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Q12884

- SEPR_HUMAN

UniProt

Q12884 - SEPR_HUMAN

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Protein

Seprase

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

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 Publication
Active sitei702 – 7021Charge relay system1 Publication
Active sitei734 – 7341Charge relay system1 Publication

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
Complete GO annotation...

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; Single-pass type II membrane protein. Cell projectionlamellipodium membrane; Single-pass type II membrane protein. Cell projectioninvadopodium membrane; Single-pass type II membrane protein
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.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44Cytoplasmic Reviewed prediction
Transmembranei5 – 2521Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini26 – 760735Extracellular Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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...) Reviewed prediction

Post-translational modificationi

N-glycosylated.1 Publication
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.2 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 – 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.

Miscellaneous databases

EvolutionaryTraceiQ12884.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9B family.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 521521Missing in isoform 2. VSP_005367Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071A → P in AAB49652. 1 Publication
Sequence conflicti229 – 2291T → K in AAB49652. 1 Publication
Sequence conflicti354 – 3541T → R in AAB49652. 1 Publication

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

« 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).
    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: July 9, 2014
This is version 147 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

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