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Q99PP2

- ZN318_MOUSE

UniProt

Q99PP2 - ZN318_MOUSE

Protein

Zinc finger protein 318

Gene

Znf318

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    Repressed AR-mediated transcriptional activation. May act as a transcriptional regulator during spermatogenesis and in particular, during meiotic division.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri912 – 94635Matrin-type 1Add
    BLAST
    Zinc fingeri985 – 100723Matrin-type 2Add
    BLAST

    GO - Molecular functioni

    1. nucleic acid binding Source: InterPro
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. meiotic nuclear division Source: UniProtKB-KW
    2. regulation of transcription, DNA-templated Source: UniProtKB-KW
    3. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Meiosis, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Zinc finger protein 318
    Alternative name(s):
    Testicular zinc finger protein
    Gene namesi
    Name:Znf318
    Synonyms:Tzf, Zfp318
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1889348. Zfp318.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 2064›2064Zinc finger protein 318PRO_0000191808Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei32 – 321PhosphoserineBy similarity
    Modified residuei73 – 731PhosphoserineBy similarity
    Modified residuei324 – 3241PhosphoserineBy similarity
    Modified residuei384 – 3841PhosphoserineBy similarity
    Modified residuei886 – 8861PhosphoserineBy similarity
    Modified residuei1272 – 12721PhosphoserineBy similarity
    Modified residuei1735 – 17351PhosphoserineBy similarity
    Modified residuei1881 – 18811PhosphoserineBy similarity
    Modified residuei1967 – 19671PhosphoserineBy similarity
    Modified residuei1970 – 19701PhosphoserineBy similarity
    Modified residuei2021 – 20211PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ99PP2.
    PRIDEiQ99PP2.

    PTM databases

    PhosphoSiteiQ99PP2.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 2 are highly expressed in testis, moderately expressed in adrenal gland and uterus and faintly expressed in brain, kidney and liver. Isoform 1 is expressed more in adrenal gland, uterus and liver than isoform 2 is. Expression during testicular development of isoform 1 and isoform 2 is restricted to spermatocytes at the pachytene stage of meiotic prophase and to round and elongated spermatids.2 Publications

    Gene expression databases

    CleanExiMM_ZFP318.
    GenevestigatoriQ99PP2.

    Interactioni

    Subunit structurei

    Interacts with the N-terminal domain of AR.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ99PP2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili175 – 20329Sequence AnalysisAdd
    BLAST
    Coiled coili731 – 830100Sequence AnalysisAdd
    BLAST
    Coiled coili1625 – 165430Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1297 – 132630Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 2 matrin-type zinc fingers.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri912 – 94635Matrin-type 1Add
    BLAST
    Zinc fingeri985 – 100723Matrin-type 2Add
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG87509.
    HOGENOMiHOG000043103.
    HOVERGENiHBG107139.
    InParanoidiQ99PP2.

    Family and domain databases

    InterProiIPR015880. Znf_C2H2-like.
    IPR003604. Znf_U1.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 2 hits.
    SM00451. ZnF_U1. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Fragment.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99PP2-1) [UniParc]FASTAAdd to Basket

    Also known as: TZF-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

    SLEESLRITV GNDHFCVSTP ERRRLSDRLG ISPVDGLQDM DRDDLTDDSD     50
    FTRSSQCSRG LERYISREEG PLSPFLGQLD EDYRTRETFL HRPEFSPQSS 100
    CHDELLRGTE RNRDKLKSSS YSIRSEERSR EAKRPRYDDT EKVHSSGGDH 150
    SSFTSGTRNY RQRRSSPSPR FLDPEFRELD LARRKREEEE EQSRSLSQEL 200
    VGVGDDQIGC SIPGLAGVLT TSEPGYSLQR PEEVPMMPKK SILKKRIEAD 250
    MKPSLQLESF SSGASSGEDH PLYSEHSPLP LSGAIAAFTS EIENKGTTVE 300
    ADLKEPQSNL YQWGPLREIP KDNSEKFDSF LGFKERLDLK AEGLEQQTDN 350
    LLPHERASQD GSGFSRILSM LADPTITQEK RRRSFPDIED EEKFLYGDEE 400
    EDIKSESPLK SLEDPESAGT RQKANSLPST PAVKLESLEE SNPEYAKIHN 450
    LLKTIGLDIG VAEIGKLAAR TQERLHGKKP SSRPSADRRL SADRHLSGDR 500
    HFSADRCSSV EHSFTADWRS SDPHRPESRE THHSNTQSPE VSHPHPASPV 550
    DPYLRTKNSP PFLKSDHPVC HVSGPEVVGS GFQSSVAVRC MLPSAPSTPI 600
    RLPHSAALSQ FHIPGASQFA AARIPPNYQG SVIPSASFDA YRHYMAYAAS 650
    RWPMYPASQP PSHPLSDPHR LLPVTKQAAR SRPNLRVIPT VTPAKPKQEI 700
    PVLGSISVKR IPVRVSIPSL IKYNPKKISD EKNRASQKQK VIEEREKLKT 750
    EQEARQKKMF YLTTELERLH KQQGEMLRKK RREKDGHKDP LLMEVSRLQD 800
    SIMKDIAELH KETEEAEKKQ SELDKVAQIL GIDIFDKSLK SSNDSKESTE 850
    KPEKEKSKSP EKELSPSNSS SSNKESKMNE KSCIKSPSST ESLQPTVKQS 900
    DQPVAAYEYY DAGSHWCKDC NTTCGTMFDF FTHMHNKKHT QTLDPYNRPW 950
    ASKTQSEAKQ DTVKRTDKIT VPAKGSEFLI PVTGFYCQLC EEFLGDPISG 1000
    EQHVKGHQHN ENYKKYVEEN PLYEERRNLD RQAGLAVVLE TERRRQNELK 1050
    RKLNEKPKEE KIEKKARIVR EVKEDDKAPG ELEEQLSEDG SAPEKGEVKG 1100
    NASLRPQVKE EVKKEPSVAS IAASFGKFSW KKPEKEEEKG SVVTPGAPKE 1150
    DTVETSKDRD DGKAEVGKAK PIKIKLSGKT VIAHTSPWTP VVTTSTQTKI 1200
    RPNLPIPSTV LRKSGSATVS KPAPLNTFLS IKSSGTSTKP LPVVKESSSD 1250
    LLLPPDIISK AFGGEEVVLK GSPEEKVELA EKNEPSQVPE QMLALLPPPP 1300
    PPPPPPPPPP PPPPPQAVPQ LSAPSPAQAN VVLTPVKSNS VISQTFSLGF 1350
    QGPNILNPGL PVAFMASEQP TVIPSDETAP GVSESDWDQT LISMLVRPPP 1400
    PLSSVFSEQA KKLEKRNSCL ATANAKDLYD IFYSSGGKGA HETKLSSSTL 1450
    ANGESSSLPR TESSDFSSTC TLNSSMSSED LPQCSALVTA TEISNLENPI 1500
    SKGMESTGKW SVVDQIDPKS RDSTYSFLQP LTRLYQNKPY EIVSPKTDTL 1550
    VMWTSGSSQN DTHKDRPPEG KIRFDLGEPG PPGTDSTSHL SDTHCQTNGP 1600
    QKLIEINLID NQNKNQEVYQ SEGCRESEMK RKTELKGKVA TEEEEEEEEE 1650
    GANSIEDSNS NHGNRNTWEG EIGQPKLSTV DKKGEQSSKL MTGHENTSKV 1700
    VIELSPSLPS KRTKIDLFPS LLQNPKSMPE LLLLSPAGSG LCLKRQEIWE 1750
    RPEKPGLEDV ELQGTRPELT VTIESKVLEN FDTTHLEVEG FASLRNLGDM 1800
    HANFHNSQTE QTRRSPTALS EKMSEEISVS SVMCNPSSSS DIEPVPSFSG 1850
    FPLESPKTLV LNFETEGAHS SSNSRNGRIT SNSLETGHPV ENVGHDLGGE 1900
    RTHQALDLLA GGMLSEDVKE TSPLQKDLLR MESTTVSPSG LGPSPCLPDL 1950
    VDFVTRTPGV PKQKPCSPLS EPDAFLKCSS LEMGSPPPEI LSVSVSEVAV 2000
    PQVSEDNDSA LNLVKTPPSG SPSRDQVVGG NVSPREMPEQ EAAVDVIPDH 2050
    TRSNVYNSQD YLNG 2064
    Length:2,064
    Mass (Da):228,220
    Last modified:January 15, 2008 - v2
    Checksum:iCA64069FFA9D269B
    GO
    Isoform 2 (identifier: Q99PP2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         942-981: TLDPYNRPWA...PAKGSEFLIP → GQFQKSSHFQ...YGNNVRPCGQ
         982-2064: Missing.

    Show »
    Length:981
    Mass (Da):110,832
    Checksum:i8CCE812CE531C1F6
    GO

    Sequence cautioni

    The sequence AAF61636.1 differs from that shown. Reason: Frameshift at positions 13 and 32.
    The sequence AAK00650.1 differs from that shown. Reason: Frameshift at positions 13 and 32.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei942 – 98140TLDPY…EFLIP → GQFQKSSHFQTEGLKQMFLL QECRDRNHRDYGNNVRPCGQ in isoform 2. 1 PublicationVSP_016594Add
    BLAST
    Alternative sequencei982 – 20641083Missing in isoform 2. 1 PublicationVSP_016595Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF159455 mRNA. Translation: AAF61636.1. Frameshift.
    AF227194 mRNA. Translation: AAK00650.1. Frameshift.
    AK011661 mRNA. Translation: BAC25342.1.
    AK157779 mRNA. Translation: BAE34193.1.
    PIRiJC7316.
    RefSeqiNP_997554.2. NM_207671.4.
    UniGeneiMm.439916.

    Genome annotation databases

    GeneIDi57908.
    KEGGimmu:57908.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF159455 mRNA. Translation: AAF61636.1 . Frameshift.
    AF227194 mRNA. Translation: AAK00650.1 . Frameshift.
    AK011661 mRNA. Translation: BAC25342.1 .
    AK157779 mRNA. Translation: BAE34193.1 .
    PIRi JC7316.
    RefSeqi NP_997554.2. NM_207671.4.
    UniGenei Mm.439916.

    3D structure databases

    ProteinModelPortali Q99PP2.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q99PP2.

    Proteomic databases

    PaxDbi Q99PP2.
    PRIDEi Q99PP2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 57908.
    KEGGi mmu:57908.

    Organism-specific databases

    CTDi 57908.
    MGIi MGI:1889348. Zfp318.

    Phylogenomic databases

    eggNOGi NOG87509.
    HOGENOMi HOG000043103.
    HOVERGENi HBG107139.
    InParanoidi Q99PP2.

    Miscellaneous databases

    ChiTaRSi ZNF318. mouse.
    NextBioi 314073.
    PROi Q99PP2.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_ZFP318.
    Genevestigatori Q99PP2.

    Family and domain databases

    InterProi IPR015880. Znf_C2H2-like.
    IPR003604. Znf_U1.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 2 hits.
    SM00451. ZnF_U1. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcript for a novel protein with a zinc finger motif is expressed at specific stages of mouse spermatogenesis."
      Inoue A., Ishiji A., Kasagi S., Ishizuka M., Hirose S., Baba T., Hagiwara H.
      Biochem. Biophys. Res. Commun. 273:398-403(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
      Strain: ddY.
      Tissue: Testis.
    2. "Molecular cloning and characteristics of a novel zinc finger protein and its splice variant whose transcripts are expressed during spermatogenesis."
      Ishizuka M., Ohshima H., Tamura N., Nakada T., Inoue A., Hirose S., Hagiwara H.
      Biochem. Biophys. Res. Commun. 301:1079-1085(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Strain: ddY.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 393-1057 AND 1999-2064 (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Embryo.
    4. Cited for: FUNCTION, INTERACTION WITH AR.

    Entry informationi

    Entry nameiZN318_MOUSE
    AccessioniPrimary (citable) accession number: Q99PP2
    Secondary accession number(s): Q3TZL5, Q8BMX9, Q9JJ01
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 89 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3