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P41229 (KDM5C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:KDM5C
Synonyms:DXS1272E, JARID1C, SMCX, XE169
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1560 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9 Ref.10

Cofactor

Alpha-ketoglutarate. Ref.9

Binds 1 Fe2+ ion per subunit. Ref.9

Subunit structure

Part of two distinct complexes, one containing E2F6, and the other containing REST. Ref.10

Subcellular location

Nucleus Ref.10.

Tissue specificity

Expressed in all tissues examined. Highest levels found in brain and skeletal muscle. Ref.16

Domain

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.

Involvement in disease

Mental retardation, X-linked, syndromic, Claes-Jensen type (MRXSCJ) [MIM:300534]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.16 Ref.17 Ref.18

Miscellaneous

Escapes X-inactivation.

Sequence similarities

Belongs to the JARID1 histone demethylase family.

Contains 1 ARID domain.

Contains 1 JmjC domain.

Contains 1 JmjN domain.

Contains 2 PHD-type zinc fingers.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P41229-1)

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.
Isoform 2 (identifier: P41229-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1370-1372: Missing.
Isoform 3 (identifier: P41229-3)

The sequence of this isoform differs from the canonical sequence as follows:
     77-117: Missing.
     1370-1372: Missing.
Isoform 4 (identifier: P41229-4)

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.
Isoform 5 (identifier: P41229-5)

The sequence of this isoform differs from the canonical sequence as follows:
     175-175: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15601560Lysine-specific demethylase 5C
PRO_0000200586

Regions

Domain14 – 5542JmjN
Domain79 – 16991ARID
Domain468 – 634167JmjC
Zinc finger326 – 37247PHD-type 1
Zinc finger1187 – 124862PHD-type 2

Sites

Metal binding5141Iron; catalytic By similarity
Metal binding5171Iron; catalytic By similarity
Metal binding6021Iron; catalytic By similarity

Amino acid modifications

Modified residue3171Phosphoserine Ref.11
Modified residue13591Phosphoserine Ref.7 Ref.12 Ref.13 Ref.15

Natural variations

Alternative sequence51 – 7626Missing in isoform 4.
VSP_043752
Alternative sequence77 – 11741Missing in isoform 3 and isoform 4.
VSP_026410
Alternative sequence1751Missing in isoform 5.
VSP_053420
Alternative sequence1370 – 13723Missing in isoform 2, isoform 3 and isoform 4.
VSP_000315
Alternative sequence1420 – 1560141WQLLQ…PQQQL → PESLDFCILTPRYCSDLSSW GPAPGVFPPW in isoform 4.
VSP_043753
Natural variant871D → G in MRXSCJ; no effect on subcellular location and enzymatic activity. Ref.10 Ref.18
VAR_032986
Natural variant3881A → P in MRXSCJ; impairs enzymatic activity and binding to H3-K9Me3. Ref.9 Ref.16
VAR_022730
Natural variant4021D → Y in MRXSCJ; impairs enzymatic activity. Ref.10 Ref.16
VAR_022731
Natural variant4511S → R in MRXSCJ. Ref.17
VAR_032987
Natural variant6401C → Y De novo mutation found in a patient with mental retardation. Ref.19
VAR_065091
Natural variant6421F → L in MRXSCJ; impairs enzymatic activity. Ref.9 Ref.18
VAR_032988
Natural variant6981E → K in MRXSCJ; abolishes function in vivo, but no effect on enzymatic activity or binding to H3-K9Me3. Ref.10 Ref.16
VAR_022732
Natural variant7311L → F in MRXSCJ; impairs enzymatic activity. Ref.9 Ref.16
VAR_022733
Natural variant7501R → W in MRXSCJ. Ref.18
VAR_032989
Natural variant7511Y → C in MRXSCJ; impairs enzymatic activity. Ref.9 Ref.10 Ref.18
VAR_032990

Experimental info

Mutagenesis5141H → A: Abolishes enzymatic activity. Ref.9 Ref.10
Sequence conflict161V → L in BAG65494. Ref.2
Sequence conflict231E → G in BAG65494. Ref.2
Sequence conflict3421C → Y in CAA82758. Ref.6
Sequence conflict11991A → R in AAA61302. Ref.1
Sequence conflict14191I → T in BAG65494. Ref.2

Secondary structure

.................... 1560
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 14, 2006. Version 2.
Checksum: 5DC673D0091E7C87

FASTA1,560175,720
        10         20         30         40         50         60 
MEPGSDDFLP PPECPVFEPS WAEFRDPLGY IAKIRPIAEK SGICKIRPPA DWQPPFAVEV 

        70         80         90        100        110        120 
DNFRFTPRIQ RLNELEAQTR VKLNYLDQIA KFWEIQGSSL KIPNVERRIL DLYSLSKIVV 

       130        140        150        160        170        180 
EEGGYEAICK DRRWARVAQR LNYPPGKNIG SLLRSHYERI VYPYEMYQSG ANLVQCNTRP 

       190        200        210        220        230        240 
FDNEEKDKEY KPHSIPLRQS VQPSKFNSYG RRAKRLQPDP EPTEEDIEKN PELKKLQIYG 

       250        260        270        280        290        300 
AGPKMMGLGL MAKDKTLRKK DKEGPECPPT VVVKEELGGD VKVESTSPKT FLESKEELSH 

       310        320        330        340        350        360 
SPEPCTKMTM RLRRNHSNAQ FIESYVCRMC SRGDEDDKLL LCDGCDDNYH IFCLLPPLPE 

       370        380        390        400        410        420 
IPKGVWRCPK CVMAECKRPP EAFGFEQATR EYTLQSFGEM ADSFKADYFN MPVHMVPTEL 

       430        440        450        460        470        480 
VEKEFWRLVN SIEEDVTVEY GADIHSKEFG SGFPVSDSKR HLTPEEEEYA TSGWNLNVMP 

       490        500        510        520        530        540 
VLEQSVLCHI NADISGMKVP WLYVGMVFSA FCWHIEDHWS YSINYLHWGE PKTWYGVPSL 

       550        560        570        580        590        600 
AAEHLEEVMK KLTPELFDSQ PDLLHQLVTL MNPNTLMSHG VPVVRTNQCA GEFVITFPRA 

       610        620        630        640        650        660 
YHSGFNQGYN FAEAVNFCTA DWLPAGRQCI EHYRRLRRYC VFSHEELICK MAACPEKLDL 

       670        680        690        700        710        720 
NLAAAVHKEM FIMVQEERRL RKALLEKGIT EAEREAFELL PDDERQCIKC KTTCFLSALA 

       730        740        750        760        770        780 
CYDCPDGLVC LSHINDLCKC SSSRQYLRYR YTLDELPAML HKLKVRAESF DTWANKVRVA 

       790        800        810        820        830        840 
LEVEDGRKRS LEELRALESE ARERRFPNSE LLQQLKNCLS EAEACVSRAL GLVSGQEAGP 

       850        860        870        880        890        900 
HRVAGLQMTL TELRAFLDQM NNLPCAMHQI GDVKGVLEQV EAYQAEAREA LASLPSSPGL 

       910        920        930        940        950        960 
LQSLLERGRQ LGVEVPEAQQ LQRQVEQARW LDEVKRTLAP SARRGTLAVM RGLLVAGASV 

       970        980        990       1000       1010       1020 
APSPAVDKAQ AELQELLTIA ERWEEKAHLC LEARQKHPPA TLEAIIREAE NIPVHLPNIQ 

      1030       1040       1050       1060       1070       1080 
ALKEALAKAR AWIADVDEIQ NGDHYPCLDD LEGLVAVGRD LPVGLEELRQ LELQVLTAHS 

      1090       1100       1110       1120       1130       1140 
WREKASKTFL KKNSCYTLLE VLCPCADAGS DSTKRSRWME KELGLYKSDT ELLGLSAQDL 

      1150       1160       1170       1180       1190       1200 
RDPGSVIVAF KEGEQKEKEG ILQLRRTNSA KPSPLASSST ASSTTSICVC GQVLAGAGAL 

      1210       1220       1230       1240       1250       1260 
QCDLCQDWFH GRCVSVPRLL SSPRPNPTSS PLLAWWEWDT KFLCPLCMRS RRPRLETILA 

      1270       1280       1290       1300       1310       1320 
LLVALQRLPV RLPEGEALQC LTERAISWQG RARQALASED VTALLGRLAE LRQRLQAEPR 

      1330       1340       1350       1360       1370       1380 
PEEPPNYPAA PASDPLREGS GKDMPKVQGL LENGDSVTSP EKVAPEEGSG KRDLELLSSL 

      1390       1400       1410       1420       1430       1440 
LPQLTGPVLE LPEATRAPLE ELMMEGDLLE VTLDENHSIW QLLQAGQPPD LERIRTLLEL 

      1450       1460       1470       1480       1490       1500 
EKAERHGSRA RGRALERRRR RKVDRGGEGD DPAREELEPK RVRSSGPEAE EVQEEEELEE 

      1510       1520       1530       1540       1550       1560 
ETGGEGPPAP IPTTGSPSTQ ENQNGLEPAE GTTSGPSAPF STLTPRLHLP CPQQPPQQQL 

« Hide

Isoform 2 [UniParc].

Checksum: B1823D7AD5F78374
Show »

FASTA1,557175,379
Isoform 3 [UniParc].

Checksum: F82BDA8A82C57C01
Show »

FASTA1,516170,561
Isoform 4 [UniParc].

Checksum: 20A82456B8CF788E
Show »

FASTA1,379155,119
Isoform 5 [UniParc].

Checksum: CC245E4B78A1F039
Show »

FASTA1,559175,592

References

« Hide 'large scale' references
[1]"Isolation and characterization of XE169, a novel human gene that escapes X-inactivation."
Wu J., Ellison J., Salido E., Yen P., Mohandas T., Shapiro L.J.
Hum. Mol. Genet. 3:153-160(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fibroblast.
[2]"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. expand/collapse author list , 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 4).
Tissue: Uterus.
[3]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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 5).
Tissue: Eye.
[6]"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 280-344.
Tissue: Blood.
[7]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3."
Christensen J., Agger K., Cloos P.A.C., Pasini D., Rose S., Sennels L., Rappsilber J., Hansen K.H., Salcini A.E., Helin K.
Cell 128:1063-1076(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases."
Iwase S., Lan F., Bayliss P., de la Torre-Ubieta L., Huarte M., Qi H.H., Whetstine J.R., Bonni A., Roberts T.M., Shi Y.
Cell 128:1077-1088(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COFACTOR, MUTAGENESIS OF HIS-514, CHARACTERIZATION OF VARIANTS MRXSCJ PRO-388; LEU-642; PHE-731 AND CYS-751.
[10]"The histone H3K4 demethylase SMCX links REST target genes to X-linked mental retardation."
Tahiliani M., Mei P., Fang R., Leonor T., Rutenberg M., Shimizu F., Li J., Rao A., Shi Y.
Nature 447:601-605(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF HIS-514, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS MRXSCJ GLY-87; TYR-402; LYS-698 AND CYS-751.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-1359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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-1359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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-1359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Mutations in the JARID1C gene, which is involved in transcriptional regulation and chromatin remodeling, cause X-linked mental retardation."
Jensen L.R., Amende M., Gurok U., Moser B., Gimmel V., Tzschach A., Janecke A.R., Tariverdian G., Chelly J., Fryns J.-P., Van Esch H., Kleefstra T., Hamel B.C.J., Moraine C., Gecz J., Turner G., Reinhardt R., Kalscheuer V.M., Ropers H.-H., Lenzner S.
Am. J. Hum. Genet. 76:227-236(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MRXSCJ PRO-388; TYR-402; LYS-698 AND PHE-731, TISSUE SPECIFICITY.
[17]"A novel mutation in JARID1C gene associated with mental retardation."
Santos C., Rodriguez-Revenga L., Madrigal I., Badenas C., Pineda M., Mila M.
Eur. J. Hum. Genet. 14:583-586(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MRXSCJ ARG-451.
[18]"Novel JARID1C/SMCX mutations in patients with X-linked mental retardation."
Tzschach A., Lenzner S., Moser B., Reinhardt R., Chelly J., Fryns J.-P., Kleefstra T., Raynaud M., Turner G., Ropers H.-H., Kuss A., Jensen L.R.
Hum. Mutat. 27:389-389(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MRXSCJ GLY-87; LEU-642; TRP-750 AND CYS-751.
[19]"A de novo paradigm for mental retardation."
Vissers L.E., de Ligt J., Gilissen C., Janssen I., Steehouwer M., de Vries P., van Lier B., Arts P., Wieskamp N., del Rosario M., van Bon B.W., Hoischen A., de Vries B.B., Brunner H.G., Veltman J.A.
Nat. Genet. 42:1109-1112(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TYR-640.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14351.1. [P41229-1]
CCDS55417.1. [P41229-4]
CCDS65269.1. [P41229-5]
PIRI54361.
RefSeqNP_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_005262035.2. [P41229-2]
UniGeneHs.631768.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JRZNMR-A73-188[»]
ProteinModelPortalP41229.
SMRP41229. Positions 13-188, 261-616, 1186-1253.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113870. 21 interactions.
DIPDIP-39663N.
IntActP41229. 3 interactions.
STRING9606.ENSP00000364550.

Chemistry

ChEMBLCHEMBL2163176.
GuidetoPHARMACOLOGY2682.

PTM databases

PhosphoSiteP41229.

Polymorphism databases

DMDM117949812.

Proteomic databases

MaxQBP41229.
PaxDbP41229.
PRIDEP41229.

Protocols and materials databases

DNASU8242.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375379; ENSP00000364528; ENSG00000126012. [P41229-2]
ENST00000375383; ENSP00000364532; ENSG00000126012. [P41229-3]
ENST00000375401; ENSP00000364550; ENSG00000126012. [P41229-1]
ENST00000404049; ENSP00000385394; ENSG00000126012. [P41229-5]
ENST00000452825; ENSP00000445176; ENSG00000126012. [P41229-4]
ENST00000593469; ENSP00000472656; ENSG00000269816. [P41229-3]
ENST00000594714; ENSP00000469322; ENSG00000269816. [P41229-5]
ENST00000595211; ENSP00000472624; ENSG00000269816. [P41229-2]
ENST00000596526; ENSP00000472871; ENSG00000269816. [P41229-4]
ENST00000602020; ENSP00000471752; ENSG00000269816. [P41229-1]
GeneID8242.
KEGGhsa:8242.
UCSCuc004drz.3. human. [P41229-1]
uc004dsa.3. human.
uc022bxe.1. human. [P41229-4]

Organism-specific databases

CTD8242.
GeneCardsGC0XM053237.
HGNCHGNC:11114. KDM5C.
MIM300534. phenotype.
314690. gene.
neXtProtNX_P41229.
Orphanet85279. Syndromic X-linked intellectual disability due to JARID1C mutation.
PharmGKBPA35964.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327026.
HOGENOMHOG000290719.
InParanoidP41229.
KOK11446.
OMATTSICVC.
PhylomeDBP41229.
TreeFamTF106476.

Gene expression databases

ArrayExpressP41229.
BgeeP41229.
CleanExHS_JARID1C.
GenevestigatorP41229.

Family and domain databases

Gene3D1.10.150.60. 1 hit.
3.30.40.10. 2 hits.
InterProIPR001606. 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]
PfamPF01388. ARID. 1 hit.
PF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
PF00628. PHD. 2 hits.
PF08429. PLU-1. 1 hit.
PF02928. zf-C5HC2. 1 hit.
[Graphical view]
SMARTSM00501. BRIGHT. 1 hit.
SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMSSF46774. SSF46774. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEPS51011. 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]
ProtoNetSearch...

Other

ChiTaRSKDM5C. human.
EvolutionaryTraceP41229.
GeneWikiJARID1C.
GenomeRNAi8242.
NextBio31002.
PROP41229.
SOURCESearch...

Entry information

Entry nameKDM5C_HUMAN
AccessionPrimary (citable) accession number: P41229
Secondary accession number(s): B0QZ44 expand/collapse secondary AC list , B4E3I2, F5H3T1, Q5JUX3, Q5JUX4, Q5JUX5, Q7Z5S5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 14, 2006
Last modified: July 9, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM