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Protein

Pappalysin-1

Gene

PAPPA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi562Zinc; catalyticPROSITE-ProRule annotation1
Active sitei563PROSITE-ProRule annotation1
Metal bindingi566Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi572Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

  • metalloendopeptidase activity Source: Reactome
  • metallopeptidase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000119398-MONOMER.
ZFISH:ENSG00000119398-MONOMER.
ZFISH:G66-33940-MONOMER.
BRENDAi3.4.24.79. 2681.
ReactomeiR-HSA-381426. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:8602. PAPPA.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
  • extracellular space Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi5069.
OpenTargetsiENSG00000182752.
PharmGKBiPA32935.

Polymorphism and mutation databases

BioMutaiPAPPA.
DMDMi223590248.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
PropeptideiPRO_000002924523 – 802 PublicationsAdd BLAST58
ChainiPRO_000002924681 – 1627Pappalysin-1Add BLAST1547

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi144 ↔ 235PROSITE-ProRule annotation1 Publication
Disulfide bondi327 ↔ 622PROSITE-ProRule annotation1 Publication
Disulfide bondi332 ↔ 657PROSITE-ProRule annotation1 Publication
Glycosylationi390N-linked (GlcNAc...)Sequence analysis1
Glycosylationi402N-linked (GlcNAc...)1 Publication1
Disulfide bondi414 ↔ 428PROSITE-ProRule annotation1 Publication
Disulfide bondi424 ↔ 440PROSITE-ProRule annotation1 Publication
Glycosylationi429N-linked (GlcNAc...)1 Publication1
Disulfide bondi457 ↔ 473PROSITE-ProRule annotation1 Publication
Disulfide bondi461Interchain (with C-51 in PRG2 proform)PROSITE-ProRule annotation1 Publication
Disulfide bondi474 ↔ 485PROSITE-ProRule annotation1 Publication
Glycosylationi480N-linked (GlcNAc...)1 Publication1
Disulfide bondi583 ↔ 600Or C-583 with C-612PROSITE-ProRule annotation1 Publication
Disulfide bondi587 ↔ 612Or C-587 with C-600PROSITE-ProRule annotation1 Publication
Glycosylationi601N-linked (GlcNAc...)1 Publication1
Glycosylationi619N-linked (GlcNAc...)1 Publication1
Disulfide bondi710 ↔ 878PROSITE-ProRule annotation1 Publication
Disulfide bondi713 ↔ 881PROSITE-ProRule annotation1 Publication
Glycosylationi725N-linked (GlcNAc...)1 Publication1
Disulfide bondi732Interchain (with C-169 in PRG2 proform)PROSITE-ProRule annotation1 Publication
Disulfide bondi753 ↔ 835PROSITE-ProRule annotation1 Publication
Disulfide bondi775 ↔ 781PROSITE-ProRule annotation1 Publication
Glycosylationi825N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi947 ↔ 975PROSITE-ProRule annotation1 Publication
Disulfide bondi960 ↔ 971PROSITE-ProRule annotation1 Publication
Disulfide bondi983 ↔ 990PROSITE-ProRule annotation1 Publication
Disulfide bondi999 ↔ 1011PROSITE-ProRule annotation1 Publication
Glycosylationi1026N-linked (GlcNAc...)1 Publication1
Disulfide bondi1036 ↔ 1070PROSITE-ProRule annotation1 Publication
Disulfide bondi1051 ↔ 1139PROSITE-ProRule annotation1 Publication
Disulfide bondi1192 ↔ 1205PROSITE-ProRule annotation1 Publication
Disulfide bondi1210InterchainPROSITE-ProRule annotation1 Publication
Disulfide bondi1215 ↔ 1269PROSITE-ProRule annotation1 Publication
Glycosylationi1222N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1226N-linked (GlcNAc...)1 Publication1
Disulfide bondi1227 ↔ 1238PROSITE-ProRule annotation1 Publication
Disulfide bondi1242 ↔ 1280PROSITE-ProRule annotation1 Publication
Disulfide bondi1285 ↔ 1329PROSITE-ProRule annotation1 Publication
Disulfide bondi1300 ↔ 1310PROSITE-ProRule annotation1 Publication
Disulfide bondi1314 ↔ 1342PROSITE-ProRule annotation1 Publication
Glycosylationi1323N-linked (GlcNAc...)1 Publication1
Disulfide bondi1346 ↔ 1399PROSITE-ProRule annotation1 Publication
Disulfide bondi1362 ↔ 1373PROSITE-ProRule annotation1 Publication
Disulfide bondi1377 ↔ 1410PROSITE-ProRule annotation1 Publication
Disulfide bondi1415 ↔ 1458PROSITE-ProRule annotation1 Publication
Disulfide bondi1428 ↔ 1438PROSITE-ProRule annotation1 Publication
Disulfide bondi1442 ↔ 1471PROSITE-ProRule annotation1 Publication
Glycosylationi1465N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1478 ↔ 1539PROSITE-ProRule annotation1 Publication
Disulfide bondi1492 ↔ 1502PROSITE-ProRule annotation1 Publication
Disulfide bondi1506 ↔ 1554PROSITE-ProRule annotation1 Publication
Glycosylationi1519N-linked (GlcNAc...)1 Publication1
Disulfide bondi1558 ↔ 1576PROSITE-ProRule annotation1 Publication

Post-translational modificationi

There appear to be no free sulfhydryl groups.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ13219.
PeptideAtlasiQ13219.
PRIDEiQ13219.

PTM databases

iPTMnetiQ13219.
PhosphoSitePlusiQ13219.

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

BgeeiENSG00000182752.
CleanExiHS_PAPPA.
GenevisibleiQ13219. HS.

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. 10 interactors.
IntActiQ13219. 7 interactors.
MINTiMINT-1193478.
STRINGi9606.ENSP00000330658.

Structurei

3D structure databases

ProteinModelPortaliQ13219.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1213 – 1282Sushi 1PROSITE-ProRule annotationAdd BLAST70
Domaini1283 – 1344Sushi 2PROSITE-ProRule annotationAdd BLAST62
Domaini1345 – 1412Sushi 3PROSITE-ProRule annotationAdd BLAST68
Domaini1413 – 1473Sushi 4PROSITE-ProRule annotationAdd BLAST61
Domaini1476 – 1556Sushi 5PROSITE-ProRule annotationAdd BLAST81

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni272 – 583MetalloproteaseAdd BLAST312

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi24 – 84Arg-richAdd BLAST61

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

eggNOGiENOG410KDUG. Eukaryota.
ENOG410YRGU. LUCA.
GeneTreeiENSGT00390000009007.
HOGENOMiHOG000067833.
HOVERGENiHBG053501.
InParanoidiQ13219.
KOiK07762.
OMAiGIQIYTL.
OrthoDBiEOG091G026Y.
PhylomeDBiQ13219.
TreeFamiTF331636.

Family and domain databases

CDDicd00033. CCP. 4 hits.
cd04275. ZnMc_pappalysin_like. 1 hit.
Gene3Di2.60.120.200. 1 hit.
3.40.390.10. 4 hits.
InterProiIPR013320. ConA-like_dom.
IPR006558. LamG-like.
IPR024079. MetalloPept_cat_dom.
IPR011936. Myxo_disulph_rpt.
IPR000800. Notch_dom.
IPR030433. PAPPA.
IPR008754. Peptidase_M43.
IPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PANTHERiPTHR19325:SF347. PTHR19325:SF347. 3 hits.
PfamiPF05572. 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 differs from that shown. Reason: Frameshift at positions 51 and 67.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti107R → RV in AAC50543 (PubMed:8620868).Curated1
Sequence conflicti107R → RV in CAA48341 (PubMed:7508748).Curated1
Sequence conflicti511 – 512TH → RD AA sequence (PubMed:7508748).Curated2
Sequence conflicti1622R → Q in AAH78657 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0570915S → I.Corresponds to variant rs417012dbSNPEnsembl.1
Natural variantiVAR_057092325P → L.Corresponds to variant rs445159dbSNPEnsembl.1
Natural variantiVAR_011419944S → R.2 PublicationsCorresponds to variant rs117124330dbSNPEnsembl.1
Natural variantiVAR_0187261224S → Y.2 PublicationsCorresponds to variant rs7020782dbSNPEnsembl.1

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_002581.4.
UniGeneiHs.643599.

Genome annotation databases

EnsembliENST00000328252; ENSP00000330658; ENSG00000182752.
GeneIDi5069.
KEGGihsa:5069.
UCSCiuc004bjn.4. human.

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.
CCDSiCCDS6813.1.
PIRiS65464.
RefSeqiNP_002572.2. NM_002581.4.
UniGeneiHs.643599.

3D structure databases

ProteinModelPortaliQ13219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111104. 10 interactors.
IntActiQ13219. 7 interactors.
MINTiMINT-1193478.
STRINGi9606.ENSP00000330658.

Protein family/group databases

MEROPSiM43.004.

PTM databases

iPTMnetiQ13219.
PhosphoSitePlusiQ13219.

Polymorphism and mutation databases

BioMutaiPAPPA.
DMDMi223590248.

Proteomic databases

PaxDbiQ13219.
PeptideAtlasiQ13219.
PRIDEiQ13219.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000328252; ENSP00000330658; ENSG00000182752.
GeneIDi5069.
KEGGihsa:5069.
UCSCiuc004bjn.4. human.

Organism-specific databases

CTDi5069.
DisGeNETi5069.
GeneCardsiPAPPA.
H-InvDBHIX0025885.
HGNCiHGNC:8602. PAPPA.
HPAiCAB016724.
HPA001667.
MIMi176385. gene.
neXtProtiNX_Q13219.
OpenTargetsiENSG00000182752.
PharmGKBiPA32935.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410KDUG. Eukaryota.
ENOG410YRGU. LUCA.
GeneTreeiENSGT00390000009007.
HOGENOMiHOG000067833.
HOVERGENiHBG053501.
InParanoidiQ13219.
KOiK07762.
OMAiGIQIYTL.
OrthoDBiEOG091G026Y.
PhylomeDBiQ13219.
TreeFamiTF331636.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000119398-MONOMER.
ZFISH:ENSG00000119398-MONOMER.
ZFISH:G66-33940-MONOMER.
BRENDAi3.4.24.79. 2681.
ReactomeiR-HSA-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Miscellaneous databases

ChiTaRSiPAPPA. human.
GeneWikiiPregnancy-associated_plasma_protein_A.
GenomeRNAii5069.
PMAP-CutDBQ13219.
PROiQ13219.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000182752.
CleanExiHS_PAPPA.
GenevisibleiQ13219. HS.

Family and domain databases

CDDicd00033. CCP. 4 hits.
cd04275. ZnMc_pappalysin_like. 1 hit.
Gene3Di2.60.120.200. 1 hit.
3.40.390.10. 4 hits.
InterProiIPR013320. ConA-like_dom.
IPR006558. LamG-like.
IPR024079. MetalloPept_cat_dom.
IPR011936. Myxo_disulph_rpt.
IPR000800. Notch_dom.
IPR030433. PAPPA.
IPR008754. Peptidase_M43.
IPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PANTHERiPTHR19325:SF347. PTHR19325:SF347. 3 hits.
PfamiPF05572. 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]
ProtoNetiSearch...

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 30, 2016
This is version 179 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

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 one 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.