UniProtKB - P29375 (KDM5A_HUMAN)

BLAST

>sp|P29375|KDM5A_HUMAN Lysine-specific demethylase 5A OS=Homo sapiens OX=9606 GN=KDM5A PE=1 SV=3
MAGVGPGGYAAEFVPPPECPVFEPSWEEFTDPLSFIGRIRPLAEKTGICKIRPPKDWQPP
FACEVKSFRFTPRVQRLNELEAMTRVRLDFLDQLAKFWELQGSTLKIPVVERKILDLYAL
SKIVASKGGFEMVTKEKKWSKVGSRLGYLPGKGTGSLLKSHYERILYPYELFQSGVSLMG
VQMPNLDLKEKVEPEVLSTDTQTSPEPGTRMNILPKRTRRVKTQSESGDVSRNTELKKLQ
IFGAGPKVVGLAMGTKDKEDEVTRRRKVTNRSDAFNMQMRQRKGTLSVNFVDLYVCMFCG
RGNNEDKLLLCDGCDDSYHTFCLIPPLPDVPKGDWRCPKCVAEECSKPREAFGFEQAVRE
YTLQSFGEMADNFKSDYFNMPVHMVPTELVEKEFWRLVSSIEEDVIVEYGADISSKDFGS
GFPVKDGRRKILPEEEEYALSGWNLNNMPVLEQSVLAHINVDISGMKVPWLYVGMCFSSF
CWHIEDHWSYSINYLHWGEPKTWYGVPSHAAEQLEEVMRELAPELFESQPDLLHQLVTIM
NPNVLMEHGVPVYRTNQCAGEFVVTFPRAYHSGFNQGYNFAEAVNFCTADWLPIGRQCVN
HYRRLRRHCVFSHEELIFKMAADPECLDVGLAAMVCKELTLMTEEETRLRESVVQMGVLM
SEEEVFELVPDDERQCSACRTTCFLSALTCSCNPERLVCLYHPTDLCPCPMQKKCLRYRY
PLEDLPSLLYGVKVRAQSYDTWVSRVTEALSANFNHKKDLIELRVMLEDAEDRKYPENDL
FRKLRDAVKEAETCASVAQLLLSKKQKHRQSPDSGRTRTKLTVEELKAFVQQLFSLPCVI
SQARQVKNLLDDVEEFHERAQEAMMDETPDSSKLQMLIDMGSSLYVELPELPRLKQELQQ
ARWLDEVRLTLSDPQQVTLDVMKKLIDSGVGLAPHHAVEKAMAELQELLTVSERWEEKAK
VCLQARPRHSVASLESIVNEAKNIPAFLPNVLSLKEALQKAREWTAKVEAIQSGSNYAYL
EQLESLSAKGRPIPVRLEALPQVESQVAAARAWRERTGRTFLKKNSSHTLLQVLSPRTDI
GVYGSGKNRRKKVKELIEKEKEKDLDLEPLSDLEEGLEETRDTAMVVAVFKEREQKEIEA
MHSLRAANLAKMTMVDRIEEVKFCICRKTASGFMLQCELCKDWFHNSCVPLPKSSSQKKG
SSWQAKEVKFLCPLCMRSRRPRLETILSLLVSLQKLPVRLPEGEALQCLTERAMSWQDRA
RQALATDELSSALAKLSVLSQRMVEQAAREKTEKIISAELQKAAANPDLQGHLPSFQQSA
FNRVVSSVSSSPRQTMDYDDEETDSDEDIRETYGYDMKDTASVKSSSSLEPNLFCDEEIP
IKSEEVVTHMWTAPSFCAEHAYSSASKSCSQGSSTPRKQPRKSPLVPRSLEPPVLELSPG
AKAQLEELMMVGDLLEVSLDETQHIWRILQATHPPSEDRFLHIMEDDSMEEKPLKVKGKD
SSEKKRKRKLEKVEQLFGEGKQKSKELKKMDKPRKKKLKLGADKSKELNKLAKKLAKEEE
RKKKKEKAAAAKVELVKESTEKKREKKVLDIPSKYDWSGAEESDDENAVCAAQNCQRPCK
DKVDWVQCDGGCDEWFHQVCVGVSPEMAENEDYICINCAKKQGPVSPGPAPPPSFIMSYK
LPMEDLKETS

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History
Entry version 187 (07 Nov 2018)
Sequence version 3 (25 Nov 2008)
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Protein

Lysine-specific demethylase 5A

Gene

KDM5A

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

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'. Regulates specific gene transcription through DNA-binding on 5'-CCGCCC-3' motif (PubMed:18270511). May stimulate transcription mediated by nuclear receptors. Involved in transcriptional regulation of Hox proteins during cell differentiation (PubMed:19430464). May participate in transcriptional repression of cytokines such as CXCL12. Plays a role in the regulation of the circadian rhythm and in maintaining the normal periodicity of the circadian clock. In a histone demethylase-independent manner, acts as a coactivator of the CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER1/2 and other clock-controlled genes and increases histone acetylation at PER1/2 promoters by inhibiting the activity of HDAC1 (By similarity). Seems to act as a transcriptional corepressor for some genes such as MT1F and to favor the proliferation of cancer cells (PubMed:27427228).By similarity8 Publications

Cofactorⁱ

Fe²⁺By similarityNote: Binds 1 Fe²⁺ ion per subunit.By similarity

Activity regulationⁱ

The inhibitors KDOAM-25, CPI-455 and others inhibits its demethylase activity, resulting to cell growth arrest in cancer cells.2 Publications

Kineticsⁱ

Kcat are 2.1 min(-1) and 1.9 min(-1) for 2-oxoglutarate and histone H3K4me3, respectively.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	409	2-oxoglutarate2 Publications	1
Metal bindingⁱ	483	Iron; catalyticPROSITE-ProRule annotation4 Publications	1
Metal bindingⁱ	485	Iron; catalytic4 Publications	1
Binding siteⁱ	491	2-oxoglutarate2 Publications	1
Binding siteⁱ	493	2-oxoglutarate2 Publications	1
Binding siteⁱ	501	2-oxoglutarate2 Publications	1
Metal bindingⁱ	571	Iron; catalyticPROSITE-ProRule annotation4 Publications	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Zinc fingerⁱ	293 – 343	PHD-type 1PROSITE-ProRule annotationAdd BLAST	51
Zinc fingerⁱ	676 – 728	C5HC2Combined sources2 PublicationsAdd BLAST	53
Zinc fingerⁱ	1161 – 1218	PHD-type 2PROSITE-ProRule annotationAdd BLAST	58
Zinc fingerⁱ	1607 – 1661	PHD-type 31 PublicationAdd BLAST	55

GO - Molecular functionⁱ

chromatin binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
chromatin DNA binding Source: Ensembl
core promoter sequence-specific DNA binding
Source: CAFA
Inferred from mutant phenotypeⁱ
- 18270511
dioxygenase activity Source: UniProtKB-KW
DNA binding
Source: GDB
Inferred from direct assayⁱ
- 15640446
DNA-binding transcription factor activity
Source: CAFA
Inferred from mutant phenotypeⁱ
- 18270511
DNA-binding transcription factor activity, RNA polymerase II-specific Source: NTNU_SB
DNA-binding transcription repressor activity, RNA polymerase II-specific
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
histone binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19430464
histone demethylase activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
histone demethylase activity (H3-dimethyl-K4 specific)
Source: CAFA
Inferred from direct assayⁱ
- 18270511
histone demethylase activity (H3-trimethyl-K4 specific)
Source: CAFA
Inferred from direct assayⁱ
- 18270511
methylated histone binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19430464
transcription coactivator activity Source: UniProtKB
zinc ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19430464
- 27499454

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

circadian regulation of gene expression Source: UniProtKB
histone H3-K4 demethylation
Source: CAFA
Inferred from direct assayⁱ
- 18270511
histone H3-K9 demethylation Source: GOC
male gonad development Source: Ensembl
negative regulation of histone deacetylase activity Source: UniProtKB
positive regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from direct assayⁱ
- 11358960
regulation of DNA-binding transcription factor activity
Source: CAFA
Inferred from mutant phenotypeⁱ
- 18270511
spermatogenesis Source: Ensembl
transcription by RNA polymerase II
Source: ProtInc
Traceable author statementⁱ
- 8414517

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Activator, Chromatin regulator, Developmental protein, Dioxygenase, Oxidoreductase
Biological process	Biological rhythms, Transcription, Transcription regulation
Ligand	Iron, Metal-binding, Zinc

Enzyme and pathway databases

Reactomeⁱ	R-HSA-3214842 HDMs demethylate histones
SIGNORⁱ	P29375

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Lysine-specific demethylase 5A (EC:1.14.11.-) Alternative name(s): Histone demethylase JARID1A Jumonji/ARID domain-containing protein 1A Retinoblastoma-binding protein 2 Short name: RBBP-2
Gene namesⁱ	Name:KDM5AImported Synonyms:JARID1A, RBBP2, RBP21 Publication
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 12

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000073614.11
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9886 KDM5A
MIMⁱ	180202 gene
neXtProtⁱ	NX_P29375

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	112	R → E: Decreases DNA-binding. 1 Publication	1
Mutagenesisⁱ	152	K → E: Abolishes DNA-binding. 1 Publication	1
Mutagenesisⁱ	156	S → D: Decreases DNA-binding. 1 Publication	1
Mutagenesisⁱ	157	L → E: Decreases DNA-binding. 1 Publication	1
Mutagenesisⁱ	626	C → S: No effect on lysine-specific histone demethylase activity; when associated with S-636. 1 Publication	1
Mutagenesisⁱ	636	C → S: No effect on lysine-specific histone demethylase activity; when associated with S-626. 1 Publication	1
Mutagenesisⁱ	1609	V → G: No effect on interaction with histone H3 di- and trimethylated at 'Lys-4'. 1 Publication	1
Mutagenesisⁱ	1625	W → A: Abolishes interaction with histone H3 di- and trimethylated at 'Lys-4'. 1 Publication	1
Mutagenesisⁱ	1634 – 1635	EW → AA: Abolishes interaction with histone H3 di- and trimethylated at 'Lys-4'. 1 Publication	2

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5927
Open Targets More...OpenTargetsⁱ	ENSG00000073614
PharmGKBⁱ	PA34250

Chemistry databases

ChEMBLⁱ	CHEMBL2424504
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2680

Polymorphism and mutation databases

BioMutaⁱ	KDM5A
DMDMⁱ	215274124

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000200584	1 – 1690	Lysine-specific demethylase 5AAdd BLAST		1690

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Cross-linkⁱ	191	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	204	PhosphoserineCombined sources	1
Cross-linkⁱ	1007	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	1111	PhosphoserineCombined sources	1
Modified residueⁱ	1330	PhosphoserineCombined sources	1
Modified residueⁱ	1331	PhosphoserineCombined sources	1
Modified residueⁱ	1343	PhosphothreonineBy similarity	1
Modified residueⁱ	1345	PhosphoserineBy similarity	1
Modified residueⁱ	1438	PhosphoserineCombined sources	1
Modified residueⁱ	1488	PhosphoserineCombined sources	1
Modified residueⁱ	1595	PhosphotyrosineBy similarity	1
Modified residueⁱ	1598	PhosphoserineCombined sources	1
Modified residueⁱ	1603	PhosphoserineCombined sources	1
Modified residueⁱ	1666	PhosphoserineCombined sources	1

Keywords - PTMⁱ

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	P29375
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P29375
PaxDbⁱ	P29375
PeptideAtlas More...PeptideAtlasⁱ	P29375
PRIDEⁱ	P29375
ProteomicsDBⁱ	54559 54560 [P29375-2]

PTM databases

iPTMnetⁱ	P29375
PhosphoSitePlusⁱ	P29375
SwissPalmⁱ	P29375

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000073614 Expressed in 244 organ(s), highest expression level in peritoneum
CleanExⁱ	HS_JARID1A HS_RBP2
ExpressionAtlasⁱ	P29375 baseline and differential
Genevisibleⁱ	P29375 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA006201

HPAⁱ

HPA006201

Interactionⁱ

Subunit structureⁱ

Interacts with SUZ12; the interaction is direct (By similarity). Interacts with the viral protein-binding domain of RB1. Interacts with ESR1, MYC, MYCN and LMO2. Interacts with HDAC1 (By similarity). Interacts with ARNTL/BMAL1 and CLOCK. Interacts (via PHD-type 1 zinc finger) with histone H3 unmodified at 'Lys-4' and (via PHD-type 3 zinc finger) with histone H3 di- and trimethylated at 'Lys-4' (PubMed:19430464).By similarity8 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
RB1	P06400	2	EBI-1560836,EBI-491274

With

Entry

#Exp.

IntAct

Notes

RB1

P06400

EBI-1560836,EBI-491274

GO - Molecular functionⁱ

histone binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19430464
methylated histone binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19430464

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	111862, 30 interactors
Database of interacting proteins More...DIPⁱ	DIP-472N
IntActⁱ	P29375, 11 interactors
Molecular INTeraction database More...MINTⁱ	P29375
STRINGⁱ	9606.ENSP00000382688

Chemistry databases

BindingDBⁱ

P29375

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	28 – 30	Combined sources	3
Helixⁱ	32 – 43	Combined sources	12
Turnⁱ	44 – 46	Combined sources	3
Beta strandⁱ	47 – 51	Combined sources	5
Turnⁱ	65 – 67	Combined sources	3
Beta strandⁱ	73 – 76	Combined sources	4
Turnⁱ	77 – 82	Combined sources	6
Helixⁱ	85 – 100	Combined sources	16
Helixⁱ	117 – 126	Combined sources	10
Helixⁱ	130 – 136	Combined sources	7
Helixⁱ	139 – 145	Combined sources	7
Helixⁱ	154 – 173	Combined sources	20
Beta strandⁱ	174 – 176	Combined sources	3
Helixⁱ	198 – 201	Combined sources	4
Turnⁱ	350 – 353	Combined sources	4
Helixⁱ	363 – 378	Combined sources	16
Helixⁱ	382 – 384	Combined sources	3
Helixⁱ	387 – 399	Combined sources	13
Beta strandⁱ	401 – 403	Combined sources	3
Beta strandⁱ	406 – 414	Combined sources	9
Helixⁱ	415 – 418	Combined sources	4
Beta strandⁱ	426 – 429	Combined sources	4
Helixⁱ	433 – 435	Combined sources	3
Helixⁱ	436 – 440	Combined sources	5
Helixⁱ	445 – 447	Combined sources	3
Helixⁱ	448 – 450	Combined sources	3
Helixⁱ	455 – 459	Combined sources	5
Beta strandⁱ	465 – 468	Combined sources	4
Beta strandⁱ	470 – 474	Combined sources	5
Beta strandⁱ	479 – 483	Combined sources	5
Helixⁱ	486 – 488	Combined sources	3
Beta strandⁱ	490 – 499	Combined sources	10
Beta strandⁱ	501 – 506	Combined sources	6
Helixⁱ	508 – 510	Combined sources	3
Helixⁱ	511 – 521	Combined sources	11
Helixⁱ	524 – 526	Combined sources	3
Helixⁱ	531 – 534	Combined sources	4
Turnⁱ	535 – 537	Combined sources	3
Helixⁱ	542 – 547	Combined sources	6
Beta strandⁱ	553 – 557	Combined sources	5
Beta strandⁱ	562 – 565	Combined sources	4
Beta strandⁱ	570 – 586	Combined sources	17
Helixⁱ	589 – 591	Combined sources	3
Helixⁱ	592 – 604	Combined sources	13
Helixⁱ	613 – 621	Combined sources	9
Helixⁱ	629 – 655	Combined sources	27
Beta strandⁱ	661 – 663	Combined sources	3
Helixⁱ	666 – 668	Combined sources	3
Helixⁱ	671 – 673	Combined sources	3
Beta strandⁱ	674 – 676	Combined sources	3
Beta strandⁱ	685 – 688	Combined sources	4
Beta strandⁱ	691 – 693	Combined sources	3
Helixⁱ	703 – 705	Combined sources	3
Beta strandⁱ	711 – 713	Combined sources	3
Beta strandⁱ	716 – 720	Combined sources	5
Helixⁱ	724 – 743	Combined sources	20
Helixⁱ	766 – 772	Combined sources	7
Turnⁱ	780 – 784	Combined sources	5
Beta strandⁱ	1620 – 1627	Combined sources	8
Beta strandⁱ	1629 – 1632	Combined sources	4
Beta strandⁱ	1635 – 1637	Combined sources	3
Helixⁱ	1639 – 1641	Combined sources	3
Helixⁱ	1645 – 1650	Combined sources	6
Turnⁱ	1656 – 1658	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P29375
SMRⁱ	P29375
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P29375

EvolutionaryTraceⁱ

P29375

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	19 – 60	JmjNPROSITE-ProRule annotationAdd BLAST	42
Domainⁱ	84 – 174	ARIDPROSITE-ProRule annotationAdd BLAST	91
Domainⁱ	437 – 603	JmjCPROSITE-ProRule annotationAdd BLAST	167

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	1623 – 1690	Interaction with LMO21 PublicationAdd BLAST		68

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	419 – 423	GSGFP motifBy similarity		5

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	1492 – 1587	Lys-richAdd BLAST		96

Domainⁱ

The GSGFP motif is required for the interaction with SUZ12 (By similarity). The ARID domain specifically binds to the CCGCCC motif and is required for the lysine-specific histone demethylase activity (PubMed:18270511). The PHD-type 3 zinc finger is required for the interaction with histone H3 di- and trimethylated at 'Lys-4' (PubMed:19430464).By similarity2 Publications

Sequence similaritiesⁱ

Belongs to the JARID1 histone demethylase family.Curated

Zinc finger

Feature key	Position(s)	DescriptionActions	Length
Zinc fingerⁱ	293 – 343	PHD-type 1PROSITE-ProRule annotationAdd BLAST	51
Zinc fingerⁱ	676 – 728	C5HC2Combined sources2 PublicationsAdd BLAST	53
Zinc fingerⁱ	1161 – 1218	PHD-type 2PROSITE-ProRule annotationAdd BLAST	58
Zinc fingerⁱ	1607 – 1661	PHD-type 31 PublicationAdd BLAST	55

Keywords - Domainⁱ

Repeat, Zinc-finger

Phylogenomic databases

eggNOGⁱ	KOG1246 Eukaryota ENOG410XR9J LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000063118
HOGENOMⁱ	HOG000290719
InParanoidⁱ	P29375
KEGG Orthology (KO) More...KOⁱ	K11446
OMAⁱ	PICDWRV
PhylomeDBⁱ	P29375
TreeFamⁱ	TF106476

Family and domain databases

Gene3Dⁱ	1.10.150.60, 1 hit 3.30.40.10, 2 hits
InterProⁱ	View protein in InterPro IPR001606 ARID_dom IPR036431 ARID_dom_sf 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
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01388 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
SMARTⁱ	View protein in SMART SM00501 BRIGHT, 1 hit SM00558 JmjC, 1 hit SM00545 JmjN, 1 hit SM00249 PHD, 3 hits
SUPFAMⁱ	SSF46774 SSF46774, 1 hit SSF57903 SSF57903, 3 hits
PROSITEⁱ	View 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, 3 hits

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P29375-1) [UniParc]FASTA Add 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
MAGVGPGGYA AEFVPPPECP VFEPSWEEFT DPLSFIGRIR PLAEKTGICK 
        60         70         80         90        100
IRPPKDWQPP FACEVKSFRF TPRVQRLNEL EAMTRVRLDF LDQLAKFWEL 
       110        120        130        140        150
QGSTLKIPVV ERKILDLYAL SKIVASKGGF EMVTKEKKWS KVGSRLGYLP 
       160        170        180        190        200
GKGTGSLLKS HYERILYPYE LFQSGVSLMG VQMPNLDLKE KVEPEVLSTD 
       210        220        230        240        250
TQTSPEPGTR MNILPKRTRR VKTQSESGDV SRNTELKKLQ IFGAGPKVVG 
       260        270        280        290        300
LAMGTKDKED EVTRRRKVTN RSDAFNMQMR QRKGTLSVNF VDLYVCMFCG 
       310        320        330        340        350
RGNNEDKLLL CDGCDDSYHT FCLIPPLPDV PKGDWRCPKC VAEECSKPRE 
       360        370        380        390        400
AFGFEQAVRE YTLQSFGEMA DNFKSDYFNM PVHMVPTELV EKEFWRLVSS 
       410        420        430        440        450
IEEDVIVEYG ADISSKDFGS GFPVKDGRRK ILPEEEEYAL SGWNLNNMPV 
       460        470        480        490        500
LEQSVLAHIN VDISGMKVPW LYVGMCFSSF CWHIEDHWSY SINYLHWGEP 
       510        520        530        540        550
KTWYGVPSHA AEQLEEVMRE LAPELFESQP DLLHQLVTIM NPNVLMEHGV 
       560        570        580        590        600
PVYRTNQCAG EFVVTFPRAY HSGFNQGYNF AEAVNFCTAD WLPIGRQCVN 
       610        620        630        640        650
HYRRLRRHCV FSHEELIFKM AADPECLDVG LAAMVCKELT LMTEEETRLR 
       660        670        680        690        700
ESVVQMGVLM SEEEVFELVP DDERQCSACR TTCFLSALTC SCNPERLVCL 
       710        720        730        740        750
YHPTDLCPCP MQKKCLRYRY PLEDLPSLLY GVKVRAQSYD TWVSRVTEAL 
       760        770        780        790        800
SANFNHKKDL IELRVMLEDA EDRKYPENDL FRKLRDAVKE AETCASVAQL 
       810        820        830        840        850
LLSKKQKHRQ SPDSGRTRTK LTVEELKAFV QQLFSLPCVI SQARQVKNLL 
       860        870        880        890        900
DDVEEFHERA QEAMMDETPD SSKLQMLIDM GSSLYVELPE LPRLKQELQQ 
       910        920        930        940        950
ARWLDEVRLT LSDPQQVTLD VMKKLIDSGV GLAPHHAVEK AMAELQELLT 
       960        970        980        990       1000
VSERWEEKAK VCLQARPRHS VASLESIVNE AKNIPAFLPN VLSLKEALQK 
      1010       1020       1030       1040       1050
AREWTAKVEA IQSGSNYAYL EQLESLSAKG RPIPVRLEAL PQVESQVAAA 
      1060       1070       1080       1090       1100
RAWRERTGRT FLKKNSSHTL LQVLSPRTDI GVYGSGKNRR KKVKELIEKE 
      1110       1120       1130       1140       1150
KEKDLDLEPL SDLEEGLEET RDTAMVVAVF KEREQKEIEA MHSLRAANLA 
      1160       1170       1180       1190       1200
KMTMVDRIEE VKFCICRKTA SGFMLQCELC KDWFHNSCVP LPKSSSQKKG 
      1210       1220       1230       1240       1250
SSWQAKEVKF LCPLCMRSRR PRLETILSLL VSLQKLPVRL PEGEALQCLT 
      1260       1270       1280       1290       1300
ERAMSWQDRA RQALATDELS SALAKLSVLS QRMVEQAARE KTEKIISAEL 
      1310       1320       1330       1340       1350
QKAAANPDLQ GHLPSFQQSA FNRVVSSVSS SPRQTMDYDD EETDSDEDIR 
      1360       1370       1380       1390       1400
ETYGYDMKDT ASVKSSSSLE PNLFCDEEIP IKSEEVVTHM WTAPSFCAEH 
      1410       1420       1430       1440       1450
AYSSASKSCS QGSSTPRKQP RKSPLVPRSL EPPVLELSPG AKAQLEELMM 
      1460       1470       1480       1490       1500
VGDLLEVSLD ETQHIWRILQ ATHPPSEDRF LHIMEDDSME EKPLKVKGKD 
      1510       1520       1530       1540       1550
SSEKKRKRKL EKVEQLFGEG KQKSKELKKM DKPRKKKLKL GADKSKELNK 
      1560       1570       1580       1590       1600
LAKKLAKEEE RKKKKEKAAA AKVELVKEST EKKREKKVLD IPSKYDWSGA 
      1610       1620       1630       1640       1650
EESDDENAVC AAQNCQRPCK DKVDWVQCDG GCDEWFHQVC VGVSPEMAEN 
      1660       1670       1680       1690
EDYICINCAK KQGPVSPGPA PPPSFIMSYK LPMEDLKETS

Length:1,690

Mass (Da):192,095

Last modified:November 25, 2008 - v3

Checksum:ⁱFCF6DC22DEF001DF

Isoform 2 (identifier: P29375-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1623-1690: VDWVQCDGGC...LPMEDLKETS → GVVFVTEEERDKKY

« Hide

        10         20         30         40         50
MAGVGPGGYA AEFVPPPECP VFEPSWEEFT DPLSFIGRIR PLAEKTGICK 
        60         70         80         90        100
IRPPKDWQPP FACEVKSFRF TPRVQRLNEL EAMTRVRLDF LDQLAKFWEL 
       110        120        130        140        150
QGSTLKIPVV ERKILDLYAL SKIVASKGGF EMVTKEKKWS KVGSRLGYLP 
       160        170        180        190        200
GKGTGSLLKS HYERILYPYE LFQSGVSLMG VQMPNLDLKE KVEPEVLSTD 
       210        220        230        240        250
TQTSPEPGTR MNILPKRTRR VKTQSESGDV SRNTELKKLQ IFGAGPKVVG 
       260        270        280        290        300
LAMGTKDKED EVTRRRKVTN RSDAFNMQMR QRKGTLSVNF VDLYVCMFCG 
       310        320        330        340        350
RGNNEDKLLL CDGCDDSYHT FCLIPPLPDV PKGDWRCPKC VAEECSKPRE 
       360        370        380        390        400
AFGFEQAVRE YTLQSFGEMA DNFKSDYFNM PVHMVPTELV EKEFWRLVSS 
       410        420        430        440        450
IEEDVIVEYG ADISSKDFGS GFPVKDGRRK ILPEEEEYAL SGWNLNNMPV 
       460        470        480        490        500
LEQSVLAHIN VDISGMKVPW LYVGMCFSSF CWHIEDHWSY SINYLHWGEP 
       510        520        530        540        550
KTWYGVPSHA AEQLEEVMRE LAPELFESQP DLLHQLVTIM NPNVLMEHGV 
       560        570        580        590        600
PVYRTNQCAG EFVVTFPRAY HSGFNQGYNF AEAVNFCTAD WLPIGRQCVN 
       610        620        630        640        650
HYRRLRRHCV FSHEELIFKM AADPECLDVG LAAMVCKELT LMTEEETRLR 
       660        670        680        690        700
ESVVQMGVLM SEEEVFELVP DDERQCSACR TTCFLSALTC SCNPERLVCL 
       710        720        730        740        750
YHPTDLCPCP MQKKCLRYRY PLEDLPSLLY GVKVRAQSYD TWVSRVTEAL 
       760        770        780        790        800
SANFNHKKDL IELRVMLEDA EDRKYPENDL FRKLRDAVKE AETCASVAQL 
       810        820        830        840        850
LLSKKQKHRQ SPDSGRTRTK LTVEELKAFV QQLFSLPCVI SQARQVKNLL 
       860        870        880        890        900
DDVEEFHERA QEAMMDETPD SSKLQMLIDM GSSLYVELPE LPRLKQELQQ 
       910        920        930        940        950
ARWLDEVRLT LSDPQQVTLD VMKKLIDSGV GLAPHHAVEK AMAELQELLT 
       960        970        980        990       1000
VSERWEEKAK VCLQARPRHS VASLESIVNE AKNIPAFLPN VLSLKEALQK 
      1010       1020       1030       1040       1050
AREWTAKVEA IQSGSNYAYL EQLESLSAKG RPIPVRLEAL PQVESQVAAA 
      1060       1070       1080       1090       1100
RAWRERTGRT FLKKNSSHTL LQVLSPRTDI GVYGSGKNRR KKVKELIEKE 
      1110       1120       1130       1140       1150
KEKDLDLEPL SDLEEGLEET RDTAMVVAVF KEREQKEIEA MHSLRAANLA 
      1160       1170       1180       1190       1200
KMTMVDRIEE VKFCICRKTA SGFMLQCELC KDWFHNSCVP LPKSSSQKKG 
      1210       1220       1230       1240       1250
SSWQAKEVKF LCPLCMRSRR PRLETILSLL VSLQKLPVRL PEGEALQCLT 
      1260       1270       1280       1290       1300
ERAMSWQDRA RQALATDELS SALAKLSVLS QRMVEQAARE KTEKIISAEL 
      1310       1320       1330       1340       1350
QKAAANPDLQ GHLPSFQQSA FNRVVSSVSS SPRQTMDYDD EETDSDEDIR 
      1360       1370       1380       1390       1400
ETYGYDMKDT ASVKSSSSLE PNLFCDEEIP IKSEEVVTHM WTAPSFCAEH 
      1410       1420       1430       1440       1450
AYSSASKSCS QGSSTPRKQP RKSPLVPRSL EPPVLELSPG AKAQLEELMM 
      1460       1470       1480       1490       1500
VGDLLEVSLD ETQHIWRILQ ATHPPSEDRF LHIMEDDSME EKPLKVKGKD 
      1510       1520       1530       1540       1550
SSEKKRKRKL EKVEQLFGEG KQKSKELKKM DKPRKKKLKL GADKSKELNK 
      1560       1570       1580       1590       1600
LAKKLAKEEE RKKKKEKAAA AKVELVKEST EKKREKKVLD IPSKYDWSGA 
      1610       1620       1630 
EESDDENAVC AAQNCQRPCK DKGVVFVTEE ERDKKY

Show »

Length:1,636

Mass (Da):186,289

Checksum:ⁱF308F907C2F899E0

Computationally mapped potential isoform sequencesⁱ

There are 4 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

E7EV89	E7EV89_HUMAN	Lysine-specific demethylase 5A Lysine-specific demethylase 5A	KDM5A	715	Annotation score:
F5GZR8	F5GZR8_HUMAN	Lysine-specific demethylase 5A Lysine-specific demethylase 5A	KDM5A	131	Annotation score:
F5H322	F5H322_HUMAN	Lysine-specific demethylase 5A Lysine-specific demethylase 5A	KDM5A	122	Annotation score:
F5GZ99	F5GZ99_HUMAN	Lysine-specific demethylase 5A Lysine-specific demethylase 5A	KDM5A	126	Annotation score:

Sequence cautionⁱ

The sequence AAB28544 differs from that shown. Reason: Frameshift at several positions.Curated

The sequence BAE06081 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	1411	Q → QVFFGK in AAB28544 (PubMed:8414517).Curated	1
Sequence conflictⁱ	1547	E → K in AAB28544 (PubMed:8414517).Curated	1
Sequence conflictⁱ	1612 – 1614	AQN → EPD in AAB28544 (PubMed:8414517).Curated	3

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_032984	865	M → T. Corresponds to variant dbSNP:rs11062385Ensembl.		1
Natural variantⁱVAR_032985	1190	P → A. Corresponds to variant dbSNP:rs2229353Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_035746	1623 – 1690	VDWVQ…LKETS → GVVFVTEEERDKKY in isoform 2. 1 PublicationAdd BLAST		68

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	S66431 mRNA Translation: AAB28544.1 Frameshift. AB209999 mRNA Translation: BAE06081.1 Different initiation. AC005844 Genomic DNA No translation available. AC007406 Genomic DNA No translation available. BC048307 mRNA Translation: AAH48307.1 Different termination. BC053893 mRNA Translation: AAH53893.1 Different termination. BC110916 mRNA Translation: AAI10917.1 Different termination.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS41736.1 [P29375-1]
PIRⁱ	I78879
NCBI Reference Sequences More...RefSeqⁱ	NP_001036068.1, NM_001042603.2 [P29375-1]
UniGeneⁱ	Hs.76272

Genome annotation databases

Ensemblⁱ	ENST00000399788; ENSP00000382688; ENSG00000073614 [P29375-1]
GeneIDⁱ	5927
KEGGⁱ	hsa:5927
UCSC genome browser More...UCSCⁱ	uc001qif.3 human [P29375-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P29375	Lysine-specific demethylase 5A		MOUSE		1690	UniRef90_P29375
Uncharacterized protein		PONAB		1729
Uncharacterized protein		RABIT		1715
Uncharacterized protein		MACMU		1713
Lysine demethylase 5A		SHEEP		1694
+215

Protein	Similar proteins		Species	Score	Length	Source
P29375	Lysine-specific demethylase 5A		MOUSE		1690	UniRef50_P29375
Uncharacterized protein		PONAB		1729
Uncharacterized protein		RABIT		1715
Uncharacterized protein		MACMU		1713
lysine-specific demethylase 5A		URSMA		1694
+542

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	S66431 mRNA Translation: AAB28544.1 Frameshift. AB209999 mRNA Translation: BAE06081.1 Different initiation. AC005844 Genomic DNA No translation available. AC007406 Genomic DNA No translation available. BC048307 mRNA Translation: AAH48307.1 Different termination. BC053893 mRNA Translation: AAH53893.1 Different termination. BC110916 mRNA Translation: AAI10917.1 Different termination.
CCDSⁱ	CCDS41736.1 [P29375-1]
PIRⁱ	I78879
RefSeqⁱ	NP_001036068.1, NM_001042603.2 [P29375-1]
UniGeneⁱ	Hs.76272

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2JXJ	NMR	-	A	85-175	[»]
	2KGG	NMR	-	A	1609-1659	[»]
	2KGI	NMR	-	A	1609-1659	[»]
	3GL6	X-ray	1.90	A	1609-1659	[»]
	5C11	X-ray	2.80	A	1609-1659	[»]
	5CEH	X-ray	3.14	A	12-797	[»]
	5E6H	X-ray	2.24	A	1-87	[»]
				A	348-588	[»]
	5ISL	X-ray	1.69	A	1-87	[»]
				A	348-588	[»]
	5IVB	X-ray	1.39	A	1-87	[»]
				A	348-588	[»]
	5IVC	X-ray	1.57	A	1-87	[»]
				A	348-588	[»]
	5IVE	X-ray	1.78	A	1-87	[»]
				A	348-588	[»]
	5IVF	X-ray	1.68	A	1-87	[»]
				A	348-588	[»]
	5IVJ	X-ray	1.57	A	1-87	[»]
				A	348-588	[»]
	5IVV	X-ray	1.85	A	1-87	[»]
				A	348-588	[»]
	5IVY	X-ray	1.45	A	1-87	[»]
				A	348-588	[»]
	5IW0	X-ray	1.63	A	1-87	[»]
				A	348-588	[»]
	5IWF	X-ray	2.29	A	1-87	[»]
				A	348-588	[»]
	5K4L	X-ray	3.18	A/B	12-797	[»]
	5V9P	X-ray	3.00	A	12-797	[»]
	5V9T	X-ray	3.05	A/B	12-797	[»]
	6BGU	X-ray	1.68	A	1-588	[»]
	6BGV	X-ray	1.59	A	1-588	[»]
	6BGW	X-ray	1.64	A	1-588	[»]
	6BGX	X-ray	1.88	A	1-588	[»]
	6BGY	X-ray	1.22	A	1-588	[»]
	6BGZ	X-ray	1.69	A	1-588	[»]
	6BH0	X-ray	1.99	A	1-588	[»]
	6BH1	X-ray	1.93	A	1-588	[»]
	6BH2	X-ray	1.45	A	1-588	[»]
	6BH3	X-ray	1.70	A	1-588	[»]
	6BH4	X-ray	2.05	A	1-588	[»]
	6BH5	X-ray	1.65	A	1-588	[»]
ProteinModelPortalⁱ	P29375
SMRⁱ	P29375
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	111862, 30 interactors
DIPⁱ	DIP-472N
IntActⁱ	P29375, 11 interactors
MINTⁱ	P29375
STRINGⁱ	9606.ENSP00000382688

Chemistry databases

BindingDBⁱ	P29375
ChEMBLⁱ	CHEMBL2424504
GuidetoPHARMACOLOGYⁱ	2680

PTM databases

iPTMnetⁱ	P29375
PhosphoSitePlusⁱ	P29375
SwissPalmⁱ	P29375

Polymorphism and mutation databases

BioMutaⁱ	KDM5A
DMDMⁱ	215274124

Proteomic databases

EPDⁱ	P29375
MaxQBⁱ	P29375
PaxDbⁱ	P29375
PeptideAtlasⁱ	P29375
PRIDEⁱ	P29375
ProteomicsDBⁱ	54559 54560 [P29375-2]

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000399788; ENSP00000382688; ENSG00000073614 [P29375-1]
GeneIDⁱ	5927
KEGGⁱ	hsa:5927
UCSCⁱ	uc001qif.3 human [P29375-1]

Organism-specific databases

CTDⁱ	5927
DisGeNETⁱ	5927
EuPathDBⁱ	HostDB:ENSG00000073614.11
GeneCardsⁱ	KDM5A
H-InvDBⁱ	HIX0010308
HGNCⁱ	HGNC:9886 KDM5A
HPAⁱ	HPA006201
MIMⁱ	180202 gene
neXtProtⁱ	NX_P29375
OpenTargetsⁱ	ENSG00000073614
PharmGKBⁱ	PA34250
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1246 Eukaryota ENOG410XR9J LUCA
GeneTreeⁱ	ENSGT00530000063118
HOGENOMⁱ	HOG000290719
InParanoidⁱ	P29375
KOⁱ	K11446
OMAⁱ	PICDWRV
PhylomeDBⁱ	P29375
TreeFamⁱ	TF106476

Enzyme and pathway databases

Reactomeⁱ	R-HSA-3214842 HDMs demethylate histones
SIGNORⁱ	P29375

Miscellaneous databases

ChiTaRSⁱ	KDM5A human
EvolutionaryTraceⁱ	P29375
GeneWikiⁱ	JARID1A
GenomeRNAiⁱ	5927
Protein Ontology More...PROⁱ	PR:P29375
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000073614 Expressed in 244 organ(s), highest expression level in peritoneum
CleanExⁱ	HS_JARID1A HS_RBP2
ExpressionAtlasⁱ	P29375 baseline and differential
Genevisibleⁱ	P29375 HS

Family and domain databases

Gene3Dⁱ	1.10.150.60, 1 hit 3.30.40.10, 2 hits
InterProⁱ	View protein in InterPro IPR001606 ARID_dom IPR036431 ARID_dom_sf 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
Pfamⁱ	View protein in Pfam PF01388 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
SMARTⁱ	View protein in SMART SM00501 BRIGHT, 1 hit SM00558 JmjC, 1 hit SM00545 JmjN, 1 hit SM00249 PHD, 3 hits
SUPFAMⁱ	SSF46774 SSF46774, 1 hit SSF57903 SSF57903, 3 hits
PROSITEⁱ	View 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, 3 hits
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	KDM5A_HUMAN
Accessionⁱ	P29375Primary (citable) accession number: P29375 Secondary accession number(s): A8MV76, Q4LE72, Q86XZ1
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
	Last sequence update:	November 25, 2008
	Last modified:	November 7, 2018
	This is version 187 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 12
Human chromosome 12: entries, gene names and cross-references to MIM

UniProtKB

UniParc

Help

UniRef

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Supporting data

UniProtKB - P29375 (KDM5A_HUMAN)

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Lysine-specific demethylase 5A

KDM5A

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Motif

Compositional bias

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

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Functionⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ