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A1YVX4 (KDM5C_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
Gene names
Name:KDM5C
Synonyms:JARID1C, SMCX
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length1516 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Cofactor

Alpha-ketoglutarate By similarity.

Binds 1 Fe2+ ion per subunit By similarity.

Subunit structure

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

Subcellular location

Nucleus By similarity.

Domain

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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15161516Lysine-specific demethylase 5C
PRO_0000292417

Regions

Domain14 – 5542JmjN
Domain24 – 128105ARID
Domain427 – 593167JmjC
Zinc finger283 – 33351PHD-type 1
Zinc finger1144 – 120966PHD-type 2
Compositional bias1413 – 14175Poly-Arg
Compositional bias1450 – 14578Poly-Glu

Sites

Metal binding4731Iron; catalytic By similarity
Metal binding4761Iron; catalytic By similarity
Metal binding5611Iron; catalytic By similarity

Amino acid modifications

Modified residue2761Phosphoserine By similarity
Modified residue13181Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1YVX4 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 8DE6C52868E3E7E3

FASTA1,516170,584
        10         20         30         40         50         60 
MEPGSDDFLP PPECPVFEPS WAEFRDPLGY IAKIRPIAEK SGICKIRPPA DWQPPFAVEV 

        70         80         90        100        110        120 
DNFRFTPRIQ RLNELEIVVE EGGYEAICKD RRWARVAQRL NYPPGKNIGS LLRSHYERIV 

       130        140        150        160        170        180 
YPYEMYQSGA NLVQCNTRPF DNEEKDKEYK PHSIPLRQSV QPSKFNSYGR RAKRLQPDPE 

       190        200        210        220        230        240 
PTEEDIEKNP ELKKLQIYGA GPKMMGLGLM AKDKTLRKKD KEGPECPPTV VVKEESGGDV 

       250        260        270        280        290        300 
KVESTSPKTF LESKEELSHS PEPCTKMTMR LRRNHSNAQF IESYVCRMCS RGDEDDKLLL 

       310        320        330        340        350        360 
CDGCDDNYHI FCLLPPLPEI PKGVWRCPKC VMAECKRPPE AFGFEQATRE YTLQSFGEMA 

       370        380        390        400        410        420 
DSFKADYSNM PVHMVPTELV EKEFWRLVNS IEEDVTVEYG ADIHSKEFGS GFPVSDSKRH 

       430        440        450        460        470        480 
LTPEEEEYAT SGWNLNVMPV LEQSVLCHIN ADISGMKVPW LYVGMVFSAF CWHIEDHWSY 

       490        500        510        520        530        540 
SINYLHWGEP KTWYGVPSLA AEHLEEVMKK LTPELFDSQP DLLHQLVTLM NPNTLMSHGV 

       550        560        570        580        590        600 
PVVRTNQCAG EFVITFPRAY HSGFNQGYNF AEAVNFCTAD WLPAGRQCIE HYRRLRRYCV 

       610        620        630        640        650        660 
FSHEELICKM AACPEKLDLN LAAAVHKEMF IMVQEERRLR KALLEKGITE AEREAFELLP 

       670        680        690        700        710        720 
DDERQCIKCK TTCFLSALAC YDCPDGLVCL SHINDLCKCS SSRQYLRYRY TLDELPAMLH 

       730        740        750        760        770        780 
KLKVRAESFD TWANKVRVAL EVEDGRKRSL EELRALESEA RERRFPNSEL LQRLKNCLSE 

       790        800        810        820        830        840 
AEACVSRALG LVSGQEAGPH RVAGLQMTLA ELRAFLDQMN NLPCAMHQIG DVKGILEQVE 

       850        860        870        880        890        900 
AYQAEAREAL ASLPSSPGLL QSLLERGRQL GVEVPEAQQL QRQVEQARWL DEVKRTLAPS 

       910        920        930        940        950        960 
ARRGTLAVMR GLLVAGASVA PSPAVDKAQA ELQELLTIAE RWEEKAHLCL EARQKHPPAT 

       970        980        990       1000       1010       1020 
LEAIIHEAEN IPVHLPNIQA LKEALAKARA WIADVDEIQN GDHYPCLDDL EGLVAVGRDL 

      1030       1040       1050       1060       1070       1080 
PVGLEELRQL ELQVLTAHSW REKASKTFLK KNSCYTLLEV LCPCADAGSD STKRSRWMEK 

      1090       1100       1110       1120       1130       1140 
ELGLYKSDTE LLGLSAQDLR DPGSVIVAFK EGEQKEKEGI LQLRRTNSAK PSPLASPNTS 

      1150       1160       1170       1180       1190       1200 
SSATSICVCG QVPAGVGALQ CDLCQDWFHG RCVSVPRLLS SPRPSPTSSP LLAWWEWDTK 

      1210       1220       1230       1240       1250       1260 
FLCPLCMRSR RPRLETILAL LVALQRLPVR LPEGEALQCL TERAISWQGR ARQALAFEDV 

      1270       1280       1290       1300       1310       1320 
TALLGRLAEL RQRLQAEPRP EEPPTYPSTP AFDPLREGSG KDMPKVQGLL ENGDSVTSPE 

      1330       1340       1350       1360       1370       1380 
KVAPGEGSDL ELLSSLLPQL TGPVLELPEA TRAPLEELML EGDLLEVTLD ENHSIWQLLQ 

      1390       1400       1410       1420       1430       1440 
AGKPPDLARI RTLLELEKAE RHGSRARGRA LERRRRRKVD RGGEGDDPAR EELEPKRVRS 

      1450       1460       1470       1480       1490       1500 
SWPEAEEAHE EEELEEETGG EGPPQPLPAT GSPSTQENQN GLEPALGASS GSSVPFSTLT 

      1510 
PRLHMSCPQQ PPQQQL 

« Hide

References

[1]Yi L., Xu Y.
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF139241 mRNA. Translation: ABL74503.1.
RefSeqNP_001090902.1. NM_001097433.1.
UniGeneSsc.25162.

3D structure databases

ProteinModelPortalA1YVX4.
SMRA1YVX4. Positions 22-147, 278-353.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100037295.
KEGGssc:100037295.

Organism-specific databases

CTD8242.

Phylogenomic databases

eggNOGNOG327026.
KOK11446.

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. 1 hit.
PF08429. PLU-1. 1 hit.
PF02928. zf-C5HC2. 1 hit.
[Graphical view]
SMARTSM00558. 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...

Entry information

Entry nameKDM5C_PIG
AccessionPrimary (citable) accession number: A1YVX4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: February 6, 2007
Last modified: February 19, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families