Reviewed, UniProtKB/Swiss-Prot Q13219 (PAPP1_HUMAN)

Names and origin

Protein names

Recommended name:
    Pappalysin-1
    EC=3.4.24.79
Alternative name(s):
    Pregnancy-associated plasma protein A
      Short name=PAPP-A
    Insulin-like growth factor-dependent IGF-binding protein 4 protease
      Short name=IGF-dependent IGFBP-4 protease
      Short name=IGFBP-4ase

Gene names

Name:

PAPPA

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1627 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.8 Ref.5 Ref.6
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.7 Ref.4 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.8 Ref.1
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.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Sushi
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell differentiation Inferred from electronic annotation. Source: InterPro female pregnancy Ref.7 Ref.8 Non-traceable author statement. Source: UniProtKB
Cellular component	extracellular region Ref.7 Ref.8 Inferred from direct assay. Source: UniProtKB membrane Inferred from electronic annotation. Source: InterPro
Molecular function	metallopeptidase activity Ref.7 Ref.8 Inferred from direct assay. Source: UniProtKB zinc ion binding Ref.4 Ref.7 Ref.8 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Propeptide	23 – 80	58			PRO_0000029245
	Chain	81 – 1627	1547	Pappalysin-1		PRO_0000029246
Regions
	Domain	1213 – 1282	70	Sushi 1
	Domain	1283 – 1344	62	Sushi 2
	Domain	1345 – 1412	68	Sushi 3
	Domain	1413 – 1473	61	Sushi 4
	Domain	1476 – 1556	81	Sushi 5
	Region	272 – 583	312	Metalloprotease
	Compositional bias	24 – 84	61	Arg-rich
Sites
	Active site	563	1	By similarity
	Metal binding	562	1	Zinc; catalytic By similarity
	Metal binding	566	1	Zinc; catalytic By similarity
	Metal binding	572	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	390	1	N-linked (GlcNAc...) Potential
	Glycosylation	402	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	429	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	480	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	601	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	619	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	725	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	825	1	N-linked (GlcNAc...) Potential
	Glycosylation	1026	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	1222	1	N-linked (GlcNAc...) Potential
	Glycosylation	1226	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	1323	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	1465	1	N-linked (GlcNAc...) Potential
	Glycosylation	1519	1	N-linked (GlcNAc...) Ref.6
	Disulfide bond	144 ↔ 235		Ref.5 Ref.6
	Disulfide bond	327 ↔ 622		Ref.5 Ref.6
	Disulfide bond	332 ↔ 657		Ref.5 Ref.6
	Disulfide bond	414 ↔ 428		Ref.5 Ref.6
	Disulfide bond	424 ↔ 440		Ref.5 Ref.6
	Disulfide bond	457 ↔ 473		Ref.5 Ref.6
	Disulfide bond	461		Interchain (with C-51 in PRG2 proform) Ref.5 Ref.6
	Disulfide bond	474 ↔ 485		Ref.5 Ref.6
	Disulfide bond	583 ↔ 600		Or C-583 with C-612 Ref.5 Ref.6
	Disulfide bond	587 ↔ 612		Or C-587 with C-600 Ref.5 Ref.6
	Disulfide bond	710 ↔ 878		Ref.5 Ref.6
	Disulfide bond	713 ↔ 881		Ref.5 Ref.6
	Disulfide bond	732		Interchain (with C-169 in PRG2 proform) Ref.5 Ref.6
	Disulfide bond	753 ↔ 835		Ref.5 Ref.6
	Disulfide bond	775 ↔ 781		Ref.5 Ref.6
	Disulfide bond	947 ↔ 975		Ref.5 Ref.6
	Disulfide bond	960 ↔ 971		Ref.5 Ref.6
	Disulfide bond	983 ↔ 990		Ref.5 Ref.6
	Disulfide bond	999 ↔ 1011		Ref.5 Ref.6
	Disulfide bond	1036 ↔ 1070		Ref.5 Ref.6
	Disulfide bond	1051 ↔ 1139		Ref.5 Ref.6
	Disulfide bond	1192 ↔ 1205		Ref.5 Ref.6
	Disulfide bond	1210		Interchain Ref.5 Ref.6
	Disulfide bond	1215 ↔ 1269		Ref.5 Ref.6
	Disulfide bond	1227 ↔ 1238		Ref.5 Ref.6
	Disulfide bond	1242 ↔ 1280		Ref.5 Ref.6
	Disulfide bond	1285 ↔ 1329		Ref.5 Ref.6
	Disulfide bond	1300 ↔ 1310		Ref.5 Ref.6
	Disulfide bond	1314 ↔ 1342		Ref.5 Ref.6
	Disulfide bond	1346 ↔ 1399		Ref.5 Ref.6
	Disulfide bond	1362 ↔ 1373		Ref.5 Ref.6
	Disulfide bond	1377 ↔ 1410		Ref.5 Ref.6
	Disulfide bond	1415 ↔ 1458		Ref.5 Ref.6
	Disulfide bond	1428 ↔ 1438		Ref.5 Ref.6
	Disulfide bond	1442 ↔ 1471		Ref.5 Ref.6
	Disulfide bond	1478 ↔ 1539		Ref.5 Ref.6
	Disulfide bond	1492 ↔ 1502		Ref.5 Ref.6
	Disulfide bond	1506 ↔ 1554		Ref.5 Ref.6
	Disulfide bond	1558 ↔ 1576		Ref.5 Ref.6
Natural variations
	Natural variant	5	1	S → I: dbSNP rs417012.		VAR_057091
	Natural variant	325	1	P → L: dbSNP rs445159.		VAR_057092
	Natural variant	944	1	S → R		VAR_011419
	Natural variant	1224	1	S → Y: dbSNP rs7020782. Ref.3 Ref.13		VAR_018726
Experimental info
	Sequence conflict	107	1	R → RV in AAC50543. Ref.1
	Sequence conflict	107	1	R → RV in CAA48341. Ref.4
	Sequence conflict	511 – 512	2	TH → RD AA sequence Ref.4
	Sequence conflict	1622	1	R → Q in AAH78657. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q13219-1 [UniParc]. Last modified February 10, 2009. Version 3. Checksum: 202ECA62C1107207	FASTA	1,627	180,973
	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

References

	« Hide 'large scale' referencesShow '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: 8620868] [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: 15164053] [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: 15489334] [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: 7508748] [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: 7685339] [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: 12421832] [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: 10077652] [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: 10913121] [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: 7526035] [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: 10491647] [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: 7539791] [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: 11522292] [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: 11822024] [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.
IPI	IPI00001869.
PIR	S65464.
RefSeq	NP_002572.2.
UniGene	Hs.643599 Hs.713596
3D structure databases
SMR	Q13219. Positions 352-660, 1215-1509.
ModBase	Search...
Protein-protein interaction databases
STRING	Q13219.
Protein family/group databases
MEROPS	M43.004.
Proteomic databases
PRIDE	Q13219.
Genome annotation databases
Ensembl	ENST00000328252; ENSP00000330658; ENSG00000182752; Homo sapiens. [Genome view]
GeneID	5069.
KEGG	hsa:5069.
Organism-specific databases
CTD	5069.
GeneCards	GC09P117955.
HGNC	HGNC:8602. PAPPA.
HPA	CAB016724. HPA001667.
MIM	176385. gene.
PharmGKB	PA32935.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11817.
HOGENOM	HBG447260.
HOVERGEN	Q13219.
InParanoid	Q13219.
OMA	DPRYFFS.
OrthoDB	EOG9QRKQN.
PhylomeDB	Q13219.
Enzyme and pathway databases
BRENDA	3.4.24.79. 247.
Reactome	REACT_15380. Diabetes pathways.
Gene expression databases
ArrayExpress	Q13219.
Bgee	Q13219.
CleanEx	HS_PAPPA.
Genevestigator	Q13219.
GermOnline	ENSG00000182752. Homo sapiens.
Family and domain databases
InterPro	IPR016060. Complement_control_module. IPR008985. ConA-like_lec_gl. IPR006558. LamG-like. IPR011936. Myxo_disulph_rpt. IPR000800. Notch_dom. IPR000436. Sushi_SCR_CCP. [Graphical view]
Gene3D	G3DSA:2.10.70.10. Complement_control_module. 1 hit.
Pfam	PF00066. Notch. 2 hits. PF00084. Sushi. 3 hits. [Graphical view]
SMART	SM00032. CCP. 4 hits. SM00560. LamGL. 1 hit. SM00004. NL. 3 hits. [Graphical view]
TIGRFAMs	TIGR02232. myxo_disulf_rpt. 1 hit.
PROSITE	PS50923. SUSHI. 5 hits. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	19534.
PMAP-CutDB	Q13219.
SOURCE	Search...

Entry information

Entry name

PAPP1_HUMAN

Accession

Primary (citable) accession number: Q13219
Secondary accession number(s): B1AMF9 , Q08371, Q68G52, Q9UDK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	February 10, 2009
Last modified:	February 9, 2010
This is version 116 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.