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Q5VUA4

- ZN318_HUMAN

UniProt

Q5VUA4 - ZN318_HUMAN

Protein

Zinc finger protein 318

Gene

ZNF318

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (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 By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1063 – 109735Matrin-type 1Add
    BLAST
    Zinc fingeri1136 – 116631Matrin-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):
    Endocrine regulatory protein
    Gene namesi
    Name:ZNF318
    ORF Names:HRIHFB2436
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:13578. ZNF318.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134923137.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 22792279Zinc finger protein 318PRO_0000191807Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei79 – 791Phosphoserine1 Publication
    Modified residuei81 – 811Phosphoserine1 Publication
    Modified residuei136 – 1361Phosphoserine2 Publications
    Modified residuei173 – 1731Phosphoserine2 Publications
    Modified residuei214 – 2141Phosphoserine2 Publications
    Modified residuei464 – 4641Phosphoserine1 Publication
    Modified residuei527 – 5271Phosphoserine2 Publications
    Modified residuei1037 – 10371Phosphoserine1 Publication
    Modified residuei1243 – 12431Phosphoserine3 Publications
    Modified residuei1420 – 14201Phosphoserine1 Publication
    Modified residuei1713 – 17131Phosphoserine1 Publication
    Modified residuei1896 – 18961Phosphoserine2 Publications
    Modified residuei2101 – 21011Phosphoserine2 Publications
    Modified residuei2189 – 21891Phosphoserine1 Publication
    Modified residuei2192 – 21921Phosphoserine1 Publication
    Modified residuei2243 – 22431Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ5VUA4.
    PaxDbiQ5VUA4.
    PRIDEiQ5VUA4.

    PTM databases

    PhosphoSiteiQ5VUA4.

    Expressioni

    Tissue specificityi

    Expressed in endocrine tissue.1 Publication

    Gene expression databases

    BgeeiQ5VUA4.
    CleanExiHS_ZNF318.
    GenevestigatoriQ5VUA4.

    Organism-specific databases

    HPAiHPA027022.
    HPA027031.

    Interactioni

    Subunit structurei

    Interacts with the N-terminal domain of AR.By similarity

    Protein-protein interaction databases

    BioGridi117299. 8 interactions.
    IntActiQ5VUA4. 2 interactions.
    STRINGi9606.ENSP00000354964.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5VUA4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili315 – 34329Sequence AnalysisAdd
    BLAST
    Coiled coili876 – 980105Sequence AnalysisAdd
    BLAST
    Coiled coili1768 – 179225Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi41 – 10363Pro-richAdd
    BLAST
    Compositional biasi1201 – 1327127Lys-richAdd
    BLAST
    Compositional biasi1433 – 1541109Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 2 matrin-type zinc fingers.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1063 – 109735Matrin-type 1Add
    BLAST
    Zinc fingeri1136 – 116631Matrin-type 2Add
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG87509.
    HOGENOMiHOG000043103.
    HOVERGENiHBG107139.
    InParanoidiQ5VUA4.
    OMAiQTKIRPN.
    OrthoDBiEOG71P298.
    PhylomeDBiQ5VUA4.
    TreeFamiTF350583.

    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: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5VUA4-1) [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

    MYRSSARSSV SSHRPKDDGG GGPRSGRSSG SSSGPARRSS PPPPPSGSSS     50
    RTPARRPRSP SGHRGRRASP SPPRGRRVSP SPPRARRGSP SPPRGRRLFP 100
    PGPAGFRGSS RGESRADYAR DGRGDHPGDS GSRRRSPGLC SDSLEKSLRI 150
    TVGNDHFCVS TPERRRLSDR LGSPVDNLED MDRDDLTDDS VFTRSSQCSR 200
    GLERYISQEE GPLSPFLGQL DEDYRTKETF LHRSDYSPHI SCHDELLRGT 250
    ERNREKLKGY SIRSEERSRE AKRPRYDDTV KINSMGGDHP SFTSGTRNYR 300
    QRRRSPSPRF LDPEFRELDL ARRKREEEEE RSRSLSQELV GVDGGGTGCS 350
    IPGLSGVLTA SEPGYSLHRP EEVSVMPKKS ILKKRIEVDI MEPSMQLESF 400
    SSSTSSSQDH PLYSGHPSLP LSGAIAAFAS EIENKGTMVE TALKEPQGNL 450
    YQWGPLPGIP KDNSPLREKF GSFLCHKDNL DLKAEGPERH TDFLLPHERA 500
    SQDGSGFSRI LSMLADSTST QEKRRRSFPD IEDEEKFLYG DEEEDLKAES 550
    VPKPLGSSES EVMRQKASSL PSSAPAVKLE SLEETNPEYA KIHDLLKTIG 600
    LDIGVAEISQ LAARTQERLH GKKPSLRSSA DRRSSVDRYF SADHCSSVDH 650
    RFSADRCSSV DHCFSADRRS SDPHRLESRE AHHSNTHSPE VSHPHPPSPV 700
    DPYLLTKNSP PFLKSDHPVG HISGPEVVGS GFQSSVAVRC MLPSAPSAPI 750
    RLPHTAALSQ FHMPRASQFA AARIPPNYQG PAIPPASFDA YRHYMAYAAS 800
    RWPMYPTSQP SNHPVPEPHR IMPITKQATR SRPNLRVIPT VTPDKPKQKE 850
    SLRGSIPAAQ VPVQVSIPSL IRYNPEKISD EKNRASQKQK VIEEREKLKN 900
    DREARQKKMY YLRTELERLH KQQGEMLRKK RREKDGHKDP LLVEVSRLQD 950
    NIMKDIAELR QEAEEAEKKQ SELDKVAQIL GINIFDKSQK SLSDSREPTE 1000
    KPGKAEKSKS PEKVSSFSNS SSNKESKVNN EKFRTKSPKP AESPQSATKQ 1050
    LDQPTAAYEY YDAGNHWCKD CNTICGTMFD FFTHMHNKKH TQTLDPYNRP 1100
    WASKTQSEAK QDAIKRTDKI TVPAKGSEFL VPISGFYCQL CEEFLGDPIS 1150
    GEQHVKGHQH NEKYKKYVDE NPLYEERRNL DRQAGLAVVL ETERRRQSEL 1200
    KRKLSEKPKE EKKEKKAKAV KEVKEDDKVS EKLEDQLSEG RNSPEKAENK 1250
    RNTGIKLQLK EEVKKESPTS SSFGKFSWKK PEKEEEKSSL VTPSISKEEI 1300
    LESSKDKEDG KTEAGKAKPI KIKLSGKTVV AHTSPWMPVV TTSTQTKIRP 1350
    NLPIPSTVLR KSCSATMSKP APLNTFLSIK SSGTTAKPLP VVKESSADLL 1400
    LPPDIISKAF GGEEVILKGS PEEKVVLAEK SEPSHLPEQI LPPPPPPPPP 1450
    PPPPPPVIPH PAAPSAAQAN AILAPVKSNP VVSQTLSPGF VGPNILNPVL 1500
    PVAIMASAQP AAIPSDETAP GVSESDRDQT LFSVLVRPPP PLSSVFSEQA 1550
    KKLEKRNSCL ATANAKDLYD IFYSSGGKGA PETKGAPETK LSGGPLANGE 1600
    NSNLSRTKSS DTSSTSPLNS SASQEELHQD EGLVAAPIVS NSEKPIAKTL 1650
    VALGKWSVVE HVGPKSTGST YGFLQPLTRL CQSRPYETIT PKTDTLAIWT 1700
    SSSFQSDTSR DISPEKSELD LGEPGPPGVE PPPQLLDIQC KESQKLVEIH 1750
    LRESVNQDKE SQELRKSEDC RESEIETNTE LKERVKELSE GIVDEGVSTS 1800
    IGPHSIDDSN LNHGNRYMWE GEVKQPNLLM IDKEAEQSNK LMTGSETPSK 1850
    VVIKLSPQAC SFTKAKLDSF LSEARSLLNP QDTPVKISAP ELLLHSPARS 1900
    AMCLTGSPQE QGVSVVSEEG LENSAPESAS RTSRYRSLKL KRERSKDFQV 1950
    KKIYELAVWD ENKKRPETWE SPEKPKTEAL ELQDVHPELT VTIESKALED 2000
    FEATDLKVEE LTALGNLGDM PVDFCTTRVS PAHRSPTVLC QKVCEENSVS 2050
    PIGCNSSDPA DFEPIPSFSG FPLDSPKTLV LDFETEGERN SPNPRSVRIP 2100
    SPNILKTGLT ENVDRGLGGL EGTHQALDLL AGGMMPEEVK ESSQLDKQES 2150
    LGLELKTINS AGLGPSPCLP DLVDFVTRTS GVQKDKLCSP LSEPGDPSKC 2200
    SSLELGPLQL EISNASTTEV AILQVDDDSG DPLNLVKAPV SRSPPREQVI 2250
    EDNMVPQGMP EQETTVGAIQ DHTESSVHN 2279
    Length:2,279
    Mass (Da):251,112
    Last modified:January 15, 2008 - v2
    Checksum:iCC8F7D54710E2450
    GO
    Isoform 2 (identifier: Q5VUA4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1093-1117: TLDPYNRPWASKTQSEAKQDAIKRT → GQFQKSSDFQKEGLQQTFLPPERQG
         1118-2279: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:1,117
    Mass (Da):124,880
    Checksum:i65866465A953CF07
    GO

    Sequence cautioni

    The sequence AAH98434.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 1214.
    The sequence AAD47387.1 differs from that shown. Reason: Frameshift at positions 4 and 44.
    The sequence AAD17298.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH98434.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti62 – 621G → R in AAD47387. 1 PublicationCurated
    Sequence conflicti75 – 751G → V in AAD47387. 1 PublicationCurated
    Sequence conflicti75 – 751G → V in AAD17298. 1 PublicationCurated
    Sequence conflicti1034 – 10352RT → CI in AAD47387. 1 PublicationCurated
    Sequence conflicti1034 – 10352RT → CI in AAD17298. 1 PublicationCurated
    Sequence conflicti1259 – 12591L → F in AAD47387. 1 PublicationCurated
    Sequence conflicti1259 – 12591L → F in AAD17298. 1 PublicationCurated
    Sequence conflicti1349 – 13491R → G in AAD47387. 1 PublicationCurated
    Sequence conflicti1349 – 13491R → G in AAD17298. 1 PublicationCurated
    Sequence conflicti2160 – 21601S → F in AAD47387. 1 PublicationCurated
    Sequence conflicti2160 – 21601S → F in AAD17298. 1 PublicationCurated
    Sequence conflicti2173 – 21731V → D in BAA34799. (PubMed:9853615)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti407 – 4071S → I.
    Corresponds to variant rs34541323 [ dbSNP | Ensembl ].
    VAR_053759
    Natural varianti812 – 8121N → S in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036056
    Natural varianti870 – 8701L → V.
    Corresponds to variant rs9357410 [ dbSNP | Ensembl ].
    VAR_053760
    Natural varianti1274 – 12741G → R in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036057
    Natural varianti1292 – 12921T → I.
    Corresponds to variant rs10948072 [ dbSNP | Ensembl ].
    VAR_053761
    Natural varianti1580 – 15801A → T.
    Corresponds to variant rs3734684 [ dbSNP | Ensembl ].
    VAR_053762
    Natural varianti1583 – 15831T → I.
    Corresponds to variant rs36107018 [ dbSNP | Ensembl ].
    VAR_053763
    Natural varianti1797 – 17971V → A.1 Publication
    Corresponds to variant rs1459675 [ dbSNP | Ensembl ].
    VAR_053764

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1093 – 111725TLDPY…AIKRT → GQFQKSSDFQKEGLQQTFLP PERQG in isoform 2. 1 PublicationVSP_016592Add
    BLAST
    Alternative sequencei1118 – 22791162Missing in isoform 2. 1 PublicationVSP_016593Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF090114 mRNA. Translation: AAD47387.1. Frameshift.
    AF121141 mRNA. Translation: AAD17298.1. Different initiation.
    AL590383, AL583834 Genomic DNA. Translation: CAH71374.2.
    AL583834, AL590383 Genomic DNA. Translation: CAI14459.2.
    BC030687 mRNA. No translation available.
    BC098434 mRNA. Translation: AAH98434.1. Sequence problems.
    AB015342 mRNA. Translation: BAA34799.1.
    CCDSiCCDS4895.2. [Q5VUA4-1]
    RefSeqiNP_055160.2. NM_014345.2. [Q5VUA4-1]
    UniGeneiHs.509718.

    Genome annotation databases

    EnsembliENST00000361428; ENSP00000354964; ENSG00000171467. [Q5VUA4-1]
    ENST00000605935; ENSP00000475748; ENSG00000171467. [Q5VUA4-2]
    GeneIDi24149.
    KEGGihsa:24149.
    UCSCiuc003oux.3. human. [Q5VUA4-1]

    Polymorphism databases

    DMDMi166215018.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF090114 mRNA. Translation: AAD47387.1 . Frameshift.
    AF121141 mRNA. Translation: AAD17298.1 . Different initiation.
    AL590383 , AL583834 Genomic DNA. Translation: CAH71374.2 .
    AL583834 , AL590383 Genomic DNA. Translation: CAI14459.2 .
    BC030687 mRNA. No translation available.
    BC098434 mRNA. Translation: AAH98434.1 . Sequence problems.
    AB015342 mRNA. Translation: BAA34799.1 .
    CCDSi CCDS4895.2. [Q5VUA4-1 ]
    RefSeqi NP_055160.2. NM_014345.2. [Q5VUA4-1 ]
    UniGenei Hs.509718.

    3D structure databases

    ProteinModelPortali Q5VUA4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117299. 8 interactions.
    IntActi Q5VUA4. 2 interactions.
    STRINGi 9606.ENSP00000354964.

    PTM databases

    PhosphoSitei Q5VUA4.

    Polymorphism databases

    DMDMi 166215018.

    Proteomic databases

    MaxQBi Q5VUA4.
    PaxDbi Q5VUA4.
    PRIDEi Q5VUA4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361428 ; ENSP00000354964 ; ENSG00000171467 . [Q5VUA4-1 ]
    ENST00000605935 ; ENSP00000475748 ; ENSG00000171467 . [Q5VUA4-2 ]
    GeneIDi 24149.
    KEGGi hsa:24149.
    UCSCi uc003oux.3. human. [Q5VUA4-1 ]

    Organism-specific databases

    CTDi 24149.
    GeneCardsi GC06M043346.
    HGNCi HGNC:13578. ZNF318.
    HPAi HPA027022.
    HPA027031.
    neXtProti NX_Q5VUA4.
    PharmGKBi PA134923137.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG87509.
    HOGENOMi HOG000043103.
    HOVERGENi HBG107139.
    InParanoidi Q5VUA4.
    OMAi QTKIRPN.
    OrthoDBi EOG71P298.
    PhylomeDBi Q5VUA4.
    TreeFami TF350583.

    Miscellaneous databases

    ChiTaRSi ZNF318. human.
    GeneWikii ZNF318.
    GenomeRNAii 24149.
    NextBioi 46851.
    PROi Q5VUA4.

    Gene expression databases

    Bgeei Q5VUA4.
    CleanExi HS_ZNF318.
    Genevestigatori Q5VUA4.

    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. "A novel cDNA expressed in endocrine tissue."
      Lopez-Egido J.R., Oberg K., Gobl A.E.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT ALA-1797.
    2. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1213 (ISOFORM 1).
      Tissue: Lymph and Testis.
    4. "Selection system for genes encoding nuclear-targeted proteins."
      Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.
      Nat. Biotechnol. 16:1338-1342(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2056-2279 (ISOFORM 1), SUBCELLULAR LOCATION.
      Tissue: Fetal brain.
    5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-173; SER-214; SER-1896; SER-2189; SER-2192 AND SER-2243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-214 AND SER-1713, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-527; SER-1243; SER-1420; SER-1896; SER-2101 AND SER-2243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-81; SER-136; SER-527; SER-1037; SER-1243 AND SER-2101, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-812 AND ARG-1274.

    Entry informationi

    Entry nameiZN318_HUMAN
    AccessioniPrimary (citable) accession number: Q5VUA4
    Secondary accession number(s): O94796
    , Q4G0E4, Q8NEM6, Q9UNU8, Q9Y2W9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 96 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 6
      Human chromosome 6: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3