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Protein

Lysine-specific demethylase 5C

Gene

KDM5C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code (PubMed:28262558). 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. Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2 (By similarity).By similarity5 Publications

Miscellaneous

Escapes X-inactivation.

Cofactori

Fe2+1 PublicationNote: Binds 1 Fe2+ ion per subunit.1 Publication

Enzyme regulationi

The inhibitor KDOAM-25 and others inhibit its demethylase activity, resulting to cell cycle arrest in myeloma cells.1 Publication

Kineticsi

Kcat are 1.92 min(-1) and 2.71 min(-1) for 2-oxoglutarate and histone H3K4me3, respectively.1 Publication
  1. KM=6 µM for 2-oxoglutarate1 Publication
  2. KM=3.3 µM for histone H3K4me31 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei4402-oxoglutarateBy similarity1
    Metal bindingi514Iron; catalytic1 Publication1
    Metal bindingi516Iron; catalytic1 Publication1
    Binding sitei5222-oxoglutarateBy similarity1
    Binding sitei5242-oxoglutarateBy similarity1
    Binding sitei5322-oxoglutarateBy similarity1
    Metal bindingi602Iron; catalytic1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Zinc fingeri326 – 372PHD-type 1PROSITE-ProRule annotationAdd BLAST47
    Zinc fingeri707 – 759C5HC21 PublicationAdd BLAST53
    Zinc fingeri1187 – 1248PHD-type 2PROSITE-ProRule annotationAdd BLAST62

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionChromatin regulator, Dioxygenase, Oxidoreductase, Repressor
    Biological processBiological rhythms, Transcription, Transcription regulation
    LigandIron, Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi1.14.11.B2. 2681.
    ReactomeiR-HSA-3214842. HDMs demethylate histones.

    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 1C1 Publication
    Protein SmcX1 Publication
    Protein Xe169
    Gene namesi
    Name:KDM5CImported
    Synonyms:DXS1272E, JARID1C1 Publication, SMCX1 Publication, XE169
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome X

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000126012.11.
    HGNCiHGNC:11114. KDM5C.

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, X-linked, syndromic, Claes-Jensen type (MRXSCJ)7 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXSCJ patients manifest mental retardation associated with variable features such as slowly progressive spastic paraplegia, seizures, facial dysmorphism.
    See also OMIM:300534
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_03298687D → G in MRXSCJ; no effect on subcellular location and enzymatic activity. 2 Publications1
    Natural variantiVAR_022730388A → P in MRXSCJ; impairs enzymatic activity and binding to H3-K9Me3. 2 PublicationsCorresponds to variant dbSNP:rs199422235Ensembl.1
    Natural variantiVAR_022731402D → Y in MRXSCJ; decreases enzymatic activity. 3 Publications1
    Natural variantiVAR_032987451S → R in MRXSCJ. 1 PublicationCorresponds to variant dbSNP:rs199422237Ensembl.1
    Natural variantiVAR_074308480P → L in MRXSCJ; patient fibroblasts show decreased enzymatic activity. 2 Publications1
    Natural variantiVAR_032988642F → L in MRXSCJ; impairs enzymatic activity. 2 Publications1
    Natural variantiVAR_022732698E → K in MRXSCJ. 1 Publication1
    Natural variantiVAR_022733731L → F in MRXSCJ; impairs enzymatic activity. 2 PublicationsCorresponds to variant dbSNP:rs199422234Ensembl.1
    Natural variantiVAR_032989750R → W in MRXSCJ. 1 Publication1
    Natural variantiVAR_032990751Y → C in MRXSCJ; impairs enzymatic activity. 3 Publications1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi514 – 516HIE → AIA: Abolishes lysine-specific histone demethylase activity. 1 Publication3
    Mutagenesisi514H → A: Abolishes lysine-specific histone demethylase activity. 2 Publications1

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    DisGeNETi8242.
    MalaCardsiKDM5C.
    MIMi300534. phenotype.
    OpenTargetsiENSG00000126012.
    Orphaneti85279. Syndromic X-linked intellectual disability due to JARID1C mutation.
    PharmGKBiPA35964.

    Chemistry databases

    ChEMBLiCHEMBL2163176.
    GuidetoPHARMACOLOGYi2682.

    Polymorphism and mutation databases

    BioMutaiKDM5C.
    DMDMi117949812.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002005861 – 1560Lysine-specific demethylase 5CAdd BLAST1560

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Cross-linki205Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Cross-linki229Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Cross-linki244Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Cross-linki274Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Modified residuei287PhosphoserineCombined sources1
    Cross-linki295Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Modified residuei301PhosphoserineCombined sources1
    Modified residuei317PhosphoserineCombined sources1
    Modified residuei893PhosphoserineBy similarity1
    Modified residuei897PhosphoserineCombined sources1
    Cross-linki1127Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Modified residuei1359PhosphoserineCombined sources1

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    EPDiP41229.
    MaxQBiP41229.
    PaxDbiP41229.
    PeptideAtlasiP41229.
    PRIDEiP41229.

    PTM databases

    iPTMnetiP41229.
    PhosphoSitePlusiP41229.

    Expressioni

    Tissue specificityi

    Expressed in all tissues examined. Highest levels found in brain and skeletal muscle.1 Publication

    Gene expression databases

    BgeeiENSG00000126012.
    CleanExiHS_JARID1C.
    ExpressionAtlasiP41229. baseline and differential.
    GenevisibleiP41229. HS.

    Organism-specific databases

    HPAiHPA038244.
    HPA046147.

    Interactioni

    Subunit structurei

    Part of two distinct complexes, one containing E2F6, and the other containing REST.1 Publication

    Protein-protein interaction databases

    BioGridi113870. 66 interactors.
    DIPiDIP-39663N.
    IntActiP41229. 21 interactors.
    STRINGi9606.ENSP00000364550.

    Chemistry databases

    BindingDBiP41229.

    Structurei

    Secondary structure

    11560
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi21 – 24Combined sources4
    Helixi27 – 38Combined sources12
    Turni39 – 41Combined sources3
    Beta strandi42 – 46Combined sources5
    Helixi60 – 62Combined sources3
    Beta strandi68 – 71Combined sources4
    Helixi73 – 76Combined sources4
    Turni79 – 81Combined sources3
    Helixi82 – 94Combined sources13
    Turni95 – 97Combined sources3
    Helixi112 – 122Combined sources11
    Helixi125 – 130Combined sources6
    Turni131 – 133Combined sources3
    Helixi134 – 140Combined sources7
    Helixi149 – 159Combined sources11
    Helixi162 – 172Combined sources11
    Turni178 – 180Combined sources3
    Helixi181 – 185Combined sources5
    Helixi394 – 409Combined sources16
    Helixi418 – 429Combined sources12
    Beta strandi437 – 445Combined sources9
    Helixi446 – 449Combined sources4
    Helixi464 – 471Combined sources8
    Turni476 – 478Combined sources3
    Helixi479 – 481Combined sources3
    Helixi486 – 489Combined sources4
    Turni495 – 497Combined sources3
    Beta strandi501 – 505Combined sources5
    Beta strandi510 – 514Combined sources5
    Helixi517 – 519Combined sources3
    Beta strandi521 – 530Combined sources10
    Beta strandi532 – 536Combined sources5
    Helixi539 – 541Combined sources3
    Helixi542 – 552Combined sources11
    Helixi573 – 577Combined sources5
    Turni578 – 580Combined sources3
    Beta strandi584 – 588Combined sources5
    Beta strandi593 – 596Combined sources4
    Beta strandi602 – 617Combined sources16
    Helixi620 – 622Combined sources3
    Helixi623 – 636Combined sources14
    Helixi644 – 652Combined sources9
    Helixi655 – 657Combined sources3
    Helixi660 – 687Combined sources28
    Beta strandi692 – 694Combined sources3
    Helixi697 – 699Combined sources3
    Helixi702 – 704Combined sources3
    Turni708 – 710Combined sources3
    Beta strandi716 – 723Combined sources8
    Helixi731 – 733Combined sources3
    Helixi742 – 744Combined sources3
    Beta strandi745 – 751Combined sources7
    Helixi755 – 767Combined sources13

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2JRZNMR-A73-188[»]
    5FWJX-ray2.10A/B8-83[»]
    A/B384-772[»]
    ProteinModelPortaliP41229.
    SMRiP41229.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP41229.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini14 – 55JmjNPROSITE-ProRule annotationAdd BLAST42
    Domaini79 – 169ARIDPROSITE-ProRule annotationAdd BLAST91
    Domaini468 – 634JmjCPROSITE-ProRule annotationAdd BLAST167

    Domaini

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

    Sequence similaritiesi

    Belongs to the JARID1 histone demethylase family.Curated

    Zinc finger

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Zinc fingeri326 – 372PHD-type 1PROSITE-ProRule annotationAdd BLAST47
    Zinc fingeri707 – 759C5HC21 PublicationAdd BLAST53
    Zinc fingeri1187 – 1248PHD-type 2PROSITE-ProRule annotationAdd BLAST62

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiKOG1246. Eukaryota.
    ENOG410XR9J. LUCA.
    GeneTreeiENSGT00530000063118.
    HOGENOMiHOG000290719.
    InParanoidiP41229.
    KOiK11446.
    OMAiHLCLEAR.
    OrthoDBiEOG091G0RFR.
    PhylomeDBiP41229.
    TreeFamiTF106476.

    Family and domain databases

    Gene3Di3.30.40.10. 2 hits.
    InterProiView protein in InterPro
    IPR001606. ARID_dom.
    IPR003347. JmjC_dom.
    IPR003349. JmjN.
    IPR013637. Lys_sp_deMease-like_dom.
    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.
    PfamiView protein in Pfam
    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.
    SMARTiView protein in SMART
    SM00501. BRIGHT. 1 hit.
    SM00558. JmjC. 1 hit.
    SM00545. JmjN. 1 hit.
    SM00249. PHD. 2 hits.
    SUPFAMiSSF46774. SSF46774. 1 hit.
    SSF57903. SSF57903. 2 hits.
    PROSITEiView protein in PROSITE
    PS51011. ARID. 1 hit.
    PS51184. JMJC. 1 hit.
    PS51183. JMJN. 1 hit.
    PS01359. ZF_PHD_1. 2 hits.
    PS50016. ZF_PHD_2. 1 hit.

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P41229-1) [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

            10         20         30         40         50
    MEPGSDDFLP PPECPVFEPS WAEFRDPLGY IAKIRPIAEK SGICKIRPPA
    60 70 80 90 100
    DWQPPFAVEV DNFRFTPRIQ RLNELEAQTR VKLNYLDQIA KFWEIQGSSL
    110 120 130 140 150
    KIPNVERRIL DLYSLSKIVV EEGGYEAICK DRRWARVAQR LNYPPGKNIG
    160 170 180 190 200
    SLLRSHYERI VYPYEMYQSG ANLVQCNTRP FDNEEKDKEY KPHSIPLRQS
    210 220 230 240 250
    VQPSKFNSYG RRAKRLQPDP EPTEEDIEKN PELKKLQIYG AGPKMMGLGL
    260 270 280 290 300
    MAKDKTLRKK DKEGPECPPT VVVKEELGGD VKVESTSPKT FLESKEELSH
    310 320 330 340 350
    SPEPCTKMTM RLRRNHSNAQ FIESYVCRMC SRGDEDDKLL LCDGCDDNYH
    360 370 380 390 400
    IFCLLPPLPE IPKGVWRCPK CVMAECKRPP EAFGFEQATR EYTLQSFGEM
    410 420 430 440 450
    ADSFKADYFN MPVHMVPTEL VEKEFWRLVN SIEEDVTVEY GADIHSKEFG
    460 470 480 490 500
    SGFPVSDSKR HLTPEEEEYA TSGWNLNVMP VLEQSVLCHI NADISGMKVP
    510 520 530 540 550
    WLYVGMVFSA FCWHIEDHWS YSINYLHWGE PKTWYGVPSL AAEHLEEVMK
    560 570 580 590 600
    KLTPELFDSQ PDLLHQLVTL MNPNTLMSHG VPVVRTNQCA GEFVITFPRA
    610 620 630 640 650
    YHSGFNQGYN FAEAVNFCTA DWLPAGRQCI EHYRRLRRYC VFSHEELICK
    660 670 680 690 700
    MAACPEKLDL NLAAAVHKEM FIMVQEERRL RKALLEKGIT EAEREAFELL
    710 720 730 740 750
    PDDERQCIKC KTTCFLSALA CYDCPDGLVC LSHINDLCKC SSSRQYLRYR
    760 770 780 790 800
    YTLDELPAML HKLKVRAESF DTWANKVRVA LEVEDGRKRS LEELRALESE
    810 820 830 840 850
    ARERRFPNSE LLQQLKNCLS EAEACVSRAL GLVSGQEAGP HRVAGLQMTL
    860 870 880 890 900
    TELRAFLDQM NNLPCAMHQI GDVKGVLEQV EAYQAEAREA LASLPSSPGL
    910 920 930 940 950
    LQSLLERGRQ LGVEVPEAQQ LQRQVEQARW LDEVKRTLAP SARRGTLAVM
    960 970 980 990 1000
    RGLLVAGASV APSPAVDKAQ AELQELLTIA ERWEEKAHLC LEARQKHPPA
    1010 1020 1030 1040 1050
    TLEAIIREAE NIPVHLPNIQ ALKEALAKAR AWIADVDEIQ NGDHYPCLDD
    1060 1070 1080 1090 1100
    LEGLVAVGRD LPVGLEELRQ LELQVLTAHS WREKASKTFL KKNSCYTLLE
    1110 1120 1130 1140 1150
    VLCPCADAGS DSTKRSRWME KELGLYKSDT ELLGLSAQDL RDPGSVIVAF
    1160 1170 1180 1190 1200
    KEGEQKEKEG ILQLRRTNSA KPSPLASSST ASSTTSICVC GQVLAGAGAL
    1210 1220 1230 1240 1250
    QCDLCQDWFH GRCVSVPRLL SSPRPNPTSS PLLAWWEWDT KFLCPLCMRS
    1260 1270 1280 1290 1300
    RRPRLETILA LLVALQRLPV RLPEGEALQC LTERAISWQG RARQALASED
    1310 1320 1330 1340 1350
    VTALLGRLAE LRQRLQAEPR PEEPPNYPAA PASDPLREGS GKDMPKVQGL
    1360 1370 1380 1390 1400
    LENGDSVTSP EKVAPEEGSG KRDLELLSSL LPQLTGPVLE LPEATRAPLE
    1410 1420 1430 1440 1450
    ELMMEGDLLE VTLDENHSIW QLLQAGQPPD LERIRTLLEL EKAERHGSRA
    1460 1470 1480 1490 1500
    RGRALERRRR RKVDRGGEGD DPAREELEPK RVRSSGPEAE EVQEEEELEE
    1510 1520 1530 1540 1550
    ETGGEGPPAP IPTTGSPSTQ ENQNGLEPAE GTTSGPSAPF STLTPRLHLP
    1560
    CPQQPPQQQL
    Length:1,560
    Mass (Da):175,720
    Last modified:November 14, 2006 - v2
    Checksum:i5DC673D0091E7C87
    GO
    Isoform 2 (identifier: P41229-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1370-1372: Missing.

    Show »
    Length:1,557
    Mass (Da):175,379
    Checksum:iB1823D7AD5F78374
    GO
    Isoform 3 (identifier: P41229-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         77-117: Missing.
         1370-1372: Missing.

    Show »
    Length:1,516
    Mass (Da):170,561
    Checksum:iF82BDA8A82C57C01
    GO
    Isoform 4 (identifier: P41229-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         51-76: Missing.
         77-117: Missing.
         1370-1372: Missing.
         1420-1560: WQLLQAGQPP...CPQQPPQQQL → PESLDFCILTPRYCSDLSSWGPAPGVFPPW

    Note: No experimental confirmation available.
    Show »
    Length:1,379
    Mass (Da):155,119
    Checksum:i20A82456B8CF788E
    GO
    Isoform 5 (identifier: P41229-5) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         175-175: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:1,559
    Mass (Da):175,592
    Checksum:iCC245E4B78A1F039
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti16V → L in BAG65494 (PubMed:14702039).Curated1
    Sequence conflicti23E → G in BAG65494 (PubMed:14702039).Curated1
    Sequence conflicti342C → Y in CAA82758 (PubMed:7951230).Curated1
    Sequence conflicti1199A → R in AAA61302 (PubMed:8162017).Curated1
    Sequence conflicti1419I → T in BAG65494 (PubMed:14702039).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_03298687D → G in MRXSCJ; no effect on subcellular location and enzymatic activity. 2 Publications1
    Natural variantiVAR_022730388A → P in MRXSCJ; impairs enzymatic activity and binding to H3-K9Me3. 2 PublicationsCorresponds to variant dbSNP:rs199422235Ensembl.1
    Natural variantiVAR_022731402D → Y in MRXSCJ; decreases enzymatic activity. 3 Publications1
    Natural variantiVAR_032987451S → R in MRXSCJ. 1 PublicationCorresponds to variant dbSNP:rs199422237Ensembl.1
    Natural variantiVAR_074308480P → L in MRXSCJ; patient fibroblasts show decreased enzymatic activity. 2 Publications1
    Natural variantiVAR_065091640C → Y De novo mutation found in a patient with mental retardation. 1 Publication1
    Natural variantiVAR_032988642F → L in MRXSCJ; impairs enzymatic activity. 2 Publications1
    Natural variantiVAR_022732698E → K in MRXSCJ. 1 Publication1
    Natural variantiVAR_022733731L → F in MRXSCJ; impairs enzymatic activity. 2 PublicationsCorresponds to variant dbSNP:rs199422234Ensembl.1
    Natural variantiVAR_032989750R → W in MRXSCJ. 1 Publication1
    Natural variantiVAR_032990751Y → C in MRXSCJ; impairs enzymatic activity. 3 Publications1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_04375251 – 76Missing in isoform 4. 1 PublicationAdd BLAST26
    Alternative sequenceiVSP_02641077 – 117Missing in isoform 3 and isoform 4. 1 PublicationAdd BLAST41
    Alternative sequenceiVSP_053420175Missing in isoform 5. 1 Publication1
    Alternative sequenceiVSP_0003151370 – 1372Missing in isoform 2, isoform 3 and isoform 4. 1 Publication3
    Alternative sequenceiVSP_0437531420 – 1560WQLLQ…PQQQL → PESLDFCILTPRYCSDLSSW GPAPGVFPPW in isoform 4. 1 PublicationAdd BLAST141

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L25270 mRNA. Translation: AAA61302.1.
    AK304732 mRNA. Translation: BAG65494.1.
    AL139396 Genomic DNA. Translation: CAI39836.1.
    AL139396 Genomic DNA. Translation: CAI39837.1.
    AL139396 Genomic DNA. Translation: CAI39838.1.
    CH471154 Genomic DNA. Translation: EAW93145.1.
    BC054499 mRNA. Translation: AAH54499.1.
    Z29650 mRNA. Translation: CAA82758.1.
    CCDSiCCDS14351.1. [P41229-1]
    CCDS55417.1. [P41229-4]
    CCDS65269.1. [P41229-5]
    PIRiI54361.
    RefSeqiNP_001140174.1. NM_001146702.1. [P41229-4]
    NP_001269551.1. NM_001282622.1. [P41229-5]
    NP_004178.2. NM_004187.3. [P41229-1]
    XP_005262092.1. XM_005262035.4. [P41229-2]
    XP_011529128.1. XM_011530826.2. [P41229-3]
    UniGeneiHs.631768.

    Genome annotation databases

    EnsembliENST00000375379; ENSP00000364528; ENSG00000126012. [P41229-2]
    ENST00000375383; ENSP00000364532; ENSG00000126012. [P41229-3]
    ENST00000375401; ENSP00000364550; ENSG00000126012. [P41229-1]
    ENST00000404049; ENSP00000385394; ENSG00000126012. [P41229-5]
    ENST00000452825; ENSP00000445176; ENSG00000126012. [P41229-4]
    GeneIDi8242.
    KEGGihsa:8242.
    UCSCiuc004drz.4. human. [P41229-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Similar proteinsi

    Entry informationi

    Entry nameiKDM5C_HUMAN
    AccessioniPrimary (citable) accession number: P41229
    Secondary accession number(s): B0QZ44
    , B4E3I2, F5H3T1, Q5JUX3, Q5JUX4, Q5JUX5, Q7Z5S5
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: November 14, 2006
    Last modified: September 27, 2017
    This is version 178 of the entry and version 2 of the sequence. See 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families