Q9UGL1 (KDM5B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lysine-specific demethylase 5B
EC=1.14.11.-

Alternative name(s):
Cancer/testis antigen 31
Short name=CT31
Histone demethylase JARID1B
Jumonji/ARID domain-containing protein 1B
PLU-1
Retinoblastoma-binding protein 2 homolog 1
Short name=RBP2-H1

Gene names

Name:	KDM5B
Synonyms:	JARID1B, PLU1, RBBP2H1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1544 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Favors the proliferation of breast cancer cells by repressing tumor suppressor genes such as BRCA1 and HOXA5. In contrast, may act as a tumor suppressor for melanoma. Ref.6 Ref.8 Ref.9 Ref.12
Cofactor	Binds 1 Fe2+ ion per subunit By similarity.
Subunit structure	Interacts with FOXG1B, PAX9, MYC, MYCN and RB1. Interacts with HDAC1, HDAC4, HDAC5 and HDAC7 By similarity. Ref.6 Ref.7 Ref.8 Ref.10 Ref.11
Subcellular location	Nucleus Ref.1 Ref.5.
Tissue specificity	Ubiquitously expressed, with highest levels in testis. Down-regulated in melanoma and glioblastoma. Up-regulated in breast cancer (at protein level). Ref.1 Ref.2 Ref.3 Ref.5 Ref.7
Domain	Both the JmjC domain and the JmjN domain are required for enzymatic activity. The 2 first PHD-type zinc finger domains are required for transcription repression activity.
Sequence similarities	Belongs to the JARID1 histone demethylase family. Contains 1 ARID domain. Contains 1 JmjC domain. Contains 1 JmjN domain. Contains 3 PHD-type zinc fingers.
Sequence caution	The sequence CAB63108.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	Iron Metal-binding Zinc
Molecular function	Chromatin regulator Dioxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.6. Source: GDB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleolus Inferred from direct assay. Source: HPA
Molecular_function	DNA binding Inferred from direct assay PubMed 15640446. Source: GDB histone demethylase activity (H3-dimethyl-K4 specific) Inferred from direct assay PubMed 20228790. Source: UniProtKB histone demethylase activity (H3-trimethyl-K4 specific) Inferred from direct assay PubMed 20228790. Source: UniProtKB 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 Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW sequence-specific DNA binding transcription factor activity Traceable author statement Ref.1. Source: ProtInc transcription corepressor activity Inferred from direct assay Ref.6. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UGL1-1)

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: Q9UGL1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     237-237: E → ERQSLAVLPRLECSGAILAHCNLRLLDSSNSSASASQ

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1544	1544	Lysine-specific demethylase 5B		PRO_0000292412
Regions
	Domain	32 – 73	42	JmjN
	Domain	97 – 187	91	ARID
	Domain	453 – 619	167	JmjC
	Zinc finger	309 – 359	51	PHD-type 1
	Zinc finger	1176 – 1224	49	PHD-type 2
	Zinc finger	1484 – 1538	55	PHD-type 3
	Compositional bias	1434 – 1439	6	Poly-Lys
Sites
	Metal binding	499	1	Iron; catalytic By similarity
	Metal binding	502	1	Iron; catalytic By similarity
	Metal binding	587	1	Iron; catalytic By similarity
Natural variations
	Alternative sequence	237	1	E → ERQSLAVLPRLECSGAILAH CNLRLLDSSNSSASASQ in isoform 2.		VSP_026408
Experimental info
	Mutagenesis	335	1	H → A: Slightly impairs transcription repression ability. Ref.11
	Mutagenesis	499	1	H → Y: Abolishes enzymatic activity. Ref.12
	Mutagenesis	1200	1	H → A: Impairs transcription repression ability and interaction with HDAC4. Ref.11
	Sequence conflict	78	1	V → G in CAB63108. Ref.3
	Sequence conflict	585 – 589	5	AYHSG → VPQW in AAD16061. Ref.2
	Sequence conflict	708	1	C → W in AAD16061. Ref.2
	Sequence conflict	759	1	A → P in AAD16061. Ref.2
	Sequence conflict	771	1	N → T in AAD16061. Ref.2
	Sequence conflict	771	1	N → T in CAB63108. Ref.3
	Sequence conflict	1182	1	Q → R in AAD16061. Ref.2
	Sequence conflict	1293	1	A → P in AAD16061. Ref.2
	Sequence conflict	1307	1	P → L in AAD16061. Ref.2
	Sequence conflict	1331	1	S → ST in AAD16061. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: 70A0738D9A709F61	FASTA	1,544	175,658
	10 20 30 40 50 60 MEAATTLHPG PRPALPLGGP GPLGEFLPPP ECPVFEPSWE EFADPFAFIH KIRPIAEQTG 70 80 90 100 110 120 ICKVRPPPDW QPPFACDVDK LHFTPRIQRL NELEAQTRVK LNFLDQIAKY WELQGSTLKI 130 140 150 160 170 180 PHVERKILDL FQLNKLVAEE GGFAVVCKDR KWTKIATKMG FAPGKAVGSH IRGHYERILN 190 200 210 220 230 240 PYNLFLSGDS LRCLQKPNLT TDTKDKEYKP HDIPQRQSVQ PSETCPPARR AKRMRAEAMN 250 260 270 280 290 300 IKIEPEETTE ARTHNLRRRM GCPTPKCENE KEMKSSIKQE PIERKDYIVE NEKEKPKSRS 310 320 330 340 350 360 KKATNAVDLY VCLLCGSGND EDRLLLCDGC DDSYHTFCLI PPLHDVPKGD WRCPKCLAQE 370 380 390 400 410 420 CSKPQEAFGF EQAARDYTLR TFGEMADAFK SDYFNMPVHM VPTELVEKEF WRLVSTIEED 430 440 450 460 470 480 VTVEYGADIA SKEFGSGFPV RDGKIKLSPE EEEYLDSGWN LNNMPVMEQS VLAHITADIC 490 500 510 520 530 540 GMKLPWLYVG MCFSSFCWHI EDHWSYSINY LHWGEPKTWY GVPGYAAEQL ENVMKKLAPE 550 560 570 580 590 600 LFVSQPDLLH QLVTIMNPNT LMTHEVPVYR TNQCAGEFVI TFPRAYHSGF NQGFNFAEAV 610 620 630 640 650 660 NFCTVDWLPL GRQCVEHYRL LHRYCVFSHD EMICKMASKA DVLDVVVAST VQKDMAIMIE 670 680 690 700 710 720 DEKALRETVR KLGVIDSERM DFELLPDDER QCVKCKTTCF MSAISCSCKP GLLVCLHHVK 730 740 750 760 770 780 ELCSCPPYKY KLRYRYTLDD LYPMMNALKL RAESYNEWAL NVNEALEAKI NKKKSLVSFK 790 800 810 820 830 840 ALIEESEMKK FPDNDLLRHL RLVTQDAEKC ASVAQQLLNG KRQTRYRSGG GKSQNQLTVN 850 860 870 880 890 900 ELRQFVTQLY ALPCVLSQTP LLKDLLNRVE DFQQHSQKLL SEETPSAAEL QDLLDVSFEF 910 920 930 940 950 960 DVELPQLAEM RIRLEQARWL EEVQQACLDP SSLTLDDMRR LIDLGVGLAP YSAVEKAMAR 970 980 990 1000 1010 1020 LQELLTVSEH WDDKAKSLLK ARPRHSLNSL ATAVKEIEEI PAYLPNGAAL KDSVQRARDW 1030 1040 1050 1060 1070 1080 LQDVEGLQAG GRVPVLDTLI ELVTRGRSIP VHLNSLPRLE TLVAEVQAWK ECAVNTFLTE 1090 1100 1110 1120 1130 1140 NSPYSLLEVL CPRCDIGLLG LKRKQRKLKE PLPNGKKKST KLESLSDLER ALTESKETAS 1150 1160 1170 1180 1190 1200 AMATLGEARL REMEALQSLR LANEGKLLSP LQDVDIKICL CQKAPAAPMI QCELCRDAFH 1210 1220 1230 1240 1250 1260 TSCVAVPSIS QGLRIWLCPH CRRSEKPPLE KILPLLASLQ RIRVRLPEGD ALRYMIERTV 1270 1280 1290 1300 1310 1320 NWQHRAQQLL SSGNLKFVQD RVGSGLLYSR WQASAGQVSD TNKVSQPPGT TSFSLPDDWD 1330 1340 1350 1360 1370 1380 NRTSYLHSPF STGRSCIPLH GVSPEVNELL MEAQLLQVSL PEIQELYQTL LAKPSPAQQT 1390 1400 1410 1420 1430 1440 DRSSPVRPSS EKNDCCRGKR DGINSLERKL KRRLEREGLS SERWERVKKM RTPKKKKIKL 1450 1460 1470 1480 1490 1500 SHPKDMNNFK LERERSYELV RSAETHSLPS DTSYSEQEDS EDEDAICPAV SCLQPEGDEV 1510 1520 1530 1540 DWVQCDGSCN QWFHQVCVGV SPEMAEKEDY ICVRCTVKDA PSRK
	Isoform 2 [UniParc]. Checksum: 61B03B8A7EE16B3C	FASTA	1,580	179,409
	10 20 30 40 50 60 MEAATTLHPG PRPALPLGGP GPLGEFLPPP ECPVFEPSWE EFADPFAFIH KIRPIAEQTG 70 80 90 100 110 120 ICKVRPPPDW QPPFACDVDK LHFTPRIQRL NELEAQTRVK LNFLDQIAKY WELQGSTLKI 130 140 150 160 170 180 PHVERKILDL FQLNKLVAEE GGFAVVCKDR KWTKIATKMG FAPGKAVGSH IRGHYERILN 190 200 210 220 230 240 PYNLFLSGDS LRCLQKPNLT TDTKDKEYKP HDIPQRQSVQ PSETCPPARR AKRMRAERQS 250 260 270 280 290 300 LAVLPRLECS GAILAHCNLR LLDSSNSSAS ASQAMNIKIE PEETTEARTH NLRRRMGCPT 310 320 330 340 350 360 PKCENEKEMK SSIKQEPIER KDYIVENEKE KPKSRSKKAT NAVDLYVCLL CGSGNDEDRL 370 380 390 400 410 420 LLCDGCDDSY HTFCLIPPLH DVPKGDWRCP KCLAQECSKP QEAFGFEQAA RDYTLRTFGE 430 440 450 460 470 480 MADAFKSDYF NMPVHMVPTE LVEKEFWRLV STIEEDVTVE YGADIASKEF GSGFPVRDGK 490 500 510 520 530 540 IKLSPEEEEY LDSGWNLNNM PVMEQSVLAH ITADICGMKL PWLYVGMCFS SFCWHIEDHW 550 560 570 580 590 600 SYSINYLHWG EPKTWYGVPG YAAEQLENVM KKLAPELFVS QPDLLHQLVT IMNPNTLMTH 610 620 630 640 650 660 EVPVYRTNQC AGEFVITFPR AYHSGFNQGF NFAEAVNFCT VDWLPLGRQC VEHYRLLHRY 670 680 690 700 710 720 CVFSHDEMIC KMASKADVLD VVVASTVQKD MAIMIEDEKA LRETVRKLGV IDSERMDFEL 730 740 750 760 770 780 LPDDERQCVK CKTTCFMSAI SCSCKPGLLV CLHHVKELCS CPPYKYKLRY RYTLDDLYPM 790 800 810 820 830 840 MNALKLRAES YNEWALNVNE ALEAKINKKK SLVSFKALIE ESEMKKFPDN DLLRHLRLVT 850 860 870 880 890 900 QDAEKCASVA QQLLNGKRQT RYRSGGGKSQ NQLTVNELRQ FVTQLYALPC VLSQTPLLKD 910 920 930 940 950 960 LLNRVEDFQQ HSQKLLSEET PSAAELQDLL DVSFEFDVEL PQLAEMRIRL EQARWLEEVQ 970 980 990 1000 1010 1020 QACLDPSSLT LDDMRRLIDL GVGLAPYSAV EKAMARLQEL LTVSEHWDDK AKSLLKARPR 1030 1040 1050 1060 1070 1080 HSLNSLATAV KEIEEIPAYL PNGAALKDSV QRARDWLQDV EGLQAGGRVP VLDTLIELVT 1090 1100 1110 1120 1130 1140 RGRSIPVHLN SLPRLETLVA EVQAWKECAV NTFLTENSPY SLLEVLCPRC DIGLLGLKRK 1150 1160 1170 1180 1190 1200 QRKLKEPLPN GKKKSTKLES LSDLERALTE SKETASAMAT LGEARLREME ALQSLRLANE 1210 1220 1230 1240 1250 1260 GKLLSPLQDV DIKICLCQKA PAAPMIQCEL CRDAFHTSCV AVPSISQGLR IWLCPHCRRS 1270 1280 1290 1300 1310 1320 EKPPLEKILP LLASLQRIRV RLPEGDALRY MIERTVNWQH RAQQLLSSGN LKFVQDRVGS 1330 1340 1350 1360 1370 1380 GLLYSRWQAS AGQVSDTNKV SQPPGTTSFS LPDDWDNRTS YLHSPFSTGR SCIPLHGVSP 1390 1400 1410 1420 1430 1440 EVNELLMEAQ LLQVSLPEIQ ELYQTLLAKP SPAQQTDRSS PVRPSSEKND CCRGKRDGIN 1450 1460 1470 1480 1490 1500 SLERKLKRRL EREGLSSERW ERVKKMRTPK KKKIKLSHPK DMNNFKLERE RSYELVRSAE 1510 1520 1530 1540 1550 1560 THSLPSDTSY SEQEDSEDED AICPAVSCLQ PEGDEVDWVQ CDGSCNQWFH QVCVGVSPEM 1570 1580 AEKEDYICVR CTVKDAPSRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel gene (PLU-1) containing highly conserved putative DNA/chromatin binding motifs is specifically up-regulated in breast cancer." Lu P.J., Sundquist K., Baeckstrom D., Poulsom R., Hanby A., Meier-Ewert S., Jones T., Mitchell M., Pitha-Rowe P., Freemont P., Taylor-Papadimitriou J. J. Biol. Chem. 274:15633-15645(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Tissue: Mammary cancer.
[2]	"Deficiency of a novel retinoblastoma binding protein 2-homolog is a consistent feature of sporadic human melanoma skin cancer." Vogt T., Kroiss M., McClelland M., Gruss C., Becker B., Bosserhoff A.K., Rumpler G., Bogenrieder T., Landthaler M., Stolz W. Lab. Invest. 79:1615-1627(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY. Tissue: Teratocarcinoma.
[3]	"Isolation and chromosomal localization of a new human retinoblastoma binding protein 2 homologue 1a (RBBP2H1A)." Kashuba V., Protopopov A., Podowski R., Gizatullin R., Li J., Klein G., Wahlestedt C., Zabarovsky E. Eur. J. Hum. Genet. 8:407-413(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"PLU-1 nuclear protein, which is upregulated in breast cancer, shows restricted expression in normal human adult tissues: a new cancer/testis antigen?" Barrett A., Madsen B., Copier J., Lu P.J., Cooper L., Scibetta A.G., Burchell J., Taylor-Papadimitriou J. Int. J. Cancer 101:581-588(2002) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[6]	"Human PLU-1 has transcriptional repression properties and interacts with the developmental transcription factors BF-1 and PAX9." Tan K., Shaw A.L., Madsen B., Jensen K., Taylor-Papadimitriou J., Freemont P.S. J. Biol. Chem. 278:20507-20513(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH FOXG1B AND PAX9.
[7]	"Retinoblastoma-binding protein 2-homolog 1: a retinoblastoma-binding protein downregulated in malignant melanomas." Roesch A., Becker B., Meyer S., Wild P., Hafner C., Landthaler M., Vogt T. Mod. Pathol. 18:1249-1257(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INTERACTION WITH RB1.
[8]	"Re-expression of the retinoblastoma-binding protein 2-homolog 1 reveals tumor-suppressive functions in highly metastatic melanoma cells." Roesch A., Becker B., Schneider-Brachert W., Hagen I., Landthaler M., Vogt T. J. Invest. Dermatol. 126:1850-1859(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RB1.
[9]	"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.
[10]	"The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth." Secombe J., Li L., Carlos L., Eisenman R.N. Genes Dev. 21:537-551(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MYC AND MYCN.
[11]	"Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases." Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K., Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E., Freemont P., Taylor-Papadimitriou J. Int. J. Cancer 121:265-275(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HDAC1; HDAC4; HDAC5 AND HDAC7, MUTAGENESIS OF HIS-335 AND HIS-1200.
[12]	"PLU-1 is an H3K4 demethylase involved in transcriptional repression and breast cancer cell proliferation." Yamane K., Tateishi K., Klose R.J., Fang J., Fabrizio L.A., Erdjument-Bromage H., Taylor-Papadimitriou J., Tempst P., Zhang Y. Mol. Cell 25:801-812(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF HIS-499.
[13]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ132440 mRNA. Translation: CAB43532.1. AF087481 mRNA. Translation: AAD16061.1. AJ243706 mRNA. Translation: CAB63108.1. Different initiation. AC098934 Genomic DNA. No translation available. AC104463 Genomic DNA. No translation available.
IPI	IPI00847436. IPI00873956.
RefSeq	NP_006609.3. NM_006618.3.
UniGene	Hs.443650.
3D structure databases
ProteinModelPortal	Q9UGL1.
SMR	Q9UGL1. Positions 94-208, 307-615, 1180-1222, 1485-1535.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-53652N.
IntAct	Q9UGL1. 2 interactions.
STRING	9606.ENSP00000356234.
PTM databases
PhosphoSite	Q9UGL1.
Polymorphism databases
DMDM	296439317.
Proteomic databases
PaxDb	Q9UGL1.
PRIDE	Q9UGL1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000367264; ENSP00000356233; ENSG00000117139. ENST00000367265; ENSP00000356234; ENSG00000117139.
GeneID	10765.
KEGG	hsa:10765.
UCSC	uc001gyf.3. human. uc009xag.3. human.
Organism-specific databases
CTD	10765.
GeneCards	GC01M202696.
H-InvDB	HIX0001478.
HGNC	HGNC:18039. KDM5B.
HPA	HPA027179.
MIM	605393. gene.
neXtProt	NX_Q9UGL1.
PharmGKB	PA164721626.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG327026.
HOGENOM	HOG000290719.
InParanoid	Q9UGL1.
KO	K11446.
OMA	CENEKEM.
OrthoDB	EOG4HT8RC.
Gene expression databases
ArrayExpress	Q9UGL1.
Bgee	Q9UGL1.
CleanEx	HS_JARID1B.
Genevestigator	Q9UGL1.
Family and domain databases
Gene3D	1.10.150.60. 1 hit. 3.30.40.10. 3 hits.
InterPro	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]
Pfam	PF01388. ARID. 1 hit. PF02373. JmjC. 1 hit. PF02375. JmjN. 1 hit. PF00628. PHD. 3 hits. PF08429. PLU-1. 1 hit. PF02928. zf-C5HC2. 1 hit. [Graphical view]
SMART	SM00501. BRIGHT. 1 hit. SM00558. JmjC. 1 hit. SM00545. JmjN. 1 hit. SM00249. PHD. 3 hits. [Graphical view]
SUPFAM	SSF46774. ARID. 1 hit. SSF57903. FYVE_PHD_ZnF. 3 hits.
PROSITE	PS51011. ARID. 1 hit. PS51184. JMJC. 1 hit. PS51183. JMJN. 1 hit. PS01359. ZF_PHD_1. 2 hits. PS50016. ZF_PHD_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	KDM5B. human.
GenomeRNAi	10765.
NextBio	40877.
SOURCE	Search...

Entry information

Entry name

KDM5B_HUMAN

Accession

Primary (citable) accession number: Q9UGL1
Secondary accession number(s): O95811, Q15752, Q9Y3Q5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	May 18, 2010
Last modified:	May 29, 2013
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.