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O95925

- EPPI_HUMAN

UniProt

O95925 - EPPI_HUMAN

Protein

Eppin

Gene

EPPIN

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

    Serine protease inhibitor that plays an essential role in male reproduction and fertility. Modulates the hydrolysis of SEMG1 by KLK3/PSA (a serine protease), provides antimicrobial protection for spermatozoa in the ejaculate coagulum, and binds SEMG1 thereby inhibiting sperm motility.2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

    GO - Biological processi

    1. defense response to bacterium Source: UniProtKB
    2. negative regulation of peptidase activity Source: UniProtKB

    Keywords - Molecular functioni

    Antimicrobial, Protease inhibitor, Serine protease inhibitor

    Protein family/group databases

    MEROPSiI02.058.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eppin
    Alternative name(s):
    Cancer/testis antigen 71
    Short name:
    CT71
    Epididymal protease inhibitor
    Protease inhibitor WAP7
    Serine protease inhibitor-like with Kunitz and WAP domains 1
    WAP four-disulfide core domain protein 7
    Gene namesi
    Name:EPPIN
    Synonyms:SPINLW1, WAP7, WFDC7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15932. EPPIN.
    HGNC:38825. EPPIN-WFDC6.

    Subcellular locationi

    Isoform 1 : Secreted. Cell surface
    Note: Bound to the surface of testicular and on the head and tail of ejaculate spermatozoa.

    GO - Cellular componenti

    1. cell surface Source: UniProtKB-SubCell
    2. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi87 – 871L → G: Loss of effect on KLK3 activity. 1 Publication
    Mutagenesisi102 – 1021C → A: Reduces the binding to SEMG1 by 45%. 1 Publication
    Mutagenesisi107 – 1071Y → A: Reduces the binding to SEMG1 by 68%. 1 Publication
    Mutagenesisi110 – 1101C → A: Does not affect the binding of SEMG1 or LTF. Does not affect the binding of SEMG1; when associated with A-123 and A-127. 1 Publication
    Mutagenesisi117 – 1171F → A: Reduces the binding to SEMG1 by 68% and to LTF by 73%. 1 Publication
    Mutagenesisi123 – 1231C → A: Does not affect the binding of SEMG1 or LTF. Does not affect the binding of SEMG1; when associated with A-110 and A-127. 1 Publication
    Mutagenesisi127 – 1271C → A: Does not affect the binding of SEMG1 or LTF. Does not affect the binding of SEMG1; when associated with A-110 and A-123. 1 Publication

    Organism-specific databases

    PharmGKBiPA38054.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 133112EppinPRO_0000041378Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi33 ↔ 61By similarity
    Disulfide bondi40 ↔ 65By similarity
    Disulfide bondi48 ↔ 60By similarity
    Disulfide bondi54 ↔ 69By similarity
    Disulfide bondi77 ↔ 127By similarity
    Disulfide bondi86 ↔ 110By similarity
    Disulfide bondi102 ↔ 123By similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiO95925.
    PRIDEiO95925.

    Expressioni

    Tissue specificityi

    In testis, expressed and secreted by Sertoli cells, appearing on the surface of testicular and ejaculate spermatozoa. Expressed in the spermatogonia and the earliest preleptotene spermatocytes. In the epididymis, is expressed and secreted by epithelial cells and covers the surface of epididymal spermatozoa and ciliated epithelial cells (at protein level). Expressed specifically in epididymis and testis. Isoform 2 is expressed only in the epididymis. Weak expression is detected in myoid cells as well as spermatogenic cells.2 Publications

    Gene expression databases

    ArrayExpressiO95925.
    BgeeiO95925.
    CleanExiHS_SPINLW1.
    GenevestigatoriO95925.

    Interactioni

    Subunit structurei

    Monomer. Homodimer. Homomultimers. Interacts with SEMG1 (via 164-283 AA). Interacts with LTF. Found in a complex with LTF, CLU, EPPIN and SEMG1.4 Publications

    Protein-protein interaction databases

    IntActiO95925. 1 interaction.
    STRINGi9606.ENSP00000361746.

    Structurei

    3D structure databases

    ProteinModelPortaliO95925.
    SMRiO95925. Positions 35-133.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 7348WAPPROSITE-ProRule annotationAdd
    BLAST
    Domaini77 – 12751BPTI/Kunitz inhibitorPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni102 – 13332Interaction with SEMG1Add
    BLAST
    Regioni117 – 13317Interaction with LTFAdd
    BLAST

    Domaini

    The BPTI/Kunitz inhibitor domain is required for elastase inhibitory activity. BPTI/Kunitz inhibitor and WAP domains are involved in the protein antibacterial activity.1 Publication

    Sequence similaritiesi

    Contains 1 BPTI/Kunitz inhibitor domain.PROSITE-ProRule annotation
    Contains 1 WAP domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG314382.
    HOGENOMiHOG000115819.
    HOVERGENiHBG004024.
    OMAiFPRRCPK.
    OrthoDBiEOG754HSR.
    PhylomeDBiO95925.
    TreeFamiTF342459.

    Family and domain databases

    Gene3Di4.10.410.10. 1 hit.
    4.10.75.10. 1 hit.
    InterProiIPR002223. Prot_inh_Kunz-m.
    IPR020901. Prtase_inh_Kunz-CS.
    IPR008197. WAP.
    [Graphical view]
    PfamiPF00014. Kunitz_BPTI. 1 hit.
    PF00095. WAP. 1 hit.
    [Graphical view]
    PRINTSiPR00759. BASICPTASE.
    SMARTiSM00131. KU. 1 hit.
    SM00217. WAP. 1 hit.
    [Graphical view]
    SUPFAMiSSF57256. SSF57256. 1 hit.
    SSF57362. SSF57362. 1 hit.
    PROSITEiPS00280. BPTI_KUNITZ_1. 1 hit.
    PS50279. BPTI_KUNITZ_2. 1 hit.
    PS51390. WAP. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95925-1) [UniParc]FASTAAdd to Basket

    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

    MGSSGLLSLL VLFVLLANVQ GPGLTDWLFP RRCPKIREEC EFQERDVCTK    50
    DRQCQDNKKC CVFSCGKKCL DLKQDVCEMP KETGPCLAYF LHWWYDKKDN 100
    TCSMFVYGGC QGNNNNFQSK ANCLNTCKNK RFP 133
    Length:133
    Mass (Da):15,284
    Last modified:May 1, 1999 - v1
    Checksum:iF7831B203366D9DC
    GO
    Isoform 2 (identifier: O95925-2) [UniParc]FASTAAdd to Basket

    Also known as: Eppin-2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-31: MGSSGLLSLLVLFVLLANVQGPGLTDWLFPR → MLSKAHGCKTALSLG

    Note: Lacks a cleavable signal sequence.

    Show »
    Length:117
    Mass (Da):13,486
    Checksum:i96161FAB3CFEDB47
    GO
    Isoform 3 (identifier: O95925-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         131-133: RFP → QPCPKIKVECEVEEIDQCTKPRDCPENMKCCPFSRGKKCLDFRKASLST

    Note: Based on a readthrough transcript which may produce a EPPIN-WFDC6 fusion protein. No experimental confirmation available.

    Show »
    Length:179
    Mass (Da):20,486
    Checksum:iAD2399D2093D0197
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti92 – 921H → R.
    Corresponds to variant rs2231838 [ dbSNP | Ensembl ].
    VAR_024696
    Natural varianti128 – 1281K → T.
    Corresponds to variant rs2231839 [ dbSNP | Ensembl ].
    VAR_052950

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3131MGSSG…WLFPR → MLSKAHGCKTALSLG in isoform 2. 1 PublicationVSP_006755Add
    BLAST
    Alternative sequencei131 – 1333RFP → QPCPKIKVECEVEEIDQCTK PRDCPENMKCCPFSRGKKCL DFRKASLST in isoform 3. 1 PublicationVSP_043679

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF286368 mRNA. Translation: AAG00546.1.
    AF286369 mRNA. Translation: AAG00547.1.
    AF286370 mRNA. Translation: AAG00548.1.
    AL118493 mRNA. Translation: CAB56343.1.
    AK301937 mRNA. Translation: BAG63357.1.
    AL031663 Genomic DNA. Translation: CAB37635.1.
    AL031663 Genomic DNA. Translation: CAO03536.1.
    AL031663 Genomic DNA. Translation: CAC36265.1.
    BC044829 mRNA. Translation: AAH44829.2.
    BC053369 mRNA. Translation: AAH53369.1.
    CCDSiCCDS13359.1. [O95925-1]
    RefSeqiNP_001185915.1. NM_001198986.1. [O95925-3]
    NP_065131.1. NM_020398.3. [O95925-1]
    UniGeneiHs.121084.
    Hs.274876.

    Genome annotation databases

    EnsembliENST00000336443; ENSP00000338114; ENSG00000101448. [O95925-2]
    ENST00000354280; ENSP00000361746; ENSG00000101448. [O95925-1]
    ENST00000504988; ENSP00000424176; ENSG00000249139. [O95925-3]
    GeneIDi100526773.
    57119.
    KEGGihsa:100526773.
    hsa:57119.
    UCSCiuc002xou.3. human. [O95925-1]
    uc010zxc.2. human. [O95925-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF286368 mRNA. Translation: AAG00546.1 .
    AF286369 mRNA. Translation: AAG00547.1 .
    AF286370 mRNA. Translation: AAG00548.1 .
    AL118493 mRNA. Translation: CAB56343.1 .
    AK301937 mRNA. Translation: BAG63357.1 .
    AL031663 Genomic DNA. Translation: CAB37635.1 .
    AL031663 Genomic DNA. Translation: CAO03536.1 .
    AL031663 Genomic DNA. Translation: CAC36265.1 .
    BC044829 mRNA. Translation: AAH44829.2 .
    BC053369 mRNA. Translation: AAH53369.1 .
    CCDSi CCDS13359.1. [O95925-1 ]
    RefSeqi NP_001185915.1. NM_001198986.1. [O95925-3 ]
    NP_065131.1. NM_020398.3. [O95925-1 ]
    UniGenei Hs.121084.
    Hs.274876.

    3D structure databases

    ProteinModelPortali O95925.
    SMRi O95925. Positions 35-133.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O95925. 1 interaction.
    STRINGi 9606.ENSP00000361746.

    Protein family/group databases

    MEROPSi I02.058.

    Proteomic databases

    PaxDbi O95925.
    PRIDEi O95925.

    Protocols and materials databases

    DNASUi 57119.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336443 ; ENSP00000338114 ; ENSG00000101448 . [O95925-2 ]
    ENST00000354280 ; ENSP00000361746 ; ENSG00000101448 . [O95925-1 ]
    ENST00000504988 ; ENSP00000424176 ; ENSG00000249139 . [O95925-3 ]
    GeneIDi 100526773.
    57119.
    KEGGi hsa:100526773.
    hsa:57119.
    UCSCi uc002xou.3. human. [O95925-1 ]
    uc010zxc.2. human. [O95925-3 ]

    Organism-specific databases

    CTDi 100526773.
    57119.
    GeneCardsi GC20M044164.
    GC20M044184.
    HGNCi HGNC:15932. EPPIN.
    HGNC:38825. EPPIN-WFDC6.
    MIMi 609031. gene.
    neXtProti NX_O95925.
    PharmGKBi PA38054.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG314382.
    HOGENOMi HOG000115819.
    HOVERGENi HBG004024.
    OMAi FPRRCPK.
    OrthoDBi EOG754HSR.
    PhylomeDBi O95925.
    TreeFami TF342459.

    Miscellaneous databases

    GeneWikii SPINLW1.
    NextBioi 62993.
    PROi O95925.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95925.
    Bgeei O95925.
    CleanExi HS_SPINLW1.
    Genevestigatori O95925.

    Family and domain databases

    Gene3Di 4.10.410.10. 1 hit.
    4.10.75.10. 1 hit.
    InterProi IPR002223. Prot_inh_Kunz-m.
    IPR020901. Prtase_inh_Kunz-CS.
    IPR008197. WAP.
    [Graphical view ]
    Pfami PF00014. Kunitz_BPTI. 1 hit.
    PF00095. WAP. 1 hit.
    [Graphical view ]
    PRINTSi PR00759. BASICPTASE.
    SMARTi SM00131. KU. 1 hit.
    SM00217. WAP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57256. SSF57256. 1 hit.
    SSF57362. SSF57362. 1 hit.
    PROSITEi PS00280. BPTI_KUNITZ_1. 1 hit.
    PS50279. BPTI_KUNITZ_2. 1 hit.
    PS51390. WAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of human eppin: a novel family of protease inhibitors expressed in the epididymis and testis."
      Richardson R.T., Sivashanmugam P., Hall S.H., Hamil K.G., Moore P.A., Ruben S.M., French F.S., O'Rand M.G.
      Gene 270:93-102(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBUNIT, TISSUE SPECIFICITY.
      Tissue: Epididymis and Testis.
    2. Stavrides G.S., Huckle E.J., Deloukas P.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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.
      , 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Testis.
    4. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    6. "Antimicrobial activity of human EPPIN, an androgen-regulated, sperm-bound protein with a whey acidic protein motif."
      Yenugu S., Richardson R.T., Sivashanmugam P., Wang Z., O'rand M.G., French F.S., Hall S.H.
      Biol. Reprod. 71:1484-1490(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Association of eppin with semenogelin on human spermatozoa."
      Wang Z., Widgren E.E., Sivashanmugam P., O'Rand M.G., Richardson R.T.
      Biol. Reprod. 72:1064-1070(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEMG1, SUBCELLULAR LOCATION, SUBUNIT.
    8. "Characterization of an eppin protein complex from human semen and spermatozoa."
      Wang Z., Widgren E.E., Richardson R.T., O'Rand M.G.
      Biol. Reprod. 77:476-484(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH LTF AND CLU, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "Eppin: a molecular strategy for male contraception."
      Wang Z., Widgren E.E., Richardson R.T., Orand M.G.
      Soc. Reprod. Fertil. Suppl. 65:535-542(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION ON KLK3 ACTIVITY, MUTAGENESIS OF LEU-87.
    10. "Functional domains of the human epididymal protease inhibitor, eppin."
      McCrudden M.T., Dafforn T.R., Houston D.F., Turkington P.T., Timson D.J.
      FEBS J. 275:1742-1750(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    11. "Distribution of Eppin in mouse and human testis."
      Long Y., Gu A., Yang H., Ji G., Han X., Song L., Wang S., Wang X.
      Mol. Med. Report. 4:71-75(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    12. "Characterization of EPPIN's semenogelin I binding Site: a contraceptive drug target."
      Silva E.J., Hamil K.G., Richardson R.T., O'Rand M.G.
      Biol. Reprod. 87:56-56(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LTF AND SEMG1, MUTAGENESIS OF CYS-102; TYR-107; CYS-110; PHE-117; CYS-123 AND CYS-127, PUTATIVE CONTRACEPTIVE TARGET.

    Entry informationi

    Entry nameiEPPI_HUMAN
    AccessioniPrimary (citable) accession number: O95925
    Secondary accession number(s): A6PVD6
    , Q86TP9, Q96SD7, Q9HD30
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 4, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 129 of the entry and version 1 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

    Miscellaneous

    Might be used as a target for male contraception.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3