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Reviewed, UniProtKB/Swiss-Prot Q9NPF4 (OSGEP_HUMAN)

Last modified November 3, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable O-sialoglycoprotein endopeptidase
      Short name=hOSGEP
    EC=3.4.24.57
Gene names
Name: OSGEP
Synonyms: GCPL1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

O-sialoglycoprotein endopeptidases specifically cleave the polypeptide backbone of membrane glycoproteins that contain clusters of O-linked sialoglycans By similarity.

Catalytic activity

Hydrolysis of O-sialoglycoproteins; cleaves 31-Arg-|-Asp-32 bond in glycophorin A. Does not cleave unglycosylated proteins, desialylated glycoproteins or glycoproteins that are only N-glycosylated.

Cofactor

Zinc Probable.

Tissue specificity

Widely expressed at low level. Expressed in heart, placenta, liver, kidney, lung, brain, skeletal muscle and pancreas. Ref.1

Sequence similarities

Belongs to the peptidase M22 family.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 335335Probable O-sialoglycoprotein endopeptidase
PRO_0000096984

Sites

Metal binding1091Zinc Potential
Metal binding1131Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q9NPF4-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 54DCBBB26C03E8FB

FASTA33536,427
        10         20         30         40         50         60 
MPAVLGFEGS ANKIGVGVVR DGKVLANPRR TYVTPPGTGF LPGDTARHHR AVILDLLQEA 

        70         80         90        100        110        120 
LTESGLTSQD IDCIAYTKGP GMGAPLVSVA VVARTVAQLW NKPLVGVNHC IGHIEMGRLI 

       130        140        150        160        170        180 
TGATSPTVLY VSGGNTQVIA YSEHRYRIFG ETIDIAVGNC LDRFARVLKI SNDPSPGYNI 

       190        200        210        220        230        240 
EQMAKRGKKL VELPYTVKGM DVSFSGILSF IEDVAHRMLA TGECTPEDLC FSLQETVFAM 

       250        260        270        280        290        300 
LVEITERAMA HCGSQEALIV GGVGCNVRLQ EMMATMCQER GARLFATDER FCIDNGAMIA 

       310        320        330 
QAGWEMFRAG HRTPLSDSGV TQRYRTDEVE VTWRD 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing analysis of a putative human O-sialoglycoprotein endopeptidase gene (OSGEP) and analysis of a bidirectional promoter between the OSGEP and APEX genes."
Seki Y., Ikeda S., Kiyohara H., Ayabe H., Seki T., Matsui H.
Gene 285:101-108(2002) [PubMed: 12039036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
Tissue: Placenta.
[2]"Cloning and sequencing of putative human sialoglycoprotease."
Wigelsworth D.J., Coadwell J., Rawlings N.D., Barrett A.J.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Carcinoma.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Blood.
[6]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

AB047823 Genomic DNA. Translation: BAB33147.1.
AB050442 mRNA. Translation: BAB33172.1.
AJ271669 mRNA. Translation: CAB71031.1.
AK000418 mRNA. Translation: BAA91150.1.
CR457232 mRNA. Translation: CAG33513.1.
BC032310 mRNA. Translation: AAH32310.1.
IPIIPI00015809.
RefSeqNP_060277.1.
UniGeneHs.525196
Hs.73722

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9NPF4. 3 interactions.
STRINGQ9NPF4.

Protein family/group databases

MEROPSM22.003.

Proteomic databases

PeptideAtlasQ9NPF4.
PRIDEQ9NPF4.

Genome annotation databases

EnsemblENST00000206542; ENSP00000206542; ENSG00000092094; Homo sapiens. [Genome view]
GeneID55644.
KEGGhsa:55644.
UCSCuc001vxf.1. human.

Organism-specific databases

CTD55644.
GeneCardsGC14M019985.
HGNCHGNC:18028. OSGEP.
MIM610107. gene.
PharmGKBPA32834.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9NPF4.
HOVERGENQ9NPF4.
OMATQRFRTD.

Enzyme and pathway databases

BRENDA3.4.24.57. 247.

Gene expression databases

ArrayExpressQ9NPF4.
BgeeQ9NPF4.
CleanExHS_OSGEP.
GenevestigatorQ9NPF4.
GermOnlineENSG00000092094. Homo sapiens.

Family and domain databases

InterProIPR009180. Pept_M22_Osialgl.
IPR000905. Peptidase_M22.
IPR017860. Peptidase_M22_CS.
IPR017861. Peptidase_M22_subgr.
[Graphical view]
PANTHERPTHR11735. Pept_M22_Osialgl. 1 hit.
PfamPF00814. Peptidase_M22. 1 hit.
[Graphical view]
PRINTSPR00789. OSIALOPTASE.
ProDomPD002367. Peptidase_M22. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00329. gcp. 1 hit.
PROSITEPS01016. GLYCOPROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio60334.
SOURCESearch...

Entry information

Entry nameOSGEP_HUMAN
AccessionPrimary (citable) accession number: Q9NPF4
Secondary accession number(s): Q6IAC3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: October 1, 2000
Last modified: November 3, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents