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Q13219 (PAPP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PAPPA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1627 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.8 Ref.12

Catalytic activity

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.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Inhibited by complexation with the proform of PRG2. Ref.8

Subunit structure

Homodimer; disulfide-linked. In pregnancy serum, predominantly found as a disulfide-linked 2:2 heterotetramer with the proform of PRG2. Ref.5 Ref.6 Ref.8

Subcellular location

Secreted Ref.7.

Tissue specificity

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. Ref.4 Ref.7 Ref.9 Ref.10

Developmental stage

Present in serum and placenta during pregnancy; levels increase throughout pregnancy. Ref.10 Ref.11

Induction

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

Post-translational modification

There appear to be no free sulfhydryl groups.

Sequence similarities

Belongs to the peptidase M43B family.

Contains 5 Sushi (CCP/SCR) domains.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 8058
PRO_0000029245
Chain81 – 16271547Pappalysin-1
PRO_0000029246

Regions

Domain1213 – 128270Sushi 1
Domain1283 – 134462Sushi 2
Domain1345 – 141268Sushi 3
Domain1413 – 147361Sushi 4
Domain1476 – 155681Sushi 5
Region272 – 583312Metalloprotease
Compositional bias24 – 8461Arg-rich

Sites

Active site5631 By similarity
Metal binding5621Zinc; catalytic By similarity
Metal binding5661Zinc; catalytic By similarity
Metal binding5721Zinc; catalytic By similarity

Amino acid modifications

Glycosylation3901N-linked (GlcNAc...) Potential
Glycosylation4021N-linked (GlcNAc...) Ref.6
Glycosylation4291N-linked (GlcNAc...) Ref.6
Glycosylation4801N-linked (GlcNAc...) Ref.6
Glycosylation6011N-linked (GlcNAc...) Ref.6
Glycosylation6191N-linked (GlcNAc...) Ref.6
Glycosylation7251N-linked (GlcNAc...) Ref.6
Glycosylation8251N-linked (GlcNAc...) Potential
Glycosylation10261N-linked (GlcNAc...) Ref.6
Glycosylation12221N-linked (GlcNAc...) Potential
Glycosylation12261N-linked (GlcNAc...) Ref.6
Glycosylation13231N-linked (GlcNAc...) Ref.6
Glycosylation14651N-linked (GlcNAc...) Potential
Glycosylation15191N-linked (GlcNAc...) Ref.6
Disulfide bond144 ↔ 235 Ref.5 Ref.6
Disulfide bond327 ↔ 622 Ref.5 Ref.6
Disulfide bond332 ↔ 657 Ref.5 Ref.6
Disulfide bond414 ↔ 428 Ref.5 Ref.6
Disulfide bond424 ↔ 440 Ref.5 Ref.6
Disulfide bond457 ↔ 473 Ref.5 Ref.6
Disulfide bond461Interchain (with C-51 in PRG2 proform) Ref.5 Ref.6
Disulfide bond474 ↔ 485 Ref.5 Ref.6
Disulfide bond583 ↔ 600Or C-583 with C-612 Ref.5 Ref.6
Disulfide bond587 ↔ 612Or C-587 with C-600 Ref.5 Ref.6
Disulfide bond710 ↔ 878 Ref.5 Ref.6
Disulfide bond713 ↔ 881 Ref.5 Ref.6
Disulfide bond732Interchain (with C-169 in PRG2 proform) Ref.5 Ref.6
Disulfide bond753 ↔ 835 Ref.5 Ref.6
Disulfide bond775 ↔ 781 Ref.5 Ref.6
Disulfide bond947 ↔ 975 Ref.5 Ref.6
Disulfide bond960 ↔ 971 Ref.5 Ref.6
Disulfide bond983 ↔ 990 Ref.5 Ref.6
Disulfide bond999 ↔ 1011 Ref.5 Ref.6
Disulfide bond1036 ↔ 1070 Ref.5 Ref.6
Disulfide bond1051 ↔ 1139 Ref.5 Ref.6
Disulfide bond1192 ↔ 1205 Ref.5 Ref.6
Disulfide bond1210Interchain Ref.5 Ref.6
Disulfide bond1215 ↔ 1269 Ref.5 Ref.6
Disulfide bond1227 ↔ 1238 Ref.5 Ref.6
Disulfide bond1242 ↔ 1280 Ref.5 Ref.6
Disulfide bond1285 ↔ 1329 Ref.5 Ref.6
Disulfide bond1300 ↔ 1310 Ref.5 Ref.6
Disulfide bond1314 ↔ 1342 Ref.5 Ref.6
Disulfide bond1346 ↔ 1399 Ref.5 Ref.6
Disulfide bond1362 ↔ 1373 Ref.5 Ref.6
Disulfide bond1377 ↔ 1410 Ref.5 Ref.6
Disulfide bond1415 ↔ 1458 Ref.5 Ref.6
Disulfide bond1428 ↔ 1438 Ref.5 Ref.6
Disulfide bond1442 ↔ 1471 Ref.5 Ref.6
Disulfide bond1478 ↔ 1539 Ref.5 Ref.6
Disulfide bond1492 ↔ 1502 Ref.5 Ref.6
Disulfide bond1506 ↔ 1554 Ref.5 Ref.6
Disulfide bond1558 ↔ 1576 Ref.5 Ref.6

Natural variations

Natural variant51S → I.
Corresponds to variant rs417012 [ dbSNP | Ensembl ].
VAR_057091
Natural variant3251P → L.
Corresponds to variant rs445159 [ dbSNP | Ensembl ].
VAR_057092
Natural variant9441S → R. Ref.1 Ref.4
Corresponds to variant rs117124330 [ dbSNP | Ensembl ].
VAR_011419
Natural variant12241S → Y. Ref.3 Ref.13
Corresponds to variant rs7020782 [ dbSNP | Ensembl ].
VAR_018726

Experimental info

Sequence conflict1071R → RV in AAC50543. Ref.1
Sequence conflict1071R → RV in CAA48341. Ref.4
Sequence conflict511 – 5122TH → RD AA sequence Ref.4
Sequence conflict16221R → Q in AAH78657. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q13219 [UniParc].

Last modified February 10, 2009. Version 3.
Checksum: 202ECA62C1107207

FASTA1,627180,973
        10         20         30         40         50         60 
MRLWSWVLHL GLLSAALGCG LAERPRRARR DPRAGRPPRP AAGPATCATR AARGRRASPP 

        70         80         90        100        110        120 
PPPPPGGAWE AVRVPRRRQQ REARGATEEP SPPSRALYFS GRGEQLRLRA DLELPRDAFT 

       130        140        150        160        170        180 
LQVWLRAEGG QRSPAVITGL YDKCSYISRD RGWVVGIHTI SDQDNKDPRY FFSLKTDRAR 

       190        200        210        220        230        240 
QVTTINAHRS YLPGQWVYLA ATYDGQFMKL YVNGAQVATS GEQVGGIFSP LTQKCKVLML 

       250        260        270        280        290        300 
GGSALNHNYR GYIEHFSLWK VARTQREILS DMETHGAHTA LPQLLLQENW DNVKHAWSPM 

       310        320        330        340        350        360 
KDGSSPKVEF SNAHGFLLDT SLEPPLCGQT LCDNTEVIAS YNQLSSFRQP KVVRYRVVNL 

       370        380        390        400        410        420 
YEDDHKNPTV TREQVDFQHH QLAEAFKQYN ISWELDVLEV SNSSLRRRLI LANCDISKIG 

       430        440        450        460        470        480 
DENCDPECNH TLTGHDGGDC RHLRHPAFVK KQHNGVCDMD CNYERFNFDG GECCDPEITN 

       490        500        510        520        530        540 
VTQTCFDPDS PHRAYLDVNE LKNILKLDGS THLNIFFAKS SEEELAGVAT WPWDKEALMH 

       550        560        570        580        590        600 
LGGIVLNPSF YGMPGHTHTM IHEIGHSLGL YHVFRGISEI QSCSDPCMET EPSFETGDLC 

       610        620        630        640        650        660 
NDTNPAPKHK SCGDPGPGND TCGFHSFFNT PYNNFMSYAD DDCTDSFTPN QVARMHCYLD 

       670        680        690        700        710        720 
LVYQGWQPSR KPAPVALAPQ VLGHTTDSVT LEWFPPIDGH FFERELGSAC HLCLEGRILV 

       730        740        750        760        770        780 
QYASNASSPM PCSPSGHWSP REAEGHPDVE QPCKSSVRTW SPNSAVNPHT VPPACPEPQG 

       790        800        810        820        830        840 
CYLELEFLYP LVPESLTIWV TFVSTDWDSS GAVNDIKLLA VSGKNISLGP QNVFCDVPLT 

       850        860        870        880        890        900 
IRLWDVGEEV YGIQIYTLDE HLEIDAAMLT STADTPLCLQ CKPLKYKVVR DPPLQMDVAS 

       910        920        930        940        950        960 
ILHLNRKFVD MDLNLGSVYQ YWVITISGTE ESEPSPAVTY IHGSGYCGDG IIQKDQGEQC 

       970        980        990       1000       1010       1020 
DDMNKINGDG CSLFCRQEVS FNCIDEPSRC YFHDGDGVCE EFEQKTSIKD CGVYTPQGFL 

      1030       1040       1050       1060       1070       1080 
DQWASNASVS HQDQQCPGWV IIGQPAASQV CRTKVIDLSE GISQHAWYPC TISYPYSQLA 

      1090       1100       1110       1120       1130       1140 
QTTFWLRAYF SQPMVAAAVI VHLVTDGTYY GDQKQETISV QLLDTKDQSH DLGLHVLSCR 

      1150       1160       1170       1180       1190       1200 
NNPLIIPVVH DLSQPFYHSQ AVRVSFSSPL VAISGVALRS FDNFDPVTLS SCQRGETYSP 

      1210       1220       1230       1240       1250       1260 
AEQSCVHFAC EKTDCPELAV ENASLNCSSS DRYHGAQCTV SCRTGYVLQI RRDDELIKSQ 

      1270       1280       1290       1300       1310       1320 
TGPSVTVTCT EGKWNKQVAC EPVDCSIPDH HQVYAASFSC PEGTTFGSQC SFQCRHPAQL 

      1330       1340       1350       1360       1370       1380 
KGNNSLLTCM EDGLWSFPEA LCELMCLAPP PVPNADLQTA RCRENKHKVG SFCKYKCKPG 

      1390       1400       1410       1420       1430       1440 
YHVPGSSRKS KKRAFKTQCT QDGSWQEGAC VPVTCDPPPP KFHGLYQCTN GFQFNSECRI 

      1450       1460       1470       1480       1490       1500 
KCEDSDASQG LGSNVIHCRK DGTWNGSFHV CQEMQGQCSV PNELNSNLKL QCPDGYAIGS 

      1510       1520       1530       1540       1550       1560 
ECATSCLDHN SESIILPMNV TVRDIPHWLN PTRVERVVCT AGLKWYPHPA LIHCVKGCEP 

      1570       1580       1590       1600       1610       1620 
FMGDNYCDAI NNRAFCNYDG GDCCTSTVKT KKVTPFPMSC DLQGDCACRD PQAQEHSRKD 


LRGYSHG 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS6813.1.
PIRS65464.
RefSeqNP_002572.2. NM_002581.3.
UniGeneHs.643599.

3D structure databases

ProteinModelPortalQ13219.
SMRQ13219. Positions 543-660, 1287-1506.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111104. 8 interactions.
IntActQ13219. 7 interactions.
MINTMINT-1193478.
STRING9606.ENSP00000330658.

Protein family/group databases

MEROPSM43.004.

PTM databases

PhosphoSiteQ13219.

Polymorphism databases

DMDM223590248.

Proteomic databases

PaxDbQ13219.
PRIDEQ13219.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328252; ENSP00000330658; ENSG00000182752.
GeneID5069.
KEGGhsa:5069.
UCSCuc004bjn.3. human.

Organism-specific databases

CTD5069.
GeneCardsGC09P118916.
H-InvDBHIX0025885.
HGNCHGNC:8602. PAPPA.
HPACAB016724.
HPA001667.
MIM176385. gene.
neXtProtNX_Q13219.
PharmGKBPA32935.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG128309.
HOGENOMHOG000067833.
HOVERGENHBG053501.
InParanoidQ13219.
KOK07762.
OMAGIQIYTL.
OrthoDBEOG7HB58B.
PhylomeDBQ13219.
TreeFamTF331636.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000119398-MONOMER.
ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ13219.
BgeeQ13219.
CleanExHS_PAPPA.
GenevestigatorQ13219.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
3.40.390.10. 3 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR006558. LamG-like.
IPR024079. MetalloPept_cat_dom.
IPR011936. Myxo_disulph_rpt.
IPR000800. Notch_dom.
IPR008754. Peptidase_M43.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF00066. Notch. 2 hits.
PF05572. Peptidase_M43. 1 hit.
PF00084. Sushi. 3 hits.
[Graphical view]
SMARTSM00032. CCP. 4 hits.
SM00560. LamGL. 1 hit.
SM00004. NL. 3 hits.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
SSF57535. SSF57535. 4 hits.
TIGRFAMsTIGR02232. myxo_disulf_rpt. 1 hit.
PROSITEPS50923. SUSHI. 5 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPAPPA. human.
GeneWikiPregnancy-associated_plasma_protein_A.
GenomeRNAi5069.
NextBio19534.
PMAP-CutDBQ13219.
PROQ13219.
SOURCESearch...

Entry information

Entry namePAPP1_HUMAN
AccessionPrimary (citable) accession number: Q13219
Secondary accession number(s): B1AMF9 expand/collapse secondary AC list , Q08371, Q68G52, Q9UDK7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: February 10, 2009
Last modified: July 9, 2014
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM