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Protein

Prolyl endopeptidase FAP

Gene

FAP

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

Functioni

Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2 (PubMed:14751930, PubMed:16223769, PubMed:16480718, PubMed:16410248, PubMed:17381073, PubMed:18095711, PubMed:21288888, PubMed:24371721). Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenascin, laminin, fibronectin, fibrin or casein (PubMed:9065413, PubMed:2172980, PubMed:7923219, PubMed:10347120, PubMed:10455171, PubMed:12376466, PubMed:16223769, PubMed:16651416, PubMed:18095711). Have also dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro (PubMed:10347120, PubMed:10593948, PubMed:16175601, PubMed:16223769, PubMed:16651416, PubMed:16410248, PubMed:17381073, PubMed:21314817, PubMed:24371721, PubMed:24717288). Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB) (PubMed:21314817). The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner.By similarity21 Publications

Catalytic activityi

Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.7 Publications
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.PROSITE-ProRule annotation10 Publications

Enzyme regulationi

Gelatinase activity is inhibited by serine-protease inhibitors, such as phenylmethylsulfonyl fluoride (PMSF), 4-(2-aminoethyl)-benzenesulfonyl fluoride hydrochloride (AEBSF), 4-amidino phenylsulfonyl fluoride (APSF) and diisopropyl fluorophosphate (DFP), N-ethylmaleimide (NEM) and phenylmethylsulfonyl fluoride (PMSF). Dipeptidyl peptidase activity is inhibited by 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), diisopropylfluorophosphate (DFP). Prolyl endopeptidase activity is inhibited by the boronic acid peptide Ac-Gly-BoroPro, Ac-Gly-Pro-chloromethyl ketone and Thr-Ser-Gly-chloromethyl ketone.6 Publications

Kineticsi

  1. KM=0.46 mM for Ala-Pro (Dipeptidyl peptidase activity)1 Publication
  2. KM=0.9 mM for Lys-Pro (Dipeptidyl peptidase activity)1 Publication
  3. KM=1.15 mM for Gly-Pro (Dipeptidyl peptidase activity)1 Publication
  4. KM=0.25 mM for Gly-Pro (Dipeptidyl peptidase activity)1 Publication
  5. KM=0.24 mM for Ala-Pro (Dipeptidyl peptidase activity)1 Publication
  6. KM=0.10 mM for Ile-Pro (Dipeptidyl peptidase activity)1 Publication
  7. KM=0.24 mM for Phe-Pro (Dipeptidyl peptidase activity)1 Publication
  8. KM=0.24 mM for Gly-Pro (Dipeptidyl peptidase activity)1 Publication
  9. KM=0.33 mM for Ac-Gly-Pro (Prolyl endopeptidase activity)2 Publications
  10. KM=1.3 µM for Thr-Ser-Gly-Pro-Asn-Gln (Prolyl endopeptidase activity)1 Publication
  11. KM=2.2 µM for Ala-Ser-Gly-Pro-Asn-Gln (Prolyl endopeptidase activity)1 Publication
  12. KM=0.7 µM for Thr-Ala-Gly-Pro-Asn-Gln (Prolyl endopeptidase activity)1 Publication
  13. KM=1.9 µM for Thr-Ser-Gly-Pro-Ser-Gln (Prolyl endopeptidase activity)1 Publication
  14. KM=2.2 µM for Thr-Ser-Gly-Pro-Asn-Ser (Prolyl endopeptidase activity)1 Publication
  15. KM=4.3 µM for Ala-Ser-Gly-Pro-Ser-Ser (Prolyl endopeptidase activity)1 Publication
  16. KM=0.101 mM for Gly-Pro (FAP form, prolyl endopeptidase activity)1 Publication
  17. KM=0.124 mM for Gly-Pro (Antiplasmin-cleaving enzyme FAP soluble form, prolyl endopeptidase activity)1 Publication
  18. KM=0.323 mM for Gly-Pro (FAP form, dipeptidyl peptidase activity)1 Publication
  19. KM=0.272 mM for Gly-Pro (Antiplasmin-cleaving enzyme FAP soluble form, dipeptidyl peptidase activity)1 Publication
  20. KM=0.029 mM for Arg-Gly-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu (FAP form, prolyl endopeptidase activity)1 Publication
  21. KM=0.026 mM for Arg-Gly-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu (Antiplasmin-cleaving enzyme FAP soluble form, prolyl endopeptidase activity)1 Publication

    pH dependencei

    Optimum pH is 6-8.4 for gelatinase activity. At pH lower than 5 inhibited gelatinase activity.2 Publications

    Temperature dependencei

    Optimum temperature is 37 degrees Celsius for gelatinase activity. Temperatures above 50 degrees Celsius inhibit gelatinase activity.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei23 – 242Cleavage1 Publication
    Binding sitei203 – 2031Substrate1 Publication
    Binding sitei204 – 2041Substrate1 Publication
    Active sitei624 – 6241Charge relay systemPROSITE-ProRule annotation1 Publication
    Active sitei702 – 7021Charge relay system1 Publication
    Active sitei734 – 7341Charge relay system1 Publication

    GO - Molecular functioni

    • dipeptidyl-peptidase activity Source: UniProtKB
    • endopeptidase activity Source: BHF-UCL
    • integrin binding Source: UniProtKB
    • metalloendopeptidase activity Source: UniProtKB
    • peptidase activity Source: UniProtKB
    • protease binding Source: BHF-UCL
    • protein dimerization activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    • serine-type endopeptidase activity Source: UniProtKB
    • serine-type peptidase activity Source: UniProtKB

    GO - Biological processi

    • angiogenesis Source: UniProtKB-KW
    • cell adhesion Source: UniProtKB-KW
    • endothelial cell migration Source: UniProtKB
    • melanocyte apoptotic process Source: UniProtKB
    • melanocyte proliferation Source: UniProtKB
    • mitotic cell cycle arrest Source: UniProtKB
    • negative regulation of cell proliferation involved in contact inhibition Source: UniProtKB
    • negative regulation of extracellular matrix disassembly Source: UniProtKB
    • negative regulation of extracellular matrix organization Source: UniProtKB
    • positive regulation of cell cycle arrest Source: UniProtKB
    • positive regulation of execution phase of apoptosis Source: UniProtKB
    • proteolysis Source: UniProtKB
    • proteolysis involved in cellular protein catabolic process Source: UniProtKB
    • regulation of collagen catabolic process Source: UniProtKB
    • regulation of fibrinolysis Source: BHF-UCL
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Angiogenesis, Apoptosis, Cell adhesion

    Enzyme and pathway databases

    BRENDAi3.4.21.B28. 2681.

    Protein family/group databases

    MEROPSiS09.007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prolyl endopeptidase FAPCurated (EC:3.4.21.261 Publication)
    Alternative name(s):
    170 kDa melanoma membrane-bound gelatinase2 Publications
    Dipeptidyl peptidase FAPCurated (EC:3.4.14.51 Publication)
    Fibroblast activation protein alpha1 Publication
    Short name:
    FAPalphaBy similarity
    Gelatine degradation protease FAPCurated (EC:3.4.21.-1 Publication)
    Integral membrane serine protease1 Publication
    Post-proline cleaving enzymeCurated
    Serine integral membrane protease1 Publication
    Short name:
    SIMP1 Publication
    Surface-expressed protease1 Publication
    Short name:
    Seprase1 Publication
    Cleaved into the following chain:
    Antiplasmin-cleaving enzyme FAP, soluble form1 Publication (EC:3.4.14.52 Publications, EC:3.4.21.-2 Publications, EC:3.4.21.262 Publications)
    Short name:
    APCE1 Publication
    Gene namesi
    Name:FAPImported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:3590. FAP.

    Subcellular locationi

    Chain Prolyl endopeptidase FAP :
    Chain Antiplasmin-cleaving enzyme FAP, soluble form :
    Isoform 2 :
    • Cytoplasm 1 Publication

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 44Cytoplasmic1 PublicationSequence Analysis
    Transmembranei5 – 2521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST
    Topological domaini26 – 760735Extracellular1 PublicationSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    • apical part of cell Source: Ensembl
    • basal part of cell Source: Ensembl
    • cell surface Source: UniProtKB
    • cytoplasm Source: UniProtKB-SubCell
    • extracellular space Source: BHF-UCL
    • focal adhesion Source: UniProtKB
    • integral component of membrane Source: UniProtKB
    • invadopodium membrane Source: UniProtKB
    • lamellipodium Source: UniProtKB
    • lamellipodium membrane Source: UniProtKB-SubCell
    • plasma membrane Source: UniProtKB
    • ruffle membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi123 – 1231R → A, M or E: Reduces dipeptidyl peptidase and endopeptidase activities. 1 Publication
    Mutagenesisi203 – 2031E → A, D or Q: Reduces dipeptidyl peptidase and endopeptidase activities. Does not inhibit cell adhesion, migration and invasion. Inhibits dipeptidyl peptidase and endopeptidase activities; when associated with A-204. 2 Publications
    Mutagenesisi204 – 2041E → A, D or Q: Reduces dipeptidyl peptidase and endopeptidase activities. Does not inhibit cell adhesion, migration and invasion. Inhibits dipeptidyl peptidase and endopeptidase activities; when associated with A-203. 2 Publications
    Mutagenesisi624 – 6241S → A: Reduces dipeptidyl peptidase and gelatinolytic activities. Does not inhibit cell adhesion, migration and invasion. 2 Publications
    Mutagenesisi656 – 6561Y → F: Reduces dipeptidyl peptidase and endopeptidase activities. 1 Publication
    Mutagenesisi657 – 6571A → D or N: Inhibits endopeptidase activity. Increases dipeptidyl peptidase activity. 1 Publication
    Mutagenesisi657 – 6571A → F or V: Reduces dipeptidyl peptidase and endopeptidase activities. 1 Publication
    Mutagenesisi657 – 6571A → Q: Inhibits endopeptidase activity. No change in dipeptidyl peptidase activity. 1 Publication
    Mutagenesisi657 – 6571A → S or T: Reduces strongly endopeptidase activity. No change in dipeptidyl peptidase activity. 1 Publication
    Mutagenesisi704 – 7041N → A: Reduces dipeptidyl peptidase and endopeptidase activities. 1 Publication

    Organism-specific databases

    PharmGKBiPA28003.

    Polymorphism and mutation databases

    BioMutaiFAP.
    DMDMi292495099.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 760760Prolyl endopeptidase FAPCuratedPRO_0000122424Add
    BLAST
    Chaini24 – 760737Antiplasmin-cleaving enzyme FAP, soluble form1 PublicationPRO_0000430643Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi49 – 491N-linked (GlcNAc...)PROSITE-ProRule annotation1 Publication
    Glycosylationi92 – 921N-linked (GlcNAc...)PROSITE-ProRule annotation1 Publication
    Glycosylationi99 – 991N-linked (GlcNAc...)PROSITE-ProRule annotation1 Publication
    Glycosylationi227 – 2271N-linked (GlcNAc...)PROSITE-ProRule annotation2 Publications
    Glycosylationi314 – 3141N-linked (GlcNAc...)PROSITE-ProRule annotation1 Publication
    Disulfide bondi321 ↔ 3321 Publication
    Disulfide bondi438 ↔ 4411 Publication
    Disulfide bondi448 ↔ 4661 Publication
    Disulfide bondi643 ↔ 7551 Publication
    Glycosylationi679 – 6791N-linked (GlcNAc...)PROSITE-ProRule annotation

    Post-translational modificationi

    N-glycosylated.4 Publications
    The N-terminus may be blocked.

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ12884.
    PRIDEiQ12884.

    PTM databases

    PhosphoSiteiQ12884.

    Expressioni

    Tissue specificityi

    Expressed in adipose tissue. Expressed in the dermal fibroblasts in the fetal skin. Expressed in the granulation tissue of healing wounds and on reactive stromal fibroblast in epithelial cancers. Expressed in activated fibroblast-like synoviocytes from inflamed synovial tissues. Expressed in activated hepatic stellate cells (HSC) and myofibroblasts from cirrhotic liver, but not detected in normal liver. Expressed in glioma cells (at protein level). Expressed in glioblastomas and glioma cells. Isoform 1 and isoform 2 are expressed in melanoma, carcinoma and fibroblast cell lines.8 Publications

    Inductioni

    In fibroblasts at times and sites of tissue remodeling during development, tissue repair and carcinogenesis. Up-regulated upon tumor stem cell differentiation. Up-regulated by transforming growth factor-beta, 12-O-tetradecanoyl phorbol-13-acetate and retinoids.2 Publications

    Gene expression databases

    BgeeiQ12884.
    CleanExiHS_FAP.
    ExpressionAtlasiQ12884. baseline and differential.
    GenevestigatoriQ12884.

    Organism-specific databases

    HPAiHPA059739.

    Interactioni

    Subunit structurei

    Homodimer; homodimerization is required for activity of both plasma membrane and soluble forms. The monomer is inactive. Heterodimer with DPP4. Interacts with PLAUR; the interaction occurs at the cell surface of invadopodia membranes. Interacts with ITGB1. Interacts with ITGA3. Associates with integrin alpha-3/beta-1; the association occurs in a collagen-dependent manner at the cell surface of invadopodia membranes.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GCGP012754EBI-4319803,EBI-7629173
    VIPP012822EBI-4319803,EBI-751454

    Protein-protein interaction databases

    BioGridi108485. 4 interactions.
    IntActiQ12884. 10 interactions.
    MINTiMINT-4778828.
    STRINGi9606.ENSP00000188790.

    Structurei

    Secondary structure

    1
    760
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi44 – 496Combined sources
    Turni50 – 523Combined sources
    Beta strandi60 – 7011Combined sources
    Beta strandi76 – 838Combined sources
    Beta strandi86 – 905Combined sources
    Helixi92 – 965Combined sources
    Turni97 – 993Combined sources
    Beta strandi101 – 1055Combined sources
    Beta strandi109 – 12012Combined sources
    Beta strandi122 – 1243Combined sources
    Beta strandi126 – 1349Combined sources
    Turni135 – 1384Combined sources
    Beta strandi148 – 1503Combined sources
    Beta strandi153 – 1553Combined sources
    Beta strandi162 – 1665Combined sources
    Beta strandi169 – 1757Combined sources
    Turni189 – 1913Combined sources
    Beta strandi192 – 1965Combined sources
    Helixi199 – 2046Combined sources
    Beta strandi212 – 2143Combined sources
    Beta strandi218 – 22710Combined sources
    Beta strandi233 – 2386Combined sources
    Beta strandi241 – 2444Combined sources
    Beta strandi246 – 2516Combined sources
    Beta strandi261 – 27010Combined sources
    Helixi272 – 2754Combined sources
    Helixi284 – 2874Combined sources
    Beta strandi291 – 31222Combined sources
    Beta strandi315 – 3239Combined sources
    Beta strandi325 – 3317Combined sources
    Helixi334 – 3363Combined sources
    Beta strandi337 – 3415Combined sources
    Beta strandi343 – 3453Combined sources
    Beta strandi347 – 3515Combined sources
    Beta strandi364 – 3696Combined sources
    Beta strandi375 – 3828Combined sources
    Beta strandi393 – 3953Combined sources
    Beta strandi397 – 4037Combined sources
    Beta strandi405 – 4139Combined sources
    Helixi415 – 4173Combined sources
    Beta strandi422 – 4287Combined sources
    Beta strandi430 – 4334Combined sources
    Beta strandi436 – 4405Combined sources
    Turni441 – 4477Combined sources
    Beta strandi450 – 4556Combined sources
    Helixi457 – 4593Combined sources
    Beta strandi460 – 4667Combined sources
    Beta strandi469 – 4713Combined sources
    Beta strandi473 – 4775Combined sources
    Beta strandi479 – 4813Combined sources
    Beta strandi484 – 4896Combined sources
    Helixi492 – 4976Combined sources
    Beta strandi505 – 5139Combined sources
    Beta strandi516 – 5249Combined sources
    Beta strandi530 – 5323Combined sources
    Beta strandi534 – 5407Combined sources
    Helixi557 – 5637Combined sources
    Beta strandi568 – 5736Combined sources
    Beta strandi577 – 5804Combined sources
    Helixi582 – 5854Combined sources
    Helixi586 – 5883Combined sources
    Helixi594 – 60815Combined sources
    Beta strandi613 – 62311Combined sources
    Helixi625 – 63410Combined sources
    Beta strandi637 – 6393Combined sources
    Beta strandi642 – 6487Combined sources
    Turni653 – 6553Combined sources
    Helixi658 – 6658Combined sources
    Turni670 – 6734Combined sources
    Helixi674 – 6796Combined sources
    Helixi683 – 6897Combined sources
    Beta strandi692 – 6998Combined sources
    Beta strandi703 – 7053Combined sources
    Helixi708 – 71912Combined sources
    Beta strandi725 – 7295Combined sources
    Helixi739 – 75618Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z68X-ray2.60A/B39-757[»]
    ProteinModelPortaliQ12884.
    SMRiQ12884. Positions 39-757.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12884.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9B family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1506.
    GeneTreeiENSGT00760000119233.
    HOGENOMiHOG000231875.
    HOVERGENiHBG005527.
    InParanoidiQ12884.
    KOiK08674.
    OMAiLSTKHLY.
    OrthoDBiEOG761BT2.
    PhylomeDBiQ12884.
    TreeFamiTF313309.

    Family and domain databases

    Gene3Di2.140.10.30. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR001375. Peptidase_S9.
    IPR002469. Peptidase_S9B.
    [Graphical view]
    PfamiPF00930. DPPIV_N. 1 hit.
    PF00326. Peptidase_S9. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q12884-1) [UniParc]FASTAAdd to basket

    Also known as: L, seprase-I1 Publication

    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.

    « Hide

            10         20         30         40         50
    MKTWVKIVFG VATSAVLALL VMCIVLRPSR VHNSEENTMR ALTLKDILNG
    60 70 80 90 100
    TFSYKTFFPN WISGQEYLHQ SADNNIVLYN IETGQSYTIL SNRTMKSVNA
    110 120 130 140 150
    SNYGLSPDRQ FVYLESDYSK LWRYSYTATY YIYDLSNGEF VRGNELPRPI
    160 170 180 190 200
    QYLCWSPVGS KLAYVYQNNI YLKQRPGDPP FQITFNGREN KIFNGIPDWV
    210 220 230 240 250
    YEEEMLATKY ALWWSPNGKF LAYAEFNDTD IPVIAYSYYG DEQYPRTINI
    260 270 280 290 300
    PYPKAGAKNP VVRIFIIDTT YPAYVGPQEV PVPAMIASSD YYFSWLTWVT
    310 320 330 340 350
    DERVCLQWLK RVQNVSVLSI CDFREDWQTW DCPKTQEHIE ESRTGWAGGF
    360 370 380 390 400
    FVSTPVFSYD AISYYKIFSD KDGYKHIHYI KDTVENAIQI TSGKWEAINI
    410 420 430 440 450
    FRVTQDSLFY SSNEFEEYPG RRNIYRISIG SYPPSKKCVT CHLRKERCQY
    460 470 480 490 500
    YTASFSDYAK YYALVCYGPG IPISTLHDGR TDQEIKILEE NKELENALKN
    510 520 530 540 550
    IQLPKEEIKK LEVDEITLWY KMILPPQFDR SKKYPLLIQV YGGPCSQSVR
    560 570 580 590 600
    SVFAVNWISY LASKEGMVIA LVDGRGTAFQ GDKLLYAVYR KLGVYEVEDQ
    610 620 630 640 650
    ITAVRKFIEM GFIDEKRIAI WGWSYGGYVS SLALASGTGL FKCGIAVAPV
    660 670 680 690 700
    SSWEYYASVY TERFMGLPTK DDNLEHYKNS TVMARAEYFR NVDYLLIHGT
    710 720 730 740 750
    ADDNVHFQNS AQIAKALVNA QVDFQAMWYS DQNHGLSGLS TNHLYTHMTH
    760
    FLKQCFSLSD

    Note: Major isoform.

    Length:760
    Mass (Da):87,713
    Last modified:March 23, 2010 - v5
    Checksum:i7FF817B5A4F75142
    GO
    Isoform 21 Publication (identifier: Q12884-2) [UniParc]FASTAAdd to basket

    Also known as: S, Truncated, seprase-s1 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         1-521: Missing.

    Note: Upstream open reading frames ORF(s)-containing region inhibits the translation of its downstream ORF.1 Publication

    Show »
    Length:239
    Mass (Da):26,954
    Checksum:i853731E1DF446AC6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti207 – 2071A → P in AAB49652 (PubMed:7911242).Curated
    Sequence conflicti229 – 2291T → K in AAB49652 (PubMed:7911242).Curated
    Sequence conflicti354 – 3541T → R in AAB49652 (PubMed:7911242).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti363 – 3631S → L Decreased plasma membrane expression; loss of homodimerization and dipeptidyl peptidase activity; mislocalized with the calnexin in the endoplasmic reticulum; causes induction of the unfolded protein response (UPR). 2 Publications
    VAR_071264

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 521521Missing in isoform 2. 1 PublicationVSP_005367Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U09278 mRNA. Translation: AAB49652.1.
    U76833 mRNA. Translation: AAC51668.1.
    AF007822 mRNA. Translation: AAF21600.1.
    AC007750 Genomic DNA. Translation: AAY24205.1.
    CH471058 Genomic DNA. Translation: EAX11353.1.
    BC026250 mRNA. Translation: AAH26250.1.
    CCDSiCCDS33311.1. [Q12884-1]
    RefSeqiNP_001278736.1. NM_001291807.1.
    NP_004451.2. NM_004460.3. [Q12884-1]
    UniGeneiHs.654370.

    Genome annotation databases

    EnsembliENST00000188790; ENSP00000188790; ENSG00000078098. [Q12884-1]
    GeneIDi2191.
    KEGGihsa:2191.
    UCSCiuc002ucd.3. human. [Q12884-1]
    uc010fpc.3. human. [Q12884-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U09278 mRNA. Translation: AAB49652.1.
    U76833 mRNA. Translation: AAC51668.1.
    AF007822 mRNA. Translation: AAF21600.1.
    AC007750 Genomic DNA. Translation: AAY24205.1.
    CH471058 Genomic DNA. Translation: EAX11353.1.
    BC026250 mRNA. Translation: AAH26250.1.
    CCDSiCCDS33311.1. [Q12884-1]
    RefSeqiNP_001278736.1. NM_001291807.1.
    NP_004451.2. NM_004460.3. [Q12884-1]
    UniGeneiHs.654370.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z68X-ray2.60A/B39-757[»]
    ProteinModelPortaliQ12884.
    SMRiQ12884. Positions 39-757.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108485. 4 interactions.
    IntActiQ12884. 10 interactions.
    MINTiMINT-4778828.
    STRINGi9606.ENSP00000188790.

    Chemistry

    BindingDBiQ12884.
    ChEMBLiCHEMBL4683.

    Protein family/group databases

    MEROPSiS09.007.

    PTM databases

    PhosphoSiteiQ12884.

    Polymorphism and mutation databases

    BioMutaiFAP.
    DMDMi292495099.

    Proteomic databases

    PaxDbiQ12884.
    PRIDEiQ12884.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000188790; ENSP00000188790; ENSG00000078098. [Q12884-1]
    GeneIDi2191.
    KEGGihsa:2191.
    UCSCiuc002ucd.3. human. [Q12884-1]
    uc010fpc.3. human. [Q12884-2]

    Organism-specific databases

    CTDi2191.
    GeneCardsiGC02M163027.
    H-InvDBHIX0002548.
    HGNCiHGNC:3590. FAP.
    HPAiHPA059739.
    MIMi600403. gene.
    neXtProtiNX_Q12884.
    PharmGKBiPA28003.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG1506.
    GeneTreeiENSGT00760000119233.
    HOGENOMiHOG000231875.
    HOVERGENiHBG005527.
    InParanoidiQ12884.
    KOiK08674.
    OMAiLSTKHLY.
    OrthoDBiEOG761BT2.
    PhylomeDBiQ12884.
    TreeFamiTF313309.

    Enzyme and pathway databases

    BRENDAi3.4.21.B28. 2681.

    Miscellaneous databases

    ChiTaRSiFAP. human.
    EvolutionaryTraceiQ12884.
    GeneWikiiFibroblast_activation_protein,_alpha.
    GenomeRNAii2191.
    NextBioi8851.
    PROiQ12884.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ12884.
    CleanExiHS_FAP.
    ExpressionAtlasiQ12884. baseline and differential.
    GenevestigatoriQ12884.

    Family and domain databases

    Gene3Di2.140.10.30. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR001375. Peptidase_S9.
    IPR002469. Peptidase_S9B.
    [Graphical view]
    PfamiPF00930. DPPIV_N. 1 hit.
    PF00326. Peptidase_S9. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Molecular cloning of fibroblast activation protein alpha, a member of the serine protease family selectively expressed in stromal fibroblasts of epithelial cancers."
      Scanlan M.J., Raj B.K.M., Calvo B., Garin-Chesa P., Sanz-Moncasi M.P., Healey J.H., Old L.J., Rettig W.J.
      Proc. Natl. Acad. Sci. U.S.A. 91:5657-5661(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Fibroblast.
    2. "Molecular cloning of seprase: a serine integral membrane protease from human melanoma."
      Goldstein L.A., Ghersi G., Pineiro-Sanchez M.L., Salamone M., Yeh Y., Flessate D., Chen W.-T.
      Biochim. Biophys. Acta 1361:11-19(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Melanoma.
    3. "Identification of the 170-kDa melanoma membrane-bound gelatinase (seprase) as a serine integral membrane protease."
      Pineiro-Sanchez M.L., Goldstein L.A., Dodt J., Howard L., Yeh Y., Chen W.-T.
      J. Biol. Chem. 272:7595-7601(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 220-229; 461-472 AND 511-518, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, GLYCOSYLATION, SUBCELLULAR LOCATION.
      Tissue: Melanoma.
    4. "Identification of an alternatively spliced seprase mRNA that encodes a novel intracellular isoform."
      Goldstein L.A., Chen W.-T.
      J. Biol. Chem. 275:2554-2559(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Melanoma.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 1).
      Tissue: Placenta.
    8. "A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion."
      Lee K.N., Jackson K.W., Christiansen V.J., Chung K.H., McKee P.A.
      Blood 103:3783-3788(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 24-38; 210-219; 247-254; 487-499; 500-509 AND 522-530, FUNCTION (SOLUBLE FORM), CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    9. "Fibroblast activation protein: purification, epitope mapping and induction by growth factors."
      Rettig W.J., Su S.L., Fortunato S.R., Scanlan M.J., Raj B.K.M., Garin-Chesa P., Healey J.H., Old L.J.
      Int. J. Cancer 58:385-392(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 192-208; 220-240 AND 510-521, INDUCTION.
    10. "A 170-kDa membrane-bound protease is associated with the expression of invasiveness by human malignant melanoma cells."
      Aoyama A., Chen W.T.
      Proc. Natl. Acad. Sci. U.S.A. 87:8296-8300(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    11. "A potential marker protease of invasiveness, seprase, is localized on invadopodia of human malignant melanoma cells."
      Monsky W.L., Lin C.Y., Aoyama A., Kelly T., Akiyama S.K., Mueller S.C., Chen W.T.
      Cancer Res. 54:5702-5710(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    12. "Fibroblast activation protein: a cell surface dipeptidyl peptidase and gelatinase expressed by stellate cells at the tissue remodelling interface in human cirrhosis."
      Levy M.T., McCaughan G.W., Abbott C.A., Park J.E., Cunningham A.M., Mueller E., Rettig W.J., Gorrell M.D.
      Hepatology 29:1768-1778(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    13. "Fibroblast activation protein, a dual specificity serine protease expressed in reactive human tumor stromal fibroblasts."
      Park J.E., Lenter M.C., Zimmermann R.N., Garin-Chesa P., Old L.J., Rettig W.J.
      J. Biol. Chem. 274:36505-36512(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF SER-624.
    14. Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH ITGA3 AND ITGB1, ASSOCIATION WITH INTEGRIN ALPHA-3/BETA-1, SUBCELLULAR LOCATION.
    15. "Molecular proximity of seprase and the urokinase-type plasminogen activator receptor on malignant melanoma cell membranes: dependence on beta1 integrins and the cytoskeleton."
      Artym V.V., Kindzelskii A.L., Chen W.T., Petty H.R.
      Carcinogenesis 23:1593-1601(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PLAUR, SUBCELLULAR LOCATION.
    16. "Fibroblast activation protein increases apoptosis, cell adhesion, and migration by the LX-2 human stellate cell line."
      Wang X.M., Yu D.M., McCaughan G.W., Gorrell M.D.
      Hepatology 42:935-945(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF GLU-203; GLU-204 AND SER-624.
    17. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-99 AND ASN-227.
      Tissue: Plasma.
    18. "Fibroblast activation protein is expressed by rheumatoid myofibroblast-like synoviocytes."
      Bauer S., Jendro M.C., Wadle A., Kleber S., Stenner F., Dinser R., Reich A., Faccin E., Goedde S., Dinges H., Mueller-Ladner U., Renner C.
      Arthritis Res. Ther. 8:R171-R171(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    19. "Antiplasmin-cleaving enzyme is a soluble form of fibroblast activation protein."
      Lee K.N., Jackson K.W., Christiansen V.J., Lee C.S., Chun J.G., McKee P.A.
      Blood 107:1397-1404(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (PLASMA MEMBRANE AND SOLUBLE FORMS), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.
    20. "The protease complex consisting of dipeptidyl peptidase IV and seprase plays a role in the migration and invasion of human endothelial cells in collagenous matrices."
      Ghersi G., Zhao Q., Salamone M., Yeh Y., Zucker S., Chen W.T.
      Cancer Res. 66:4652-4661(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, HETERODIMERIZATION WITH DPP4, SUBCELLULAR LOCATION.
    21. "Peptide substrate profiling defines fibroblast activation protein as an endopeptidase of strict Gly(2)-Pro(1)-cleaving specificity."
      Edosada C.Y., Quan C., Tran T., Pham V., Wiesmann C., Fairbrother W., Wolf B.B.
      FEBS Lett. 580:1581-1586(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    22. "Selective inhibition of fibroblast activation protein protease based on dipeptide substrate specificity."
      Edosada C.Y., Quan C., Wiesmann C., Tran T., Sutherlin D., Reynolds M., Elliott J.M., Raab H., Fairbrother W., Wolf B.B.
      J. Biol. Chem. 281:7437-7444(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
    23. "Ala657 and conserved active site residues promote fibroblast activation protein endopeptidase activity via distinct mechanisms of transition state stabilization."
      Meadows S.A., Edosada C.Y., Mayeda M., Tran T., Quan C., Raab H., Wiesmann C., Wolf B.B.
      Biochemistry 46:4598-4605(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ARG-123; GLU-203; TYR-656; ALA-657 AND ASN-704, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    24. "Fibroblast activation protein peptide substrates identified from human collagen I derived gelatin cleavage sites."
      Aggarwal S., Brennen W.N., Kole T.P., Schneider E., Topaloglu O., Yates M., Cotter R.J., Denmeade S.R.
      Biochemistry 47:1076-1086(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    25. "Seprase: an overview of an important matrix serine protease."
      O'Brien P., O'Connor B.F.
      Biochim. Biophys. Acta 1784:1130-1145(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW, FUNCTION.
    26. "Expression and role of the cell surface protease seprase/fibroblast activation protein-alpha (FAP-alpha) in astroglial tumors."
      Mentlein R., Hattermann K., Hemion C., Jungbluth A.A., Held-Feindt J.
      Biol. Chem. 392:199-207(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    27. "Neuropeptide Y, B-type natriuretic peptide, substance P and peptide YY are novel substrates of fibroblast activation protein-alpha."
      Keane F.M., Nadvi N.A., Yao T.W., Gorrell M.D.
      FEBS J. 278:1316-1332(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    28. "Cleavage-site specificity of prolyl endopeptidase FAP investigated with a full-length protein substrate."
      Huang C.H., Suen C.S., Lin C.T., Chien C.H., Lee H.Y., Chung K.M., Tsai T.Y., Jiaang W.T., Hwang M.J., Chen X.
      J. Biochem. 149:685-692(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    29. Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT LEU-363.
    30. "A rare variant in human fibroblast activation protein associated with ER stress, loss of enzymatic function and loss of cell surface localisation."
      Osborne B., Yao T.W., Wang X.M., Chen Y., Kotan L.D., Nadvi N.A., Herdem M., McCaughan G.W., Allen J.D., Yu D.M., Topaloglu A.K., Gorrell M.D.
      Biochim. Biophys. Acta 1844:1248-1259(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT LEU-363.
    31. "Structural and kinetic analysis of the substrate specificity of human fibroblast activation protein alpha."
      Aertgeerts K., Levin I., Shi L., Snell G.P., Jennings A., Prasad G.S., Zhang Y., Kraus M.L., Salakian S., Sridhar V., Wijnands R., Tennant M.G.
      J. Biol. Chem. 280:19441-19444(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 39-757, SUBSTRATE BINDING, SUBUNIT, DISULFIDE BONDS, ACTIVE SITE, GLYCOSYLATION AT ASN-49; ASN-92; ASN-227 AND ASN-314.

    Entry informationi

    Entry nameiSEPR_HUMAN
    AccessioniPrimary (citable) accession number: Q12884
    Secondary accession number(s): O00199
    , Q53TP5, Q86Z29, Q99998, Q9UID4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: March 23, 2010
    Last modified: April 29, 2015
    This is version 153 of the entry and version 5 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.