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Q12884

- SEPR_HUMAN

UniProt

Q12884 - SEPR_HUMAN

Protein

Seprase

Gene

FAP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 5 (23 Mar 2010)
      Previous versions | rss
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    Functioni

    In association with DPP4 is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers.1 Publication

    Catalytic activityi

    Degrades gelatin and heat-denatured type I and type IV collagen, but not native type I or type IV collagen. Does not cleave laminin, fibronectin, fibrin or casein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei203 – 2031Substrate
    Binding sitei204 – 2041Substrate
    Active sitei624 – 6241Charge relay system1 PublicationPROSITE-ProRule annotation
    Active sitei702 – 7021Charge relay system1 PublicationPROSITE-ProRule annotation
    Active sitei734 – 7341Charge relay system1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. dipeptidyl-peptidase activity Source: UniProtKB
    2. endopeptidase activity Source: BHF-UCL
    3. metalloendopeptidase activity Source: UniProtKB
    4. peptidase activity Source: MGI
    5. protease binding Source: BHF-UCL
    6. protein binding Source: UniProtKB
    7. protein dimerization activity Source: UniProtKB
    8. protein homodimerization activity Source: UniProtKB
    9. serine-type endopeptidase activity Source: InterPro
    10. serine-type peptidase activity Source: UniProtKB

    GO - Biological processi

    1. endothelial cell migration Source: UniProtKB
    2. negative regulation of extracellular matrix disassembly Source: UniProtKB
    3. regulation of fibrinolysis Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS09.007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Seprase (EC:3.4.21.-)
    Alternative name(s):
    170 kDa melanoma membrane-bound gelatinase
    Fibroblast activation protein alpha
    Integral membrane serine protease
    Gene namesi
    Name:FAP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:3590. FAP.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type II membrane protein 1 Publication. Cell projectionlamellipodium membrane 1 Publication; Single-pass type II membrane protein 1 Publication. Cell projectioninvadopodium membrane 1 Publication; Single-pass type II membrane protein 1 Publication
    Note: Found in cell surface lamellipodia, invadopodia and on shed vesicles. Colocalized with DPP4 in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma.

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. extracellular space Source: BHF-UCL
    3. integral component of membrane Source: UniProtKB
    4. invadopodium membrane Source: UniProtKB-SubCell
    5. lamellipodium Source: UniProtKB
    6. lamellipodium membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28003.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 760760SeprasePRO_0000122424Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi49 – 491N-linked (GlcNAc...)1 Publication
    Glycosylationi92 – 921N-linked (GlcNAc...)1 Publication
    Glycosylationi99 – 991N-linked (GlcNAc...)1 Publication
    Glycosylationi227 – 2271N-linked (GlcNAc...)2 Publications
    Glycosylationi314 – 3141N-linked (GlcNAc...)1 Publication
    Disulfide bondi321 ↔ 3321 Publication
    Disulfide bondi438 ↔ 4411 Publication
    Disulfide bondi448 ↔ 4661 Publication
    Disulfide bondi643 ↔ 7551 Publication
    Glycosylationi679 – 6791N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.2 Publications
    The N-terminus may be blocked.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ12884.
    PRIDEiQ12884.

    PTM databases

    PhosphoSiteiQ12884.

    Expressioni

    Tissue specificityi

    Fibroblast specific.

    Inductioni

    In fibroblasts at times and sites of tissue remodeling during development, tissue repair, and carcinogenesis.

    Gene expression databases

    ArrayExpressiQ12884.
    BgeeiQ12884.
    CleanExiHS_FAP.
    GenevestigatoriQ12884.

    Organism-specific databases

    HPAiHPA059739.

    Interactioni

    Subunit structurei

    Homodimer, or heterodimer with DPP4. The monomer is inactive.1 Publication

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

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ12884.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 44CytoplasmicSequence Analysis
    Topological domaini26 – 760735ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei5 – 2521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9B family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1506.
    HOGENOMiHOG000231875.
    HOVERGENiHBG005527.
    InParanoidiQ12884.
    KOiK08674.
    OMAiQYYTARF.
    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.
    PROSITEiPS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

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

    Also known as: L

    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

    MKTWVKIVFG VATSAVLALL VMCIVLRPSR VHNSEENTMR ALTLKDILNG    50
    TFSYKTFFPN WISGQEYLHQ SADNNIVLYN IETGQSYTIL SNRTMKSVNA 100
    SNYGLSPDRQ FVYLESDYSK LWRYSYTATY YIYDLSNGEF VRGNELPRPI 150
    QYLCWSPVGS KLAYVYQNNI YLKQRPGDPP FQITFNGREN KIFNGIPDWV 200
    YEEEMLATKY ALWWSPNGKF LAYAEFNDTD IPVIAYSYYG DEQYPRTINI 250
    PYPKAGAKNP VVRIFIIDTT YPAYVGPQEV PVPAMIASSD YYFSWLTWVT 300
    DERVCLQWLK RVQNVSVLSI CDFREDWQTW DCPKTQEHIE ESRTGWAGGF 350
    FVSTPVFSYD AISYYKIFSD KDGYKHIHYI KDTVENAIQI TSGKWEAINI 400
    FRVTQDSLFY SSNEFEEYPG RRNIYRISIG SYPPSKKCVT CHLRKERCQY 450
    YTASFSDYAK YYALVCYGPG IPISTLHDGR TDQEIKILEE NKELENALKN 500
    IQLPKEEIKK LEVDEITLWY KMILPPQFDR SKKYPLLIQV YGGPCSQSVR 550
    SVFAVNWISY LASKEGMVIA LVDGRGTAFQ GDKLLYAVYR KLGVYEVEDQ 600
    ITAVRKFIEM GFIDEKRIAI WGWSYGGYVS SLALASGTGL FKCGIAVAPV 650
    SSWEYYASVY TERFMGLPTK DDNLEHYKNS TVMARAEYFR NVDYLLIHGT 700
    ADDNVHFQNS AQIAKALVNA QVDFQAMWYS DQNHGLSGLS TNHLYTHMTH 750
    FLKQCFSLSD 760

    Note: Major isoform.

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

    Also known as: S, Truncated

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

    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

    Alternative sequence

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi292495099.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS33311.1. [Q12884-1 ]
    RefSeqi NP_001278736.1. NM_001291807.1.
    NP_004451.2. NM_004460.3. [Q12884-1 ]
    UniGenei Hs.654370.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Z68 X-ray 2.60 A/B 39-757 [» ]
    ProteinModelPortali Q12884.
    SMRi Q12884. Positions 39-757.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108485. 4 interactions.
    IntActi Q12884. 10 interactions.
    MINTi MINT-4778828.
    STRINGi 9606.ENSP00000188790.

    Chemistry

    ChEMBLi CHEMBL4683.

    Protein family/group databases

    MEROPSi S09.007.

    PTM databases

    PhosphoSitei Q12884.

    Polymorphism databases

    DMDMi 292495099.

    Proteomic databases

    PaxDbi Q12884.
    PRIDEi Q12884.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000188790 ; ENSP00000188790 ; ENSG00000078098 . [Q12884-1 ]
    GeneIDi 2191.
    KEGGi hsa:2191.
    UCSCi uc002ucd.3. human. [Q12884-1 ]
    uc010fpc.3. human. [Q12884-2 ]

    Organism-specific databases

    CTDi 2191.
    GeneCardsi GC02M163027.
    H-InvDB HIX0002548.
    HGNCi HGNC:3590. FAP.
    HPAi HPA059739.
    MIMi 600403. gene.
    neXtProti NX_Q12884.
    PharmGKBi PA28003.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1506.
    HOGENOMi HOG000231875.
    HOVERGENi HBG005527.
    InParanoidi Q12884.
    KOi K08674.
    OMAi QYYTARF.
    OrthoDBi EOG761BT2.
    PhylomeDBi Q12884.
    TreeFami TF313309.

    Miscellaneous databases

    ChiTaRSi FAP. human.
    EvolutionaryTracei Q12884.
    GeneWikii Fibroblast_activation_protein,_alpha.
    GenomeRNAii 2191.
    NextBioi 8851.
    PROi Q12884.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12884.
    Bgeei Q12884.
    CleanExi HS_FAP.
    Genevestigatori Q12884.

    Family and domain databases

    Gene3Di 2.140.10.30. 1 hit.
    3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR001375. Peptidase_S9.
    IPR002469. Peptidase_S9B.
    [Graphical view ]
    Pfami PF00930. DPPIV_N. 1 hit.
    PF00326. Peptidase_S9. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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).
      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.
      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] (ISOFORM 2).
      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. "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.
    9. "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.
    10. "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, HETERODIMERIZATION, SUBCELLULAR LOCATION.
    11. "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, 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: October 1, 2014
    This is version 148 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3