320. ConA-like_dom.
IPR006558. LamG-like.
IPR024079. MetalloPept_cat_dom.
IPR011936. Myxo_disulph_rpt.
IPR000800. Notch_dom.
IPR008754. Peptidase_M43.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamiPF00066. Notch. 2 hits.
PF05572. Peptidase_M43. 1 hit.
PF00084. Sushi. 3 hits.
[Graphical view]
SMARTiSM00032. CCP. 4 hits.
SM00560. LamGL. 1 hit.
SM00004. NL. 3 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF57535. SSF57535. 4 hits.
TIGRFAMsiTIGR02232. myxo_disulf_rpt. 1 hit.
PROSITEiPS50923. SUSHI. 5 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q13219-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLWSWVLHL GLLSAALGCG LAERPRRARR DPRAGRPPRP AAGPATCATR
60 70 80 90 100
AARGRRASPP PPPPPGGAWE AVRVPRRRQQ REARGATEEP SPPSRALYFS
110 120 130 140 150
GRGEQLRLRA DLELPRDAFT LQVWLRAEGG QRSPAVITGL YDKCSYISRD
160 170 180 190 200
RGWVVGIHTI SDQDNKDPRY FFSLKTDRAR QVTTINAHRS YLPGQWVYLA
210 220 230 240 250
ATYDGQFMKL YVNGAQVATS GEQVGGIFSP LTQKCKVLML GGSALNHNYR
260 270 280 290 300
GYIEHFSLWK VARTQREILS DMETHGAHTA LPQLLLQENW DNVKHAWSPM
310 320 330 340 350
KDGSSPKVEF SNAHGFLLDT SLEPPLCGQT LCDNTEVIAS YNQLSSFRQP
360 370 380 390 400
KVVRYRVVNL YEDDHKNPTV TREQVDFQHH QLAEAFKQYN ISWELDVLEV
410 420 430 440 450
SNSSLRRRLI LANCDISKIG DENCDPECNH TLTGHDGGDC RHLRHPAFVK
460 470 480 490 500
KQHNGVCDMD CNYERFNFDG GECCDPEITN VTQTCFDPDS PHRAYLDVNE
510 520 530 540 550
LKNILKLDGS THLNIFFAKS SEEELAGVAT WPWDKEALMH LGGIVLNPSF
560 570 580 590 600
YGMPGHTHTM IHEIGHSLGL YHVFRGISEI QSCSDPCMET EPSFETGDLC
610 620 630 640 650
NDTNPAPKHK SCGDPGPGND TCGFHSFFNT PYNNFMSYAD DDCTDSFTPN
660 670 680 690 700
QVARMHCYLD LVYQGWQPSR KPAPVALAPQ VLGHTTDSVT LEWFPPIDGH
710 720 730 740 750
FFERELGSAC HLCLEGRILV QYASNASSPM PCSPSGHWSP REAEGHPDVE
760 770 780 790 800
QPCKSSVRTW SPNSAVNPHT VPPACPEPQG CYLELEFLYP LVPESLTIWV
810 820 830 840 850
TFVSTDWDSS GAVNDIKLLA VSGKNISLGP QNVFCDVPLT IRLWDVGEEV
860 870 880 890 900
YGIQIYTLDE HLEIDAAMLT STADTPLCLQ CKPLKYKVVR DPPLQMDVAS
910 920 930 940 950
ILHLNRKFVD MDLNLGSVYQ YWVITISGTE ESEPSPAVTY IHGSGYCGDG
960 970 980 990 1000
IIQKDQGEQC DDMNKINGDG CSLFCRQEVS FNCIDEPSRC YFHDGDGVCE
1010 1020 1030 1040 1050
EFEQKTSIKD CGVYTPQGFL DQWASNASVS HQDQQCPGWV IIGQPAASQV
1060 1070 1080 1090 1100
CRTKVIDLSE GISQHAWYPC TISYPYSQLA QTTFWLRAYF SQPMVAAAVI
1110 1120 1130 1140 1150
VHLVTDGTYY GDQKQETISV QLLDTKDQSH DLGLHVLSCR NNPLIIPVVH
1160 1170 1180 1190 1200
DLSQPFYHSQ AVRVSFSSPL VAISGVALRS FDNFDPVTLS SCQRGETYSP
1210 1220 1230 1240 1250
AEQSCVHFAC EKTDCPELAV ENASLNCSSS DRYHGAQCTV SCRTGYVLQI
1260 1270 1280 1290 1300
RRDDELIKSQ TGPSVTVTCT EGKWNKQVAC EPVDCSIPDH HQVYAASFSC
1310 1320 1330 1340 1350
PEGTTFGSQC SFQCRHPAQL KGNNSLLTCM EDGLWSFPEA LCELMCLAPP
1360 1370 1380 1390 1400
PVPNADLQTA RCRENKHKVG SFCKYKCKPG YHVPGSSRKS KKRAFKTQCT
1410 1420 1430 1440 1450
QDGSWQEGAC VPVTCDPPPP KFHGLYQCTN GFQFNSECRI KCEDSDASQG
1460 1470 1480 1490 1500
LGSNVIHCRK DGTWNGSFHV CQEMQGQCSV PNELNSNLKL QCPDGYAIGS
1510 1520 1530 1540 1550
ECATSCLDHN SESIILPMNV TVRDIPHWLN PTRVERVVCT AGLKWYPHPA
1560 1570 1580 1590 1600
LIHCVKGCEP FMGDNYCDAI NNRAFCNYDG GDCCTSTVKT KKVTPFPMSC
1610 1620
DLQGDCACRD PQAQEHSRKD LRGYSHG
Length:1,627
Mass (Da):180,973
Last modified:February 10, 2009 - v3
Checksum:i202ECA62C1107207
GO

Sequence cautioni

The sequence AAC50543.1 differs from that shown. Reason: Frameshift at positions 51 and 67. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071R → RV in AAC50543. (PubMed:8620868)Curated
Sequence conflicti107 – 1071R → RV in CAA48341. (PubMed:7508748)Curated
Sequence conflicti511 – 5122TH → RD AA sequence (PubMed:7508748)Curated
Sequence conflicti1622 – 16221R → Q in AAH78657. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51S → I.
Corresponds to variant rs417012 [ dbSNP | Ensembl ].
VAR_057091
Natural varianti325 – 3251P → L.
Corresponds to variant rs445159 [ dbSNP | Ensembl ].
VAR_057092
Natural varianti944 – 9441S → R.2 Publications
Corresponds to variant rs117124330 [ dbSNP | Ensembl ].
VAR_011419
Natural varianti1224 – 12241S → Y.2 Publications
Corresponds to variant rs7020782 [ dbSNP | Ensembl ].
VAR_018726

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28727 mRNA. Translation: AAC50543.1. Frameshift.
AL353141, AL137024, AL691426 Genomic DNA. Translation: CAI16083.1.
AL691426, AL137024, AL353141 Genomic DNA. Translation: CAI16715.1.
BC078657 mRNA. Translation: AAH78657.1.
X68280 mRNA. Translation: CAA48341.1.
CCDSiCCDS6813.1.
PIRiS65464.
RefSeqiNP_002572.2. NM_002581.3.
UniGeneiHs.643599.

Genome annotation databases

EnsembliENST00000328252; ENSP00000330658; ENSG00000182752.
GeneIDi5069.
KEGGihsa:5069.
UCSCiuc004bjn.3. human.

Polymorphism databases

DMDMi223590248.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28727 mRNA. Translation: AAC50543.1 . Frameshift.
AL353141 , AL137024 , AL691426 Genomic DNA. Translation: CAI16083.1 .
AL691426 , AL137024 , AL353141 Genomic DNA. Translation: CAI16715.1 .
BC078657 mRNA. Translation: AAH78657.1 .
X68280 mRNA. Translation: CAA48341.1 .
CCDSi CCDS6813.1.
PIRi S65464.
RefSeqi NP_002572.2. NM_002581.3.
UniGenei Hs.643599.

3D structure databases

ProteinModelPortali Q13219.
SMRi Q13219. Positions 543-660, 1191-1506.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111104. 8 interactions.
IntActi Q13219. 7 interactions.
MINTi MINT-1193478.
STRINGi 9606.ENSP00000330658.

Protein family/group databases

MEROPSi M43.004.

PTM databases

PhosphoSitei Q13219.

Polymorphism databases

DMDMi 223590248.

Proteomic databases

PaxDbi Q13219.
PRIDEi Q13219.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000328252 ; ENSP00000330658 ; ENSG00000182752 .
GeneIDi 5069.
KEGGi hsa:5069.
UCSCi uc004bjn.3. human.

Organism-specific databases

CTDi 5069.
GeneCardsi GC09P118916.
H-InvDB HIX0025885.
HGNCi HGNC:8602. PAPPA.
HPAi CAB016724.
HPA001667.
MIMi 176385. gene.
neXtProti NX_Q13219.
PharmGKBi PA32935.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG128309.
GeneTreei ENSGT00390000009007.
HOGENOMi HOG000067833.
HOVERGENi HBG053501.
InParanoidi Q13219.
KOi K07762.
OMAi GIQIYTL.
OrthoDBi EOG7HB58B.
PhylomeDBi Q13219.
TreeFami TF331636.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000119398-MONOMER.
Reactomei REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Miscellaneous databases

ChiTaRSi PAPPA. human.
GeneWikii Pregnancy-associated_plasma_protein_A.
GenomeRNAii 5069.
NextBioi 19534.
PMAP-CutDB Q13219.
PROi Q13219.
SOURCEi Search...

Gene expression databases

Bgeei Q13219.
CleanExi HS_PAPPA.
ExpressionAtlasi Q13219. baseline and differential.
Genevestigatori Q13219.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
3.40.390.10. 3 hits.
InterProi IPR013320. ConA-like_dom.
IPR006558. LamG-like.
IPR024079. MetalloPept_cat_dom.
IPR011936. Myxo_disulph_rpt.
IPR000800. Notch_dom.
IPR008754. Peptidase_M43.
IPR000436. Sushi_SCR_CCP.
[Graphical view ]
Pfami PF00066. Notch. 2 hits.
PF05572. Peptidase_M43. 1 hit.
PF00084. Sushi. 3 hits.
[Graphical view ]
SMARTi SM00032. CCP. 4 hits.
SM00560. LamGL. 1 hit.
SM00004. NL. 3 hits.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF57535. SSF57535. 4 hits.
TIGRFAMsi TIGR02232. myxo_disulf_rpt. 1 hit.
PROSITEi PS50923. SUSHI. 5 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete cDNA sequence of the preproform of human pregnancy-associated plasma protein-A. Evidence for expression in the brain and induction by cAMP."
    Haaning J., Oxvig C., Overgaard M.T., Ebbesen P., Kristensen T., Sottrup-Jensen L.
    Eur. J. Biochem. 237:159-163(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, VARIANT ARG-944.
    Tissue: Placenta.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [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], VARIANT TYR-1224.
    Tissue: Placenta.
  4. "Amino acid sequence of human pregnancy-associated plasma protein-A derived from cloned cDNA."
    Kristensen T., Oxvig C., Sand O., Moller N.P.H., Sottrup-Jensen L.
    Biochemistry 33:1592-1598(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 77-1627, PROTEIN SEQUENCE OF 81-98; 117-126; 210-224; 466-485; 507-519; 576-593; 609-621; 718-736; 742-754; 1006-1017; 1259-1273; 1369-1374; 1389-1398; 1490-1509; 1524-1533 AND 1537-1544, VARIANT ARG-944, TISSUE SPECIFICITY.
    Tissue: Placenta and Serum.
  5. "Circulating human pregnancy-associated plasma protein-A is disulfide-bridged to the proform of eosinophil major basic protein."
    Oxvig C., Sand O., Kristensen T., Gleich G.J., Sottrup-Jensen L.
    J. Biol. Chem. 268:12243-12246(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 81-89; 117-126; 210-224; 460-485; 507-519; 576-593; 718-736; 742-754; 1259-1273; 1369-1374; 1490-1509; 1524-1533 AND 1537-1544, SUBUNIT, INTERCHAIN DISULFIDE BOND.
    Tissue: Serum.
  6. "Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein. Disulfide structure and carbohydrate attachment 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) [PubMed] [Europe PMC] [Abstract]
    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, DISULFIDE BONDS.
  7. "The insulin-like growth factor (IGF)-dependent IGF binding protein-4 protease secreted by human fibroblasts is pregnancy-associated plasma protein-A."
    Lawrence J.B., Oxvig C., Overgaard M.T., Sottrup-Jensen L., Gleich G.J., Hays L.G., Yates J.R. III, Conover C.A.
    Proc. Natl. Acad. Sci. U.S.A. 96:3149-3153(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Fibroblast.
  8. "Expression of recombinant human pregnancy-associated plasma protein-A and identification of the proform of eosinophil major basic protein as its physiological inhibitor."
    Overgaard M.T., Haaning J., Boldt H.B., Olsen I.M., Laursen L.S., Christiansen M., Gleich G.J., Sottrup-Jensen L., Conover C.A., Oxvig C.
    J. Biol. Chem. 275:31128-31133(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, ENZYME REGULATION.
  9. "Localization of pregnancy-associated plasma protein-A and colocalization of pregnancy-associated plasma protein-A messenger ribonucleic acid and eosinophil granule major basic protein messenger ribonucleic acid in placenta."
    Bonno M., Oxvig C., Kephart G.M., Wagner J.M., Kristensen T., Sottrup-Jensen L., Gleich G.J.
    Lab. Invest. 71:560-566(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  10. "Messenger ribonucleic acid levels of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein: expression in human reproductive and nonreproductive tissues."
    Overgaard M.T., Oxvig C., Christiansen M., Lawrence J.B., Conover C.A., Gleich G.J., Sottrup-Jensen L., Haaning J.
    Biol. Reprod. 61:1083-1089(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  11. "Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma."
    Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I., Stigbrand T., Gleich G.J., Sottrup-Jensen L.
    J. Biol. Chem. 270:13645-13651(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  12. "Pregnancy-associated plasma protein-A (PAPP-A) cleaves insulin-like growth factor binding protein (IGFBP)-5 independent of IGF: implications for the mechanism of IGFBP-4 proteolysis by PAPP-A."
    Laursen L.S., Overgaard M.T., Soe R., Boldt H.B., Sottrup-Jensen L., Giudice L.C., Conover C.A., Oxvig C.
    FEBS Lett. 504:36-40(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Limb-girdle muscular dystrophy type 2H associated with mutation in TRIM32, a putative E3-ubiquitin-ligase gene."
    Frosk P., Weiler T., Nylen E., Sudha T., Greenberg C.R., Morgan K., Fujiwara T.M., Wrogemann K.
    Am. J. Hum. Genet. 70:663-672(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TYR-1224.

Entry informationi

Entry nameiPAPP1_HUMAN
AccessioniPrimary (citable) accession number: Q13219
Secondary accession number(s): B1AMF9
, Q08371, Q68G52, Q9UDK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: February 10, 2009
Last modified: November 26, 2014
This is version 161 of the entry and version 3 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 9
    Human chromosome 9: 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. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3