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P41230

- KDM5C_MOUSE

UniProt

P41230 - KDM5C_MOUSE

Protein

Lysine-specific demethylase 5C

Gene

Kdm5c

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 4 (26 Jun 2007)
      Previous versions | rss
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    Functioni

    Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Participates in transcriptional repression of neuronal genes by recruiting histone deacetylases and REST at neuron-restrictive silencer elements By similarity.By similarity

    Cofactori

    Alpha-ketoglutarate.By similarity
    Binds 1 Fe2+ ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi514 – 5141Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi517 – 5171Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi602 – 6021Iron; catalyticPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri326 – 37247PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1187 – 124862PHD-type 2PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. histone demethylase activity (H3-K4 specific) Source: Ensembl
    3. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors Source: InterPro
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysine-specific demethylase 5C (EC:1.14.11.-)
    Alternative name(s):
    Histone demethylase JARID1C
    Jumonji/ARID domain-containing protein 1C
    Protein SmcX
    Protein Xe169
    Gene namesi
    Name:Kdm5c
    Synonyms:Jarid1c, Kiaa0234, Smcx, Xe169
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:99781. Kdm5c.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15541554Lysine-specific demethylase 5CPRO_0000200587Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei317 – 3171PhosphoserineBy similarity
    Modified residuei1353 – 13531PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP41230.
    PaxDbiP41230.
    PRIDEiP41230.

    PTM databases

    PhosphoSiteiP41230.

    Expressioni

    Gene expression databases

    ArrayExpressiP41230.
    BgeeiP41230.
    GenevestigatoriP41230.

    Interactioni

    Subunit structurei

    Part of two distinct complexes, one containing E2F6, and the other containing REST.By similarity

    Protein-protein interaction databases

    BioGridi203341. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP41230.
    SMRiP41230. Positions 13-188, 261-616, 1187-1254.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 5542JmjNPROSITE-ProRule annotationAdd
    BLAST
    Domaini79 – 16991ARIDPROSITE-ProRule annotationAdd
    BLAST
    Domaini468 – 634167JmjCPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The first PHD-type zinc finger domain recognizes and binds H3-K9Me3.By similarity
    Both the JmjC domain and the JmjN domain are required for enzymatic activity.By similarity

    Sequence similaritiesi

    Belongs to the JARID1 histone demethylase family.Curated
    Contains 1 ARID domain.PROSITE-ProRule annotation
    Contains 1 JmjC domain.PROSITE-ProRule annotation
    Contains 1 JmjN domain.PROSITE-ProRule annotation
    Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri326 – 37247PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1187 – 124862PHD-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG327026.
    GeneTreeiENSGT00530000063118.
    InParanoidiP41230.
    KOiK11446.
    OMAiTTSICVC.
    OrthoDBiEOG7D85VK.
    PhylomeDBiP41230.
    TreeFamiTF106476.

    Family and domain databases

    Gene3Di1.10.150.60. 1 hit.
    3.30.40.10. 2 hits.
    InterProiIPR001606. ARID/BRIGHT_DNA-bd.
    IPR003347. JmjC_dom.
    IPR013637. Lys_sp_deMease_like_dom.
    IPR003349. TF_JmjN.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR004198. Znf_C5HC2.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF01388. ARID. 1 hit.
    PF02373. JmjC. 1 hit.
    PF02375. JmjN. 1 hit.
    PF00628. PHD. 1 hit.
    PF08429. PLU-1. 1 hit.
    PF02928. zf-C5HC2. 1 hit.
    [Graphical view]
    SMARTiSM00501. BRIGHT. 1 hit.
    SM00558. JmjC. 1 hit.
    SM00545. JmjN. 1 hit.
    SM00249. PHD. 2 hits.
    [Graphical view]
    SUPFAMiSSF46774. SSF46774. 1 hit.
    SSF57903. SSF57903. 2 hits.
    PROSITEiPS51011. ARID. 1 hit.
    PS51184. JMJC. 1 hit.
    PS51183. JMJN. 1 hit.
    PS01359. ZF_PHD_1. 2 hits.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P41230-1) [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

    MELGSDDFLP PPECPVFEPS WAEFRDPLGY IAKIRPIAEK SGICKIRPPA     50
    DWQPPFAVEV DNFRFTPRIQ RLNELEAQTR VKLNYLDQIA KFWEIQGSSL 100
    KIPNVERRIL DLYSLSKIVV EEGGYETICK DRRWARVAQR LNYPPGKNIG 150
    SLLRSHYERI VYPYEMYQSG ANLVQCNTRP FDNEEKDKEY KPHSIPLRQS 200
    VQPSKFNSYG RRAKRLQPDP EPTEEDIEKN PELKKLQIYG AGPKMMGLGL 250
    MAKDKTLRKK DKEGPECPPT VVVKEELGGD VKMESTSPKT FLEGKEELSH 300
    SPEPCTKMTM RLRRNHSNAQ FIESYVCRMC SRGDEDDKLL LCDGCDDNYH 350
    IFCLLPPLPE IPKGVWRCPK CVMAECKRPP EAFGFEQATR EYTLQSFGEM 400
    ADSFKADYFN MPVHMVPTEL VEKEFWRLVN SIEEDVTVEY GADIHSKEFG 450
    SGFPVSDSKR HLTPEEEEYA TSGWNLNVMP VLEQSVLCHI NADISGMKVP 500
    WLYVGMVFSA FCWHIEDHWS YSINYLHWGE PKTWYGVPSL AAEHLEEVMK 550
    KLTPELFDSQ PDLLHQLVTL MNPNTLMSHG VPVVRTNQCA GEFVITFPRA 600
    YHSGFNQGYN FAEAVNFCTA DWLPAGRQCI EHYRRLRRYC VFSHEELICK 650
    MAACPEKLDL NLAAAVHKEM FIMVQEERRL RKALLEKGIT EAEREAFELL 700
    PDDERQCIKC KTTCFLSALA CYDCPDGLVC LSHINDLCKC SSSRQYLRYR 750
    YTLDELPAML HKLKVRAESF DTWANKVRVA LEVEDGRKRS LEELRALESE 800
    ARERRFPNSE LLQRLKNCLS EAEACVSRAL GLVSGQEAGP DRVAGLQMTL 850
    AELRDFLGQM NNLPCAMHQI GDVKGILEQV EAYQTEAREA LVSQPSSPGL 900
    LQSLLERGQQ LGVEVPEAQQ LQRQVEQARW LDEVKRTLAP SARRGTLAIM 950
    RGLLVAGASV APSPAVDKAQ AELQELLTIA ERWEEKAHLC LEARQKHPPA 1000
    TLEAIIHEAE NIPVHLPNIQ SLKEALAKAR AWIADVDEIQ NGDHYPCLDD 1050
    LEGLVAVGRD LPVGLEELRQ LELQVLTAHS WREKASKTFL KKNSCYTLLE 1100
    VLCPCADAGS DSTKRSRWME KELGLYKSDT ELLGLSAQDL RDPGSVIVAF 1150
    KEGEQKEKEG ILQLRRTNSA KPSPLALLTT ASSTASICVC GQVPAGVGAL 1200
    QCDLCQDWFH GRCVTVPRLL SSQRSSLPSS PLLAWWEWDT KFLCPLCMRS 1250
    RRPRLETILA LLVALQRLPV RLPEGEALQC LTERAISWQG RARQVLASEE 1300
    VTALLGRLAE LRQRLQAESK PEESLAYPSD GGEGTGNMPK VQGLLENGDS 1350
    VTSPEKVATE EGSGKRDLEL LSSILPQLSG PVLELPEATR APLEELMMEG 1400
    DLLEVTLDEN HSIWQLLQAG QPPDLKRVQT LLELEKAERH GSRTRGRALE 1450
    RRRRRKVDRG GEPDDPAREE LEPKRVRSSG PEAEEVQEEE ELEEETGGEV 1500
    PPVPFPNSGS PSIQEDQDGL EPVLEAGSDT SAPFSTLTSR LLMSCPQQPS 1550
    LQQL 1554
    Length:1,554
    Mass (Da):175,313
    Last modified:June 26, 2007 - v4
    Checksum:i585EA9F890B0D9A0
    GO
    Isoform 2 (identifier: P41230-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1364-1366: Missing.

    Show »
    Length:1,551
    Mass (Da):174,972
    Checksum:iC2061676EA2DC238
    GO
    Isoform 3 (identifier: P41230-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         77-117: Missing.
         1364-1366: Missing.

    Show »
    Length:1,510
    Mass (Da):170,154
    Checksum:iBAA3698F0A0A1E24
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31L → M in AAB96762. (PubMed:9723615)Curated
    Sequence conflicti26 – 261D → G in AAB96762. (PubMed:9723615)Curated
    Sequence conflicti123 – 1231G → S in BAE33161. (PubMed:16141072)Curated
    Sequence conflicti123 – 1231G → S in BAE33260. (PubMed:16141072)Curated
    Sequence conflicti249 – 2491G → D in BAE34464. (PubMed:16141072)Curated
    Sequence conflicti726 – 7261D → N in BAC97906. (PubMed:14621295)Curated
    Sequence conflicti865 – 8651C → L in AAD53049. (PubMed:10441747)Curated
    Sequence conflicti865 – 8651C → L in CAA82759. (PubMed:7951230)Curated
    Sequence conflicti1068 – 10681L → P in CAA82759. (PubMed:7951230)Curated
    Sequence conflicti1126 – 11261Y → C in BAE33367. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei77 – 11741Missing in isoform 3. 1 PublicationVSP_026411Add
    BLAST
    Alternative sequencei1364 – 13663Missing in isoform 2 and isoform 3. 3 PublicationsVSP_000316

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF127245 mRNA. Translation: AAD53049.1.
    AK008105 mRNA. Translation: BAB25462.1.
    AK155279 mRNA. Translation: BAE33161.1.
    AK155427 mRNA. Translation: BAE33260.1.
    AK155651 mRNA. Translation: BAE33367.1.
    AK158340 mRNA. Translation: BAE34464.1.
    AK011577 mRNA. No translation available.
    BC043096 mRNA. Translation: AAH43096.1.
    BC054550 mRNA. Translation: AAH54550.1.
    Z29651 mRNA. Translation: CAA82759.1.
    AK129096 mRNA. Translation: BAC97906.1.
    L29563 mRNA. Translation: AAA62384.1.
    AF039894 mRNA. Translation: AAB96762.1.
    CCDSiCCDS41178.1. [P41230-2]
    PIRiI48775.
    I84689.
    RefSeqiNP_038696.2. NM_013668.4. [P41230-2]
    XP_006528832.1. XM_006528769.1. [P41230-1]
    XP_006528835.1. XM_006528772.1. [P41230-3]
    UniGeneiMm.142655.
    Mm.482277.

    Genome annotation databases

    EnsembliENSMUST00000082177; ENSMUSP00000080814; ENSMUSG00000025332. [P41230-3]
    ENSMUST00000112584; ENSMUSP00000108203; ENSMUSG00000025332. [P41230-1]
    ENSMUST00000112588; ENSMUSP00000108207; ENSMUSG00000025332. [P41230-2]
    GeneIDi20591.
    KEGGimmu:20591.
    UCSCiuc009uqc.2. mouse. [P41230-2]
    uc009uqd.2. mouse. [P41230-3]
    uc009uqe.2. mouse. [P41230-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF127245 mRNA. Translation: AAD53049.1 .
    AK008105 mRNA. Translation: BAB25462.1 .
    AK155279 mRNA. Translation: BAE33161.1 .
    AK155427 mRNA. Translation: BAE33260.1 .
    AK155651 mRNA. Translation: BAE33367.1 .
    AK158340 mRNA. Translation: BAE34464.1 .
    AK011577 mRNA. No translation available.
    BC043096 mRNA. Translation: AAH43096.1 .
    BC054550 mRNA. Translation: AAH54550.1 .
    Z29651 mRNA. Translation: CAA82759.1 .
    AK129096 mRNA. Translation: BAC97906.1 .
    L29563 mRNA. Translation: AAA62384.1 .
    AF039894 mRNA. Translation: AAB96762.1 .
    CCDSi CCDS41178.1. [P41230-2 ]
    PIRi I48775.
    I84689.
    RefSeqi NP_038696.2. NM_013668.4. [P41230-2 ]
    XP_006528832.1. XM_006528769.1. [P41230-1 ]
    XP_006528835.1. XM_006528772.1. [P41230-3 ]
    UniGenei Mm.142655.
    Mm.482277.

    3D structure databases

    ProteinModelPortali P41230.
    SMRi P41230. Positions 13-188, 261-616, 1187-1254.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203341. 2 interactions.

    PTM databases

    PhosphoSitei P41230.

    Proteomic databases

    MaxQBi P41230.
    PaxDbi P41230.
    PRIDEi P41230.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000082177 ; ENSMUSP00000080814 ; ENSMUSG00000025332 . [P41230-3 ]
    ENSMUST00000112584 ; ENSMUSP00000108203 ; ENSMUSG00000025332 . [P41230-1 ]
    ENSMUST00000112588 ; ENSMUSP00000108207 ; ENSMUSG00000025332 . [P41230-2 ]
    GeneIDi 20591.
    KEGGi mmu:20591.
    UCSCi uc009uqc.2. mouse. [P41230-2 ]
    uc009uqd.2. mouse. [P41230-3 ]
    uc009uqe.2. mouse. [P41230-1 ]

    Organism-specific databases

    CTDi 8242.
    MGIi MGI:99781. Kdm5c.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG327026.
    GeneTreei ENSGT00530000063118.
    InParanoidi P41230.
    KOi K11446.
    OMAi TTSICVC.
    OrthoDBi EOG7D85VK.
    PhylomeDBi P41230.
    TreeFami TF106476.

    Miscellaneous databases

    ChiTaRSi KDM5C. mouse.
    NextBioi 298901.
    PROi P41230.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P41230.
    Bgeei P41230.
    Genevestigatori P41230.

    Family and domain databases

    Gene3Di 1.10.150.60. 1 hit.
    3.30.40.10. 2 hits.
    InterProi IPR001606. ARID/BRIGHT_DNA-bd.
    IPR003347. JmjC_dom.
    IPR013637. Lys_sp_deMease_like_dom.
    IPR003349. TF_JmjN.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR004198. Znf_C5HC2.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF01388. ARID. 1 hit.
    PF02373. JmjC. 1 hit.
    PF02375. JmjN. 1 hit.
    PF00628. PHD. 1 hit.
    PF08429. PLU-1. 1 hit.
    PF02928. zf-C5HC2. 1 hit.
    [Graphical view ]
    SMARTi SM00501. BRIGHT. 1 hit.
    SM00558. JmjC. 1 hit.
    SM00545. JmjN. 1 hit.
    SM00249. PHD. 2 hits.
    [Graphical view ]
    SUPFAMi SSF46774. SSF46774. 1 hit.
    SSF57903. SSF57903. 2 hits.
    PROSITEi PS51011. ARID. 1 hit.
    PS51184. JMJC. 1 hit.
    PS51183. JMJN. 1 hit.
    PS01359. ZF_PHD_1. 2 hits.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mouse H-Y encoding Smcy gene and its X chromosomal homolog Smcx."
      Agulnik A.I., Longepied G., Ty M.T., Bishop C.E., Mitchell M.J.
      Mamm. Genome 10:926-929(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: 129/SvJ.
    2. "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] (ISOFORM 2).
      Strain: C57BL/6J and NOD.
      Tissue: Dendritic cell, Embryo, Inner ear and Small intestine.
    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 3).
      Strain: C57BL/6.
      Tissue: Brain.
    4. "A novel X gene with a widely transcribed Y-linked homologue escapes X-inactivation in mouse and human."
      Agulnik A.I., Mitchell M.J., Mattei M.-G., Borsani G., Avner P.A., Lerner J.L., Bishop C.E.
      Hum. Mol. Genet. 3:879-884(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 36-1068.
      Strain: BALB/c.
      Tissue: Testis.
    5. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
      DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-1554 (ISOFORM 1).
      Tissue: Embryonic tail.
    6. "The murine Xe169 gene escapes X-inactivation like its human homologue."
      Wu J., Salido E., Yen P., Mohandas T., Shapiro L.J.
      Nat. Genet. 7:491-496(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1206-1385 (ISOFORM 1).
    7. "A proposed path by which genes common to mammalian X and Y chromosomes evolve to become X inactivated."
      Jegalian K.G., Page D.C.
      Nature 394:776-780(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-39.
    8. "Identification of a mouse male-specific transplantation antigen, H-Y."
      Scott D.M., Ehrmann I.E., Ellis P.S., Bishop C.E., Agulnik A.I., Simpson E., Mitchell M.J.
      Nature 376:695-698(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: C3H.

    Entry informationi

    Entry nameiKDM5C_MOUSE
    AccessioniPrimary (citable) accession number: P41230
    Secondary accession number(s): O54995
    , Q3TYU8, Q3U1X6, Q3U282, Q6ZQF8, Q80XQ9, Q9CVI4, Q9D0C3, Q9QVR8, Q9R039
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 128 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Escapes X-inactivation.

    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