Q9BXP8 (PAPP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pappalysin-2
EC=3.4.24.-

Alternative name(s):
Pregnancy-associated plasma protein A2
Short name=PAPP-A2
Pregnancy-associated plasma protein E1
Short name=PAPP-E

Gene names

Name:	PAPPA2
Synonyms:	PLAC3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1791 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-5. Shows limited proteolysis toward IGFBP-3. Ref.1
Catalytic activity	Cleavage of the 143-Ser-|-Lys-144 bond in insulin-like growth factor binding protein (IGFBP)-5.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Monomer.
Subcellular location	Secreted By similarity.
Tissue specificity	Expressed abundantly in placenta, and non-pregnant mammary gland with low expression in the kidney, fetal brain and pancreas. Ref.1 Ref.2
Sequence similarities	Belongs to the peptidase M43B family. Contains 5 Sushi (CCP/SCR) domains.
Sequence caution	The sequence AAL17779.1 differs from that shown. Reason: Erroneous initiation. The sequence AAL17780.1 differs from that shown. Reason: Erroneous initiation. The sequence CAC11134.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Alternative splicing 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 Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: InterPro cellular protein metabolic process Traceable author statement. Source: Reactome proteolysis Inferred from direct assay Ref.1. Source: UniProtKB regulation of cell growth Non-traceable author statement Ref.1. Source: UniProtKB
Cellular_component	extracellular region Traceable author statement. Source: Reactome intracellular Non-traceable author statement Ref.1. Source: UniProtKB membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	metallopeptidase activity Inferred from direct assay Ref.1. Source: UniProtKB zinc ion binding Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BXP8-1)

Also known as: Papp-e(1);

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.

Isoform 2 (identifier: Q9BXP8-2)

Also known as: Papp-e(2);

The sequence of this isoform differs from the canonical sequence as follows:
     811-827: DDNCTDNFTPNQVARMH → GITTVLFCFLLRIHGGL
     828-1791: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Propeptide	23 – 234	212			PRO_0000029249
	Chain	235 – 1791	1557	Pappalysin-2		PRO_0000029250
Regions
	Domain	1393 – 1461	69	Sushi 1
	Domain	1462 – 1521	60	Sushi 2
	Domain	1523 – 1592	70	Sushi 3
	Domain	1593 – 1648	56	Sushi 4
	Domain	1651 – 1731	81	Sushi 5
	Region	442 – 754	313	Metalloprotease
	Compositional bias	171 – 174	4	Poly-Thr
	Compositional bias	1654 – 1657	4	Poly-Pro
Sites
	Active site	734	1
	Metal binding	733	1	Zinc; catalytic By similarity
	Metal binding	737	1	Zinc; catalytic By similarity
	Metal binding	743	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	311	1	N-linked (GlcNAc...) Potential
	Glycosylation	562	1	N-linked (GlcNAc...) Potential
	Glycosylation	574	1	N-linked (GlcNAc...) Potential
	Glycosylation	679	1	N-linked (GlcNAc...) Potential
	Glycosylation	813	1	N-linked (GlcNAc...) Potential
	Glycosylation	857	1	N-linked (GlcNAc...) Potential
	Glycosylation	941	1	N-linked (GlcNAc...) Potential
	Glycosylation	1243	1	N-linked (GlcNAc...) Potential
	Glycosylation	1308	1	N-linked (GlcNAc...) Potential
	Glycosylation	1326	1	N-linked (GlcNAc...) Potential
	Glycosylation	1344	1	N-linked (GlcNAc...) Potential
	Glycosylation	1408	1	N-linked (GlcNAc...) Potential
	Glycosylation	1456	1	N-linked (GlcNAc...) Potential
	Glycosylation	1476	1	N-linked (GlcNAc...) Potential
	Glycosylation	1694	1	N-linked (GlcNAc...) Potential
	Disulfide bond	312 ↔ 403		By similarity
	Disulfide bond	499 ↔ 793		By similarity
	Disulfide bond	504 ↔ 828		By similarity
	Disulfide bond	586 ↔ 600		By similarity
	Disulfide bond	596 ↔ 612		By similarity
	Disulfide bond	628 ↔ 644		By similarity
	Disulfide bond	645 ↔ 656		By similarity
	Disulfide bond	754 ↔ 771		Or C-754 with C-783 By similarity
	Disulfide bond	758 ↔ 783		Or C-788 with C-771 By similarity
	Disulfide bond	881 ↔ 1045		By similarity
	Disulfide bond	884 ↔ 1048		By similarity
	Disulfide bond	924 ↔ 1003		By similarity
	Disulfide bond	946 ↔ 951		By similarity
	Disulfide bond	1115 ↔ 1143		By similarity
	Disulfide bond	1128 ↔ 1139		By similarity
	Disulfide bond	1151 ↔ 1158		By similarity
	Disulfide bond	1167 ↔ 1179		By similarity
	Disulfide bond	1205 ↔ 1238		By similarity
	Disulfide bond	1219 ↔ 1318		By similarity
	Disulfide bond	1371 ↔ 1385		By similarity
	Disulfide bond	1396 ↔ 1448		By similarity
	Disulfide bond	1423 ↔ 1459		By similarity
	Disulfide bond	1464 ↔ 1508		By similarity
	Disulfide bond	1479 ↔ 1489		By similarity
	Disulfide bond	1493 ↔ 1521		By similarity
	Disulfide bond	1525 ↔ 1579		By similarity
	Disulfide bond	1541 ↔ 1552		By similarity
	Disulfide bond	1556 ↔ 1590		By similarity
	Disulfide bond	1595 ↔ 1633		By similarity
	Disulfide bond	1608 ↔ 1618		By similarity
	Disulfide bond	1622 ↔ 1646		By similarity
	Disulfide bond	1653 ↔ 1714		By similarity
	Disulfide bond	1667 ↔ 1677		By similarity
	Disulfide bond	1681 ↔ 1729		By similarity
	Disulfide bond	1733 ↔ 1751		By similarity
Natural variations
	Alternative sequence	811 – 827	17	DDNCT…VARMH → GITTVLFCFLLRIHGGL in isoform 2.		VSP_012194
	Alternative sequence	828 – 1791	964	Missing in isoform 2.		VSP_012195
	Natural variant	171	1	T → S. Corresponds to variant rs36112782 [ dbSNP | Ensembl ].		VAR_051595
	Natural variant	1657	1	P → R. Corresponds to variant rs34602579 [ dbSNP | Ensembl ].		VAR_051596
Experimental info
	Mutagenesis	734	1	E → Q: Loss of activity. Ref.1
	Sequence conflict	447	1	G → E in AAL17779. Ref.2
	Sequence conflict	447	1	G → E in CAC11134. Ref.6
	Sequence conflict	568	1	S → N in AAL17780. Ref.2
	Sequence conflict	846	1	I → T in AAL17779. Ref.2
	Sequence conflict	846	1	I → T in CAC11134. Ref.6
	Sequence conflict	1343	1	L → P in AAL17779. Ref.2
	Sequence conflict	1343	1	L → P in CAC11134. Ref.6
	Sequence conflict	1739	1	D → N in CAC11134. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Papp-e(1)) [UniParc]. Last modified February 20, 2007. Version 4. Checksum: F436030821EC6EDD	FASTA	1,791	198,539
	10 20 30 40 50 60 MMCLKILRIS LAILAGWALC SANSELGWTR KKSLVEREHL NQVLLEGERC WLGAKVRRPR 70 80 90 100 110 120 ASPQHHLFGV YPSRAGNYLR PYPVGEQEIH HTGRSKPDTE GNAVSLVPPD LTENPAGLRG 130 140 150 160 170 180 AVEEPAAPWV GDSPIGQSEL LGDDDAYLGN QRSKESLGEA GIQKGSAMAA TTTTAIFTTL 190 200 210 220 230 240 NEPKPETQRR GWAKSRQRRQ VWKRRAEDGQ GDSGISSHFQ PWPKHSLKHR VKKSPPEESN 250 260 270 280 290 300 QNGGEGSYRE AETFNSQVGL PILYFSGRRE RLLLRPEVLA EIPREAFTVE AWVKPEGGQN 310 320 330 340 350 360 NPAIIAGVFD NCSHTVSDKG WALGIRSGKD KGKRDARFFF SLCTDRVKKA TILISHSRYQ 370 380 390 400 410 420 PGTWTHVAAT YDGRHMALYV DGTQVASSLD QSGPLNSPFM ASCRSLLLGG DSSEDGHYFR 430 440 450 460 470 480 GHLGTLVFWS TALPQSHFQH SSQHSSGEEE ATDLVLTASF EPVNTEWVPF RDEKYPRLEV 490 500 510 520 530 540 LQGFEPEPEI LSPLQPPLCG QTVCDNVELI SQYNGYWPLR GEKVIRYQVV NICDDEGLNP 550 560 570 580 590 600 IVSEEQIRLQ HEALNEAFSR YNISWQLSVH QVHNSTLRHR VVLVNCEPSK IGNDHCDPEC 610 620 630 640 650 660 EHPLTGYDGG DCRLQGRCYS WNRRDGLCHV ECNNMLNDFD DGDCCDPQVA DVRKTCFDPD 670 680 690 700 710 720 SPKRAYMSVK ELKEALQLNS THFLNIYFAS SVREDLAGAA TWPWDKDAVT HLGGIVLSPA 730 740 750 760 770 780 YYGMPGHTDT MIHEVGHVLG LYHVFKGVSE RESCNDPCKE TVPSMETGDL CADTAPTPKS 790 800 810 820 830 840 ELCREPEPTS DTCGFTRFPG APFTNYMSYT DDNCTDNFTP NQVARMHCYL DLVYQQWTES 850 860 870 880 890 900 RKPTPIPIPP MVIGQTNKSL TIHWLPPISG VVYDRASGSL CGACTEDGTF RQYVHTASSR 910 920 930 940 950 960 RVCDSSGYWT PEEAVGPPDV DQPCEPSLQA WSPEVHLYHM NMTVPCPTEG CSLELLFQHP 970 980 990 1000 1010 1020 VQADTLTLWV TSFFMESSQV LFDTEILLEN KESVHLGPLD TFCDIPLTIK LHVDGKVSGV 1030 1040 1050 1060 1070 1080 KVYTFDERIE IDAALLTSQP HSPLCSGCRP VRYQVLRDPP FASGLPVVVT HSHRKFTDVE 1090 1100 1110 1120 1130 1140 VTPGQMYQYQ VLAEAGGELG EASPPLNHIH GAPYCGDGKV SERLGEECDD GDLVSGDGCS 1150 1160 1170 1180 1190 1200 KVCELEEGFN CVGEPSLCYM YEGDGICEPF ERKTSIVDCG IYTPKGYLDQ WATRAYSSHE 1210 1220 1230 1240 1250 1260 DKKKCPVSLV TGEPHSLICT SYHPDLPNHR PLTGWFPCVA SENETQDDRS EQPEGSLKKE 1270 1280 1290 1300 1310 1320 DEVWLKVCFN RPGEARAIFI FLTTDGLVPG EHQQPTVTLY LTDVRGSNHS LGTYGLSCQH 1330 1340 1350 1360 1370 1380 NPLIINVTHH QNVLFHHTTS VLLNFSSPRV GISAVALRTS SRIGLSAPSN CISEDEGQNH 1390 1400 1410 1420 1430 1440 QGQSCIHRPC GKQDSCPSLL LDHADVVNCT SIGPGLMKCA ITCQRGFALQ ASSGQYIRPM 1450 1460 1470 1480 1490 1500 QKEILLTCSS GHWDQNVSCL PVDCGVPDPS LVNYANFSCS EGTKFLKRCS ISCVPPAKLQ 1510 1520 1530 1540 1550 1560 GLSPWLTCLE DGLWSLPEVY CKLECDAPPI ILNANLLLPH CLQDNHDVGT ICKYECKPGY 1570 1580 1590 1600 1610 1620 YVAESAEGKV RNKLLKIQCL EGGIWEQGSC IPVVCEPPPP VFEGMYECTN GFSLDSQCVL 1630 1640 1650 1660 1670 1680 NCNQEREKLP ILCTKEGLWT QEFKLCENLQ GECPPPPSEL NSVEYKCEQG YGIGAVCSPL 1690 1700 1710 1720 1730 1740 CVIPPSDPVM LPENITADTL EHWMEPVKVQ SIVCTGRRQW HPDPVLVHCI QSCEPFQADG 1750 1760 1770 1780 1790 WCDTINNRAY CHYDGGDCCS STLSSKKVIP FAADCDLDEC TCRDPKAEEN Q
	Isoform 2 (Papp-e(2)) [UniParc]. Checksum: FB3B6F1E944F7C24	FASTA	827	92,136
	10 20 30 40 50 60 MMCLKILRIS LAILAGWALC SANSELGWTR KKSLVEREHL NQVLLEGERC WLGAKVRRPR 70 80 90 100 110 120 ASPQHHLFGV YPSRAGNYLR PYPVGEQEIH HTGRSKPDTE GNAVSLVPPD LTENPAGLRG 130 140 150 160 170 180 AVEEPAAPWV GDSPIGQSEL LGDDDAYLGN QRSKESLGEA GIQKGSAMAA TTTTAIFTTL 190 200 210 220 230 240 NEPKPETQRR GWAKSRQRRQ VWKRRAEDGQ GDSGISSHFQ PWPKHSLKHR VKKSPPEESN 250 260 270 280 290 300 QNGGEGSYRE AETFNSQVGL PILYFSGRRE RLLLRPEVLA EIPREAFTVE AWVKPEGGQN 310 320 330 340 350 360 NPAIIAGVFD NCSHTVSDKG WALGIRSGKD KGKRDARFFF SLCTDRVKKA TILISHSRYQ 370 380 390 400 410 420 PGTWTHVAAT YDGRHMALYV DGTQVASSLD QSGPLNSPFM ASCRSLLLGG DSSEDGHYFR 430 440 450 460 470 480 GHLGTLVFWS TALPQSHFQH SSQHSSGEEE ATDLVLTASF EPVNTEWVPF RDEKYPRLEV 490 500 510 520 530 540 LQGFEPEPEI LSPLQPPLCG QTVCDNVELI SQYNGYWPLR GEKVIRYQVV NICDDEGLNP 550 560 570 580 590 600 IVSEEQIRLQ HEALNEAFSR YNISWQLSVH QVHNSTLRHR VVLVNCEPSK IGNDHCDPEC 610 620 630 640 650 660 EHPLTGYDGG DCRLQGRCYS WNRRDGLCHV ECNNMLNDFD DGDCCDPQVA DVRKTCFDPD 670 680 690 700 710 720 SPKRAYMSVK ELKEALQLNS THFLNIYFAS SVREDLAGAA TWPWDKDAVT HLGGIVLSPA 730 740 750 760 770 780 YYGMPGHTDT MIHEVGHVLG LYHVFKGVSE RESCNDPCKE TVPSMETGDL CADTAPTPKS 790 800 810 820 ELCREPEPTS DTCGFTRFPG APFTNYMSYT GITTVLFCFL LRIHGGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Pregnancy-associated plasma protein-A2 (PAPP-A2), a novel insulin-like growth factor-binding protein-5 proteinase." Overgaard M.T., Boldt H.B., Laursen L.S., Sottrup-Jensen L., Conover C.A., Oxvig C. J. Biol. Chem. 276:21849-21853(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 234-241, TISSUE SPECIFICITY, MUTAGENESIS OF GLU-734, FUNCTION. Tissue: Term placenta.
[2]	"The characterization of pregnancy associated plasma protein-E and the identification of an alternative splice variant." Page N.M., Butlin D.J., Lomthaisong K., Lowry P.J. Placenta 22:681-687(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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).
[6]	"Pregnancy-associated plasma protein-E (PAPP-E)." Farr M., Struebe J., Geppert H.-G., Kocourek A., Mahne M., Tschesche H. Biochim. Biophys. Acta 1493:356-362(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-1791 (ISOFORM 1). Tissue: Placenta.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF311940 mRNA. Translation: AAK31073.1. AF342989 mRNA. Translation: AAL17779.1. Different initiation. AF342990 mRNA. Translation: AAL17780.1. Different initiation. AL031290 , AL031734, AL139282, AL596254 Genomic DNA. Translation: CAI22721.1. AL031734 , AL031290, AL139282, AL596254 Genomic DNA. Translation: CAI22172.1. AL031734, AL596254 Genomic DNA. Translation: CAI22173.1. AL139282 , AL031290, AL031734, AL596254 Genomic DNA. Translation: CAI19567.1. AL596254 , AL031290, AL031734, AL139282 Genomic DNA. Translation: CAH71731.1. AL596254, AL031734 Genomic DNA. Translation: CAH71732.1. CH471067 Genomic DNA. Translation: EAW91003.1. BC117193 mRNA. Translation: AAI17194.3. BC117195 mRNA. Translation: AAI17196.3. AJ278348 mRNA. Translation: CAC11134.1. Different initiation.
IPI	IPI00013569. IPI00171951.
RefSeq	NP_064714.2. NM_020318.2. NP_068755.2. NM_021936.2.
UniGene	Hs.187284.
3D structure databases
ProteinModelPortal	Q9BXP8.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1181124.
STRING	9606.ENSP00000356634.
Protein family/group databases
MEROPS	M43.005.
PTM databases
PhosphoSite	Q9BXP8.
Polymorphism databases
DMDM	126302580.
Proteomic databases
PaxDb	Q9BXP8.
PRIDE	Q9BXP8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000367661; ENSP00000356633; ENSG00000116183. ENST00000367662; ENSP00000356634; ENSG00000116183.
GeneID	60676.
KEGG	hsa:60676.
UCSC	uc001gky.1. human. uc001gkz.3. human.
Organism-specific databases
CTD	60676.
GeneCards	GC01P176432.
HGNC	HGNC:14615. PAPPA2.
HPA	HPA018412. HPA018430.
neXtProt	NX_Q9BXP8.
PharmGKB	PA33373.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG128309.
HOGENOM	HOG000033711.
HOVERGEN	HBG053501.
InParanoid	Q9BXP8.
KO	K08647.
OMA	HIHGAPY.
OrthoDB	EOG4255RW.
PhylomeDB	Q9BXP8.
Enzyme and pathway databases
Reactome	REACT_116125. Disease.
Gene expression databases
Bgee	Q9BXP8.
CleanEx	HS_PAPPA2.
Genevestigator	Q9BXP8.
GermOnline	ENSG00000116183. Homo sapiens.
Family and domain databases
Gene3D	2.60.120.200. 1 hit.
InterPro	IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. IPR003961. Fibronectin_type3. IPR011936. Myxo_disulph_rpt. IPR000800. Notch_dom. IPR026918. PAPPA2. IPR008754. Peptidase_M43. IPR000436. Sushi_SCR_CCP. [Graphical view]
PANTHER	PTHR19325:SF1. PTHR19325:SF1. 1 hit.
Pfam	PF00066. Notch. 2 hits. PF05572. Peptidase_M43. 1 hit. PF00084. Sushi. 1 hit. [Graphical view]
SMART	SM00032. CCP. 4 hits. SM00060. FN3. 1 hit. SM00004. NL. 2 hits. [Graphical view]
SUPFAM	SSF57535. Complement_control_module. 3 hits. SSF49899. ConA_like_lec_gl. 1 hit. SSF49265. FN_III-like. 1 hit.
TIGRFAMs	TIGR02232. myxo_disulf_rpt. 1 hit.
PROSITE	PS50923. SUSHI. 3 hits. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PAPPA2. human.
GenomeRNAi	60676.
NextBio	65486.

Entry information

Entry name

PAPP2_HUMAN

Accession

Primary (citable) accession number: Q9BXP8
Secondary accession number(s): A9Z1Y8 , Q96PH7, Q96PH8, Q9H4C9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	February 20, 2007
Last modified:	May 29, 2013
This is version 107 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.