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P21754

- ZP3_HUMAN

UniProt

P21754 - ZP3_HUMAN

Protein

Zona pellucida sperm-binding protein 3

Gene

ZP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (07 Jul 2009)
      Previous versions | rss
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    Functioni

    The mammalian zona pellucida, which mediates species-specific sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy, is composed of three to four glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona matrix formation.

    GO - Molecular functioni

    1. acrosin binding Source: UniProtKB
    2. carbohydrate binding Source: UniProtKB
    3. manganese ion transmembrane transporter activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. signal transducer activity Source: UniProtKB
    6. store-operated calcium channel activity Source: UniProtKB

    GO - Biological processi

    1. binding of sperm to zona pellucida Source: UniProtKB
    2. blastocyst formation Source: UniProtKB
    3. calcium ion transmembrane transport Source: GOC
    4. egg coat formation Source: UniProtKB
    5. humoral immune response mediated by circulating immunoglobulin Source: UniProtKB
    6. intracellular protein transport Source: UniProtKB
    7. intracellular signal transduction Source: UniProtKB
    8. manganese ion transmembrane transport Source: GOC
    9. manganese ion transport Source: UniProtKB
    10. multicellular organism reproduction Source: Reactome
    11. negative regulation of binding of sperm to zona pellucida Source: UniProtKB
    12. negative regulation of transcription, DNA-templated Source: UniProtKB
    13. oocyte development Source: UniProtKB
    14. phosphatidylinositol-mediated signaling Source: UniProtKB
    15. positive regulation of acrosomal vesicle exocytosis Source: UniProtKB
    16. positive regulation of acrosome reaction Source: UniProtKB
    17. positive regulation of antral ovarian follicle growth Source: UniProtKB
    18. positive regulation of calcium ion import Source: UniProtKB
    19. positive regulation of humoral immune response Source: UniProtKB
    20. positive regulation of inflammatory response Source: UniProtKB
    21. positive regulation of interferon-gamma production Source: UniProtKB
    22. positive regulation of interleukin-4 production Source: UniProtKB
    23. positive regulation of leukocyte migration Source: UniProtKB
    24. positive regulation of ovarian follicle development Source: UniProtKB
    25. positive regulation of phosphatidylinositol biosynthetic process Source: UniProtKB
    26. positive regulation of protein kinase activity Source: UniProtKB
    27. positive regulation of protein kinase B signaling Source: UniProtKB
    28. positive regulation of T cell proliferation Source: UniProtKB
    29. positive regulation of transcription, DNA-templated Source: UniProtKB
    30. positive regulation of type IV hypersensitivity Source: UniProtKB
    31. protein kinase C signaling Source: UniProtKB
    32. single fertilization Source: Reactome

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Fertilization

    Enzyme and pathway databases

    ReactomeiREACT_163933. Interaction With The Zona Pellucida.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Zona pellucida sperm-binding protein 3
    Alternative name(s):
    Sperm receptor
    ZP3A/ZP3B
    Zona pellucida glycoprotein 3
    Short name:
    Zp-3
    Zona pellucida protein C
    Cleaved into the following chain:
    Gene namesi
    Name:ZP3
    Synonyms:ZP3A, ZP3B, ZPC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:13189. ZP3.

    Subcellular locationi

    Chain Processed zona pellucida sperm-binding protein 3 : Secretedextracellular spaceextracellular matrix
    Note: The glycoproteinaceous translucent extracellular matrix that surrounds the mammalian oocyte is called zona pellucida.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. endoplasmic reticulum Source: UniProtKB
    3. extracellular matrix Source: UniProtKB
    4. extracellular region Source: Reactome
    5. extracellular space Source: UniProtKB
    6. Golgi apparatus Source: UniProtKB
    7. integral component of membrane Source: UniProtKB-KW
    8. multivesicular body Source: UniProtKB
    9. outer acrosomal membrane Source: UniProtKB
    10. perinuclear region of cytoplasm Source: UniProtKB
    11. plasma membrane Source: UniProtKB
    12. proteinaceous extracellular matrix Source: UniProtKB-SubCell
    13. secretory granule Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Extracellular matrix, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37757.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 350328Zona pellucida sperm-binding protein 3PRO_0000041709Add
    BLAST
    Chaini23 – ?Processed zona pellucida sperm-binding protein 3PRO_0000304569
    Propeptidei351 – 42474Removed in mature formBy similarityPRO_0000041710Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei23 – 231Pyrrolidone carboxylic acid1 Publication
    Disulfide bondi46 ↔ 1401 Publication
    Disulfide bondi78 ↔ 991 Publication
    Glycosylationi125 – 1251N-linked (GlcNAc...)1 Publication
    Glycosylationi147 – 1471N-linked (GlcNAc...)1 Publication
    Glycosylationi156 – 1561O-linked (GalNAc...)By similarity
    Glycosylationi162 – 1621O-linked (GalNAc...)By similarity
    Glycosylationi163 – 1631O-linked (GalNAc...)By similarity
    Disulfide bondi217 ↔ 2821 Publication
    Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi239 ↔ 3001 Publication
    Glycosylationi272 – 2721N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.1 Publication
    N-glycosylated.By similarity
    O-glycosylated; removal of O-linked glycans may play an important role in the post-fertilization block to polyspermy.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    PaxDbiP21754.
    PRIDEiP21754.

    PTM databases

    PhosphoSiteiP21754.

    Expressioni

    Tissue specificityi

    Oocytes.

    Gene expression databases

    ArrayExpressiP21754.
    BgeeiP21754.
    CleanExiHS_ZP3.
    GenevestigatoriP21754.

    Organism-specific databases

    HPAiHPA054061.

    Interactioni

    Subunit structurei

    Polymers of ZP2 and ZP3 organized into long filaments cross-linked by ZP1 homodimers.By similarity

    Protein-protein interaction databases

    BioGridi113565. 9 interactions.
    STRINGi9606.ENSP00000378326.

    Structurei

    3D structure databases

    ProteinModelPortaliP21754.
    SMRiP21754. Positions 41-330.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 387365ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini409 – 42416CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei388 – 40821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 307263ZPPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.

    Sequence similaritiesi

    Belongs to the ZP domain family. ZPC subfamily.Curated
    Contains 1 ZP domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG43042.
    HOGENOMiHOG000220813.
    HOVERGENiHBG007985.
    OMAiLMEEDWG.
    OrthoDBiEOG773XG3.
    PhylomeDBiP21754.
    TreeFamiTF331369.

    Family and domain databases

    InterProiIPR001507. ZP_dom.
    IPR017977. ZP_dom_CS.
    [Graphical view]
    PfamiPF00100. Zona_pellucida. 1 hit.
    [Graphical view]
    PRINTSiPR00023. ZPELLUCIDA.
    SMARTiSM00241. ZP. 1 hit.
    [Graphical view]
    PROSITEiPS00682. ZP_1. 1 hit.
    PS51034. ZP_2. 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 ZP3A (identifier: P21754-1) [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

    MELSYRLFIC LLLWGSTELC YPQPLWLLQG GASHPETSVQ PVLVECQEAT    50
    LMVMVSKDLF GTGKLIRAAD LTLGPEACEP LVSMDTEDVV RFEVGLHECG 100
    NSMQVTDDAL VYSTFLLHDP RPVGNLSIVR TNRAEIPIEC RYPRQGNVSS 150
    QAILPTWLPF RTTVFSEEKL TFSLRLMEEN WNAEKRSPTF HLGDAAHLQA 200
    EIHTGSHVPL RLFVDHCVAT PTPDQNASPY HTIVDFHGCL VDGLTDASSA 250
    FKVPRPGPDT LQFTVDVFHF ANDSRNMIYI TCHLKVTLAE QDPDELNKAC 300
    SFSKPSNSWF PVEGSADICQ CCNKGDCGTP SHSRRQPHVM SQWSRSASRN 350
    RRHVTEEADV TVGPLIFLDR RGDHEVEQWA LPSDTSVVLL GVGLAVVVSL 400
    TLTAVILVLT RRCRTASHPV SASE 424
    Length:424
    Mass (Da):47,018
    Last modified:July 7, 2009 - v2
    Checksum:i0F3CCDA2427C0E3A
    GO
    Isoform ZP3B (identifier: P21754-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         364-372: PLIFLDRRG → ATDLPGQEW
         373-424: Missing.

    Note: Found in a second polymorphic locus which, due to an extra G residue in exon 8, has the potential to encode a truncated protein of 372 amino acids.

    Show »
    Length:372
    Mass (Da):41,469
    Checksum:iAB7BD85572DB7B4A
    GO
    Isoform 3 (identifier: P21754-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-51: Missing.

    Show »
    Length:373
    Mass (Da):41,272
    Checksum:i2CF838B25DC801C0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti345 – 3451R → T in CAA40095. (PubMed:1478648)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311G → R.
    Corresponds to variant rs2286428 [ dbSNP | Ensembl ].
    VAR_058011
    Natural varianti315 – 3151S → P.4 Publications
    Corresponds to variant rs2906999 [ dbSNP | Ensembl ].
    VAR_058012
    Natural varianti340 – 3401M → V.
    Corresponds to variant rs2906997 [ dbSNP | Ensembl ].
    VAR_058013

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5151Missing in isoform 3. 2 PublicationsVSP_037556Add
    BLAST
    Alternative sequencei364 – 3729PLIFLDRRG → ATDLPGQEW in isoform ZP3B. 1 PublicationVSP_006949
    Alternative sequencei373 – 42452Missing in isoform ZP3B. 1 PublicationVSP_006950Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60504 mRNA. Translation: AAA61336.1.
    X56777 mRNA. Translation: CAA40095.1.
    AK292763 mRNA. Translation: BAF85452.1.
    AC005522 Genomic DNA. No translation available.
    BC113949 mRNA. Translation: AAI13950.2.
    CCDSiCCDS47618.1. [P21754-1]
    CCDS5586.1. [P21754-3]
    PIRiA36000.
    RefSeqiNP_001103824.1. NM_001110354.1. [P21754-1]
    NP_009086.4. NM_007155.5. [P21754-3]
    UniGeneiHs.656137.

    Genome annotation databases

    EnsembliENST00000336517; ENSP00000337310; ENSG00000188372. [P21754-3]
    ENST00000394857; ENSP00000378326; ENSG00000188372. [P21754-1]
    GeneIDi7784.
    KEGGihsa:7784.
    UCSCiuc003ufc.4. human. [P21754-1]

    Polymorphism databases

    DMDMi251757420.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Molecular chastity - Issue 93 of April 2008

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60504 mRNA. Translation: AAA61336.1 .
    X56777 mRNA. Translation: CAA40095.1 .
    AK292763 mRNA. Translation: BAF85452.1 .
    AC005522 Genomic DNA. No translation available.
    BC113949 mRNA. Translation: AAI13950.2 .
    CCDSi CCDS47618.1. [P21754-1 ]
    CCDS5586.1. [P21754-3 ]
    PIRi A36000.
    RefSeqi NP_001103824.1. NM_001110354.1. [P21754-1 ]
    NP_009086.4. NM_007155.5. [P21754-3 ]
    UniGenei Hs.656137.

    3D structure databases

    ProteinModelPortali P21754.
    SMRi P21754. Positions 41-330.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113565. 9 interactions.
    STRINGi 9606.ENSP00000378326.

    PTM databases

    PhosphoSitei P21754.

    Polymorphism databases

    DMDMi 251757420.

    Proteomic databases

    PaxDbi P21754.
    PRIDEi P21754.

    Protocols and materials databases

    DNASUi 7784.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336517 ; ENSP00000337310 ; ENSG00000188372 . [P21754-3 ]
    ENST00000394857 ; ENSP00000378326 ; ENSG00000188372 . [P21754-1 ]
    GeneIDi 7784.
    KEGGi hsa:7784.
    UCSCi uc003ufc.4. human. [P21754-1 ]

    Organism-specific databases

    CTDi 7784.
    GeneCardsi GC07P076026.
    HGNCi HGNC:13189. ZP3.
    HPAi HPA054061.
    MIMi 182889. gene.
    neXtProti NX_P21754.
    PharmGKBi PA37757.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43042.
    HOGENOMi HOG000220813.
    HOVERGENi HBG007985.
    OMAi LMEEDWG.
    OrthoDBi EOG773XG3.
    PhylomeDBi P21754.
    TreeFami TF331369.

    Enzyme and pathway databases

    Reactomei REACT_163933. Interaction With The Zona Pellucida.

    Miscellaneous databases

    GeneWikii ZP3.
    GenomeRNAii 7784.
    NextBioi 30137.
    PROi P21754.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21754.
    Bgeei P21754.
    CleanExi HS_ZP3.
    Genevestigatori P21754.

    Family and domain databases

    InterProi IPR001507. ZP_dom.
    IPR017977. ZP_dom_CS.
    [Graphical view ]
    Pfami PF00100. Zona_pellucida. 1 hit.
    [Graphical view ]
    PRINTSi PR00023. ZPELLUCIDA.
    SMARTi SM00241. ZP. 1 hit.
    [Graphical view ]
    PROSITEi PS00682. ZP_1. 1 hit.
    PS51034. ZP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZP3A), VARIANT PRO-315.
    2. "Cloning and characterization of the human sperm receptor ligand ZP3: evidence for a second polymorphic allele with a different frequency in the Caucasian and Japanese populations."
      van Duin M., Polman J.E., Verkoelen C.C., Bunschoten H., Meyerink J.H., Olijve W., Aitken R.J.
      Genomics 14:1064-1070(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ZP3A AND ZP3B), VARIANT PRO-315.
      Tissue: Ovary.
    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), VARIANT PRO-315.
      Tissue: Lung.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [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 3), VARIANT PRO-315.
      Tissue: Brain.
    6. "Mass spectrometry analysis of recombinant human ZP3 expressed in glycosylation-deficient CHO cells."
      Zhao M., Boja E.S., Hoodbhoy T., Nawrocki J., Kaufman J.B., Kresge N., Ghirlando R., Shiloach J., Pannell L., Levine R.L., Fales H.M., Dean J.
      Biochemistry 43:12090-12104(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIGNAL SEQUENCE CLEAVAGE SITE, PYROGLUTAMATE FORMATION AT GLU-23, PROTEOLYTIC PROCESSING, DISULFIDE BONDS, GLYCOSYLATION AT ASN-125; ASN-147 AND ASN-272.

    Entry informationi

    Entry nameiZP3_HUMAN
    AccessioniPrimary (citable) accession number: P21754
    Secondary accession number(s): Q06633, Q29RW0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 135 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3