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O95925

- EPPI_HUMAN

UniProt

O95925 - EPPI_HUMAN

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Protein
Eppin
Gene
EPPIN, SPINLW1, WAP7, WFDC7
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

GO - Biological processi

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

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.2 Publications

GO - Cellular componenti

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

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 – 2121 Reviewed prediction
Add
BLAST
Chaini22 – 133112Eppin
PRO_0000041378Add
BLAST

Amino acid modifications

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 7348WAP
Add
BLAST
Domaini77 – 12751BPTI/Kunitz inhibitor
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni102 – 13332Interaction with SEMG1
Add
BLAST
Regioni117 – 13317Interaction with LTF
Add
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 WAP domain.

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.
VSP_006755Add
BLAST
Alternative sequencei131 – 1333RFP → QPCPKIKVECEVEEIDQCTK PRDCPENMKCCPFSRGKKCL DFRKASLST in isoform 3.
VSP_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]
ENST00000555685; ENSP00000452085; ENSG00000101448. [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...

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 ]
ENST00000555685 ; ENSP00000452085 ; ENSG00000101448 . [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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 128 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

Similar proteinsi