UHRF1

Functionⁱ

Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. Plays a role in DNA repair by cooperating with UHRF1 to ensure recruitment of FANCD2 to interstrand cross-links (ICLs) leading to FANCD2 activation.

10 Publications

Catalytic activityⁱ

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. EC:2.3.2.27

Pathwayⁱ: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	316	Histone H3K4me0 binding	1
Siteⁱ	327	Histone H3R2me0 binding	1
Siteⁱ	330	Histone H3R2me0 binding	1
Binding siteⁱ	469	5-methylcytosine residue	1
Siteⁱ	479	Required to confer preferential recognition of cytosine over thymine	1
Siteⁱ	489	Required to discriminate between hemimethylated DNA versus symmetrically methylated DNA	1
Siteⁱ	491	Required for affinity and specificity for 5-mCpG sequence	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	310 – 366	PHD-typePROSITE-ProRule annotationAdd BLAST		57
Zinc fingerⁱ	724 – 763	RING-typePROSITE-ProRule annotationAdd BLAST		40

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Chromatin regulator, DNA-binding, Repressor, Transferase
Biological process	Cell cycle, DNA damage, DNA repair, Transcription, Transcription regulation, Ubl conjugation pathway
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

PathwayCommonsⁱ	Q96T88
Reactomeⁱ	R-HSA-5334118, DNA methylation
SignaLinkⁱ	Q96T88
SIGNORⁱ	Q96T88
UniPathwayⁱ	UPA00143

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: E3 ubiquitin-protein ligase UHRF1 (EC:2.3.2.27) Alternative name(s): Inverted CCAAT box-binding protein of 90 kDa Nuclear protein 95 Nuclear zinc finger protein Np95 Short name: HuNp95 Short name: hNp95 RING finger protein 106 RING-type E3 ubiquitin transferase UHRF1 Transcription factor ICBP90 Ubiquitin-like PHD and RING finger domain-containing protein 1 Short name: hUHRF1 Ubiquitin-like-containing PHD and RING finger domains protein 1
Gene namesⁱ	Name:UHRF1 Synonyms:ICBP90, NP95, RNF106
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 19

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:12556, UHRF1
MIMⁱ	607990, gene
neXtProtⁱ	NX_Q96T88
VEuPathDBⁱ	HostDB:ENSG00000276043

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Defects in UHRF1 may be a cause of cancers. Overexpressed in many different forms of human cancers, including bladder, breast, cervical, colorectal and prostate cancers, as well as pancreatic adenocarcinomas, rhabdomyosarcomas and gliomas. Plays an important role in the correlation of histone modification and gene silencing in cancer progression. Expression is associated with a poor prognosis in patients with various cancers, suggesting that it participates in cancer progression.

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	142	D → A: Impaired binding to histone H3 without affecting the protein folding; when associated with A-153. 1 Publication	1
Mutagenesisⁱ	145	D → A: Impaired binding to histone H3. 1 Publication	1
Mutagenesisⁱ	152	F → A: Impaired binding to histone H3. 1 Publication	1
Mutagenesisⁱ	153	E → A: Impaired binding to histone H3 without affecting the protein folding; when associated with A-142. 1 Publication	1
Mutagenesisⁱ	188	Y → A: Impaired binding to histone H3. 2 Publications	1
Mutagenesisⁱ	190	D → A: Slightly impaired binding to histone H3. 1 Publication	1
Mutagenesisⁱ	191	Y → A: Impaired binding to histone H3. 1 Publication	1
Mutagenesisⁱ	295 – 296	RR → AA: Disrupts the simultaneous binding to H3R2me0 and H3K9me3. 1 Publication	2
Mutagenesisⁱ	298	S → A: Diminishes phosphorylation by PKA. 1 Publication	1
Mutagenesisⁱ	330	Q → A or K: Does not affect ability to bind histone H3 peptide. 1 Publication	1
Mutagenesisⁱ	334 – 335	DE → AA: Abolishes binding to histone H3. 1 Publication	2
Mutagenesisⁱ	334	D → A: Impaired binding to histone H3. 3 Publications	1
Mutagenesisⁱ	337	D → A: Impaired binding to histone H3. 3 Publications	1
Mutagenesisⁱ	433	R → A: Does not affect ability to bind DNA. 1 Publication	1
Mutagenesisⁱ	443	R → A: Decreased ability to bind DNA. 1 Publication	1
Mutagenesisⁱ	448	G → D: Decreased affinity for DNA. 1 Publication	1
Mutagenesisⁱ	466	Y → G: Decreased ability to bind DNA. 1 Publication	1
Mutagenesisⁱ	469	D → G: Abolishes ability to bind hemimethylated DNA. 1 Publication	1
Mutagenesisⁱ	489	N → A: Abolishes specificity to hemimethylated DNA. 1 Publication	1
Mutagenesisⁱ	491	R → A: Decreased binding to methylated DNA but does not affect ability to bind DNA. 2 Publications	1
Mutagenesisⁱ	639	S → A: Prevents phosphorylation by CDK1 during M phase, leading to increased stability. 1 Publication	1
Mutagenesisⁱ	639	S → D: Mimics phosphorylation; impaired interaction with USP7, leading to decreased stability. 1 Publication	1
Mutagenesisⁱ	651	S → A: No effect on in vitro phosphorylation by PKA. 1 Publication	1
Mutagenesisⁱ	666	S → A: No effect on in vitro phosphorylation by PKA. 1 Publication	1
Mutagenesisⁱ	741	H → A: Abolishes E3 ubiquitin-protein ligase activity. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	29128
Open Targets More...OpenTargetsⁱ	ENSG00000276043
PharmGKBⁱ	PA37196

Miscellaneous databases

Pharosⁱ	Q96T88, Tbio

Pharosⁱ

Q96T88, Tbio

Chemistry databases

ChEMBLⁱ	CHEMBL2424510

ChEMBLⁱ

CHEMBL2424510

Genetic variation databases

BioMutaⁱ	UHRF1
DMDMⁱ	67462077

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000056144	1 – 793	E3 ubiquitin-protein ligase UHRF1Add BLAST		793

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	76	PhosphoserineCombined sources	1
Modified residueⁱ	91	PhosphoserineCombined sources	1
Modified residueⁱ	95	PhosphoserineBy similarity	1
Modified residueⁱ	165	PhosphoserineBy similarity	1
Cross-linkⁱ	279	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	287	PhosphoserineCombined sources	1
Modified residueⁱ	298	Phosphoserine; by PKA2 Publications	1
Modified residueⁱ	368	PhosphoserineCombined sources	1
Cross-linkⁱ	385	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	399	N6-acetyllysineCombined sources	1
Modified residueⁱ	546	N6-acetyllysine; alternateCombined sources	1
Cross-linkⁱ	546	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residueⁱ	639	Phosphoserine; by CDK1Combined sources1 Publication	1
Modified residueⁱ	651	PhosphoserineCombined sources	1
Cross-linkⁱ	670	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	707	PhosphoserineCombined sources	1
Modified residueⁱ	709	PhosphoserineCombined sources	1

Post-translational modificationⁱ

Phosphorylation at Ser-298 of the linker region decreases the binding to H3K9me3. Phosphorylation at Ser-639 by CDK1 during M phase impairs interaction with USP7, preventing deubiquitination and leading to degradation by the proteasome.3 Publications

Ubiquitinated; which leads to proteasomal degradation. Autoubiquitinated; interaction with USP7 leads to deubiquitination and prevents degradation. Ubiquitination and degradation takes place during M phase, when phosphorylation at Ser-639 prevents interaction with USP7 and subsequent deubiquitination. Polyubiquitination may be stimulated by DNA damage.4 Publications

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	Q96T88
jPOSTⁱ	Q96T88
MassIVEⁱ	Q96T88
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q96T88
PeptideAtlas More...PeptideAtlasⁱ	Q96T88
PRIDEⁱ	Q96T88
ProteomicsDBⁱ	78215 [Q96T88-1]

PTM databases

GlyGenⁱ	Q96T88, 1 site, 1 O-linked glycan (1 site)
iPTMnetⁱ	Q96T88
PhosphoSitePlusⁱ	Q96T88
SwissPalmⁱ	Q96T88

Expressionⁱ

Tissue specificityⁱ

Expressed in thymus, bone marrow, testis, lung and heart. Overexpressed in breast cancer.3 Publications

Developmental stageⁱ

Expressed in fetal thymus, liver and kidney.1 Publication

Inductionⁱ

Up-regulated in proliferating cells, and down-regulated in quiescent cells. Down-regulated upon adriamycin-induced DNA damage, in a p53/TP53 and CDKN1A-dependent way. Induced by E2F1 transcription factor.4 Publications

Gene expression databases

Bgeeⁱ	ENSG00000276043, Expressed in oocyte and 170 other tissues
ExpressionAtlasⁱ	Q96T88, baseline and differential
Genevisibleⁱ	Q96T88, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000276043, Tissue enriched (lymphoid)

HPAⁱ

ENSG00000276043, Tissue enriched (lymphoid)

Interactionⁱ

Subunit structureⁱ

Interacts with DNMT3A and DNMT3B (By similarity).

Interacts with DNMT1; the interaction is direct.

Interacts with USP7; leading to its deubiquitination.

Interacts with histone H3.

Interacts with HDAC1, but not with HDAC2.

Interacts with UHRF1BP1.

Interacts with PML.

Interacts with EHMT2. Binds hemimethylated CpG containing oligonucleotides.

Interacts with ZNF263; recruited to the SIX3 promoter along with other proteins involved in chromatin modification and transcriptional corepression where it contributes to transcriptional repression (PubMed:32051553).

Interacts with UHRF2 (PubMed:30335751).

Interacts with FANCD2 (PubMed:30335751).

By similarity12 Publications

Binary interactionsⁱ

Hide details

Q96T88

With	#Exp.	IntAct
DNMT1 [P26358]	12	EBI-1548946,EBI-719459
DNMT3A [Q9Y6K1]	7	EBI-1548946,EBI-923653
DNMT3B [Q9UBC3]	7	EBI-1548946,EBI-80125

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	118893, 123 interactors
IntActⁱ	Q96T88, 36 interactors
Molecular INTeraction database More...MINTⁱ	Q96T88
STRINGⁱ	9606.ENSP00000479617

Chemistry databases

BindingDBⁱ

Q96T88

Miscellaneous databases

RNActⁱ	Q96T88, protein

RNActⁱ

Q96T88, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	1 – 7	Combined sources	7
Beta strandⁱ	13 – 19	Combined sources	7
Helixⁱ	25 – 36	Combined sources	12
Helixⁱ	40 – 42	Combined sources	3
Beta strandⁱ	43 – 47	Combined sources	5
Turnⁱ	58 – 62	Combined sources	5
Beta strandⁱ	68 – 73	Combined sources	6
Beta strandⁱ	126 – 128	Combined sources	3
Beta strandⁱ	130 – 132	Combined sources	3
Beta strandⁱ	133 – 135	Combined sources	3
Beta strandⁱ	140 – 144	Combined sources	5
Turnⁱ	146 – 148	Combined sources	3
Beta strandⁱ	151 – 162	Combined sources	12
Beta strandⁱ	164 – 167	Combined sources	4
Beta strandⁱ	173 – 175	Combined sources	3
Helixⁱ	179 – 181	Combined sources	3
Beta strandⁱ	183 – 190	Combined sources	8
Helixⁱ	192 – 194	Combined sources	3
Beta strandⁱ	196 – 200	Combined sources	5
Helixⁱ	201 – 203	Combined sources	3
Beta strandⁱ	204 – 206	Combined sources	3
Beta strandⁱ	210 – 212	Combined sources	3
Helixⁱ	214 – 216	Combined sources	3
Beta strandⁱ	222 – 227	Combined sources	6
Beta strandⁱ	229 – 231	Combined sources	3
Beta strandⁱ	237 – 248	Combined sources	12
Beta strandⁱ	253 – 260	Combined sources	8
Beta strandⁱ	266 – 270	Combined sources	5
Helixⁱ	274 – 276	Combined sources	3
Beta strandⁱ	277 – 279	Combined sources	3
Beta strandⁱ	283 – 286	Combined sources	4
Turnⁱ	303 – 307	Combined sources	5
Beta strandⁱ	309 – 311	Combined sources	3
Turnⁱ	314 – 316	Combined sources	3
Turnⁱ	319 – 321	Combined sources	3
Beta strandⁱ	323 – 325	Combined sources	3
Helixⁱ	327 – 329	Combined sources	3
Beta strandⁱ	330 – 332	Combined sources	3
Turnⁱ	334 – 336	Combined sources	3
Beta strandⁱ	339 – 341	Combined sources	3
Helixⁱ	342 – 344	Combined sources	3
Beta strandⁱ	345 – 347	Combined sources	3
Beta strandⁱ	354 – 356	Combined sources	3
Turnⁱ	361 – 363	Combined sources	3
Beta strandⁱ	417 – 419	Combined sources	3
Beta strandⁱ	429 – 432	Combined sources	4
Helixⁱ	433 – 438	Combined sources	6
Turnⁱ	439 – 442	Combined sources	4
Beta strandⁱ	448 – 452	Combined sources	5
Turnⁱ	453 – 455	Combined sources	3
Beta strandⁱ	456 – 462	Combined sources	7
Beta strandⁱ	473 – 479	Combined sources	7
Turnⁱ	487 – 489	Combined sources	3
Helixⁱ	503 – 511	Combined sources	9
Beta strandⁱ	512 – 514	Combined sources	3
Turnⁱ	518 – 520	Combined sources	3
Helixⁱ	527 – 529	Combined sources	3
Beta strandⁱ	533 – 538	Combined sources	6
Helixⁱ	539 – 544	Combined sources	6
Beta strandⁱ	546 – 548	Combined sources	3
Beta strandⁱ	550 – 568	Combined sources	19
Beta strandⁱ	572 – 582	Combined sources	11
Helixⁱ	592 – 601	Combined sources	10
Helixⁱ	611 – 617	Combined sources	7
Helixⁱ	678 – 686	Combined sources	9
Helixⁱ	688 – 690	Combined sources	3
Helixⁱ	691 – 699	Combined sources	9
Beta strandⁱ	706 – 708	Combined sources	3
Helixⁱ	710 – 721	Combined sources	12
Turnⁱ	725 – 727	Combined sources	3
Beta strandⁱ	728 – 730	Combined sources	3
Beta strandⁱ	732 – 736	Combined sources	5
Beta strandⁱ	742 – 744	Combined sources	3
Helixⁱ	745 – 753	Combined sources	9
Turnⁱ	760 – 762	Combined sources	3
Helixⁱ	776 – 785	Combined sources	10
Turnⁱ	787 – 792	Combined sources	6

Show more details

3D structure databases

BMRBⁱ	Q96T88
SASBDBⁱ	Q96T88
SMRⁱ	Q96T88
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q96T88

EvolutionaryTraceⁱ

Q96T88

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	1 – 78	Ubiquitin-likePROSITE-ProRule annotationAdd BLAST		78
Domainⁱ	419 – 582	YDGPROSITE-ProRule annotationAdd BLAST		164

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	82 – 124	DisorderedSequence analysisAdd BLAST	43
Regionⁱ	133 – 209	Tudor-like 1Add BLAST	77
Regionⁱ	216 – 283	Tudor-like 2Add BLAST	68
Regionⁱ	296 – 301	Linker	6
Regionⁱ	333 – 337	Histone H3R2me0 binding	5
Regionⁱ	353 – 355	Histone H3R2me0 binding	3
Regionⁱ	445 – 446	Required to promote base flippingBy similarity	2
Regionⁱ	463 – 464	5-methylcytosine residue binding	2
Regionⁱ	466 – 469	Required for formation of a 5-methylcytosine-binding pocket	4
Regionⁱ	478 – 481	Required for formation of a 5-methylcytosine-binding pocket	4
Regionⁱ	618 – 673	DisorderedSequence analysisAdd BLAST	56

Compositional bias

Feature key	Position(s)	DescriptionActions	Length
Compositional biasⁱ	94 – 108	Polar residuesSequence analysisAdd BLAST	15
Compositional biasⁱ	109 – 124	Basic and acidic residuesSequence analysisAdd BLAST	16
Compositional biasⁱ	618 – 635	Basic and acidic residuesSequence analysisAdd BLAST	18

Domainⁱ

The tudor-like regions specifically recognize and bind histone H3 unmethylated at 'Arg-2' (H3R2me0), while the PHD-type zinc finger specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3). The tudor-like regions simultaneously recognizes H3K9me3 through a conserved aromatic cage in the first tudor-like subdomain and unmodified H3K4 (H3K4me0) within a groove between the tandem subdomains (PubMed:21489993, PubMed:21777816 and PubMed:22100450). The linker region plays a role in the formation of a histone H3-binding hole between the reader modules formed by the tudor-like regions and the PHD-type zinc finger by making extended contacts with the tandem tudor-like regions (PubMed:22837395).1 Publication

The YDG domain (also named SRA domain) specifically recognizes and binds hemimethylated DNA at replication forks (DNA that is only methylated on the mother strand of replicating DNA) (PubMed:17673620). It contains a binding pocket that accommodates the 5-methylcytosine that is flipped out of the duplex DNA. 2 specialized loops reach through the resulting gap in the DNA from both the major and the minor grooves to read the other 3 bases of the CpG duplex. The major groove loop confers both specificity for the CpG dinucleotide and discrimination against methylation of deoxycytidine of the complementary strand (PubMed:18772889). The YDG domain also recognizes and binds 5-hydroxymethylcytosine (5hmC) (PubMed:21731699).3 Publications

The RING finger is required for ubiquitin ligase activity.By similarity

Zinc finger

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	310 – 366	PHD-typePROSITE-ProRule annotationAdd BLAST		57
Zinc fingerⁱ	724 – 763	RING-typePROSITE-ProRule annotationAdd BLAST		40

Keywords - Domainⁱ

Repeat, Zinc-finger

Phylogenomic databases

eggNOGⁱ	ENOG502QRDQ, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000008296
HOGENOMⁱ	CLU_022357_0_0_1
InParanoidⁱ	Q96T88
Database of Orthologous Groups More...OrthoDBⁱ	705927at2759
PhylomeDBⁱ	Q96T88

Family and domain databases

Database of protein disorder More...DisProtⁱ	DP01651
Gene3Dⁱ	2.30.280.10, 1 hit 3.30.40.10, 1 hit
IDEALⁱ	IID00327
InterProⁱ	View protein in InterPro IPR015947, PUA-like_sf IPR036987, SRA-YDG_sf IPR003105, SRA_YDG IPR021991, TTD_dom IPR000626, Ubiquitin-like_dom IPR029071, Ubiquitin-like_domsf IPR011011, Znf_FYVE_PHD IPR001965, Znf_PHD IPR019787, Znf_PHD-finger IPR001841, Znf_RING IPR013083, Znf_RING/FYVE/PHD IPR017907, Znf_RING_CS
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00628, PHD, 1 hit PF02182, SAD_SRA, 1 hit PF12148, TTD, 1 hit PF00240, ubiquitin, 1 hit
SMARTⁱ	View protein in SMART SM00249, PHD, 1 hit SM00184, RING, 2 hits SM00466, SRA, 1 hit SM00213, UBQ, 1 hit
SUPFAMⁱ	SSF54236, SSF54236, 1 hit SSF57903, SSF57903, 1 hit SSF88697, SSF88697, 1 hit
PROSITEⁱ	View protein in PROSITE PS50053, UBIQUITIN_2, 1 hit PS51015, YDG, 1 hit PS01359, ZF_PHD_1, 1 hit PS50016, ZF_PHD_2, 1 hit PS00518, ZF_RING_1, 1 hit PS50089, ZF_RING_2, 2 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 3 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q96T88-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ 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
MWIQVRTMDG RQTHTVDSLS RLTKVEELRR KIQELFHVEP GLQRLFYRGK 
        60         70         80         90        100
QMEDGHTLFD YEVRLNDTIQ LLVRQSLVLP HSTKERDSEL SDTDSGCCLG 
       110        120        130        140        150
QSESDKSSTH GEAAAETDSR PADEDMWDET ELGLYKVNEY VDARDTNMGA 
       160        170        180        190        200
WFEAQVVRVT RKAPSRDEPC SSTSRPALEE DVIYHVKYDD YPENGVVQMN 
       210        220        230        240        250
SRDVRARART IIKWQDLEVG QVVMLNYNPD NPKERGFWYD AEISRKRETR 
       260        270        280        290        300
TARELYANVV LGDDSLNDCR IIFVDEVFKI ERPGEGSPMV DNPMRRKSGP 
       310        320        330        340        350
SCKHCKDDVN RLCRVCACHL CGGRQDPDKQ LMCDECDMAF HIYCLDPPLS 
       360        370        380        390        400
SVPSEDEWYC PECRNDASEV VLAGERLRES KKKAKMASAT SSSQRDWGKG 
       410        420        430        440        450
MACVGRTKEC TIVPSNHYGP IPGIPVGTMW RFRVQVSESG VHRPHVAGIH 
       460        470        480        490        500
GRSNDGAYSL VLAGGYEDDV DHGNFFTYTG SGGRDLSGNK RTAEQSCDQK 
       510        520        530        540        550
LTNTNRALAL NCFAPINDQE GAEAKDWRSG KPVRVVRNVK GGKNSKYAPA 
       560        570        580        590        600
EGNRYDGIYK VVKYWPEKGK SGFLVWRYLL RRDDDEPGPW TKEGKDRIKK 
       610        620        630        640        650
LGLTMQYPEG YLEALANRER EKENSKREEE EQQEGGFASP RTGKGKWKRK 
       660        670        680        690        700
SAGGGPSRAG SPRRTSKKTK VEPYSLTAQQ SSLIREDKSN AKLWNEVLAS 
       710        720        730        740        750
LKDRPASGSP FQLFLSKVEE TFQCICCQEL VFRPITTVCQ HNVCKDCLDR 
       760        770        780        790 
SFRAQVFSCP ACRYDLGRSY AMQVNQPLQT VLNQLFPGYG NGR

Length:793

Mass (Da):89,814

Last modified:December 1, 2001 - v1

Checksum:ⁱE65B15657525C89F

GO

Isoform 2 (identifier: Q96T88-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MGVFAVPPLSSDTM

« Hide

        10         20         30         40         50
MGVFAVPPLS SDTMWIQVRT MDGRQTHTVD SLSRLTKVEE LRRKIQELFH 
        60         70         80         90        100
VEPGLQRLFY RGKQMEDGHT LFDYEVRLND TIQLLVRQSL VLPHSTKERD 
       110        120        130        140        150
SELSDTDSGC CLGQSESDKS STHGEAAAET DSRPADEDMW DETELGLYKV 
       160        170        180        190        200
NEYVDARDTN MGAWFEAQVV RVTRKAPSRD EPCSSTSRPA LEEDVIYHVK 
       210        220        230        240        250
YDDYPENGVV QMNSRDVRAR ARTIIKWQDL EVGQVVMLNY NPDNPKERGF 
       260        270        280        290        300
WYDAEISRKR ETRTARELYA NVVLGDDSLN DCRIIFVDEV FKIERPGEGS 
       310        320        330        340        350
PMVDNPMRRK SGPSCKHCKD DVNRLCRVCA CHLCGGRQDP DKQLMCDECD 
       360        370        380        390        400
MAFHIYCLDP PLSSVPSEDE WYCPECRNDA SEVVLAGERL RESKKKAKMA 
       410        420        430        440        450
SATSSSQRDW GKGMACVGRT KECTIVPSNH YGPIPGIPVG TMWRFRVQVS 
       460        470        480        490        500
ESGVHRPHVA GIHGRSNDGA YSLVLAGGYE DDVDHGNFFT YTGSGGRDLS 
       510        520        530        540        550
GNKRTAEQSC DQKLTNTNRA LALNCFAPIN DQEGAEAKDW RSGKPVRVVR 
       560        570        580        590        600
NVKGGKNSKY APAEGNRYDG IYKVVKYWPE KGKSGFLVWR YLLRRDDDEP 
       610        620        630        640        650
GPWTKEGKDR IKKLGLTMQY PEGYLEALAN REREKENSKR EEEEQQEGGF 
       660        670        680        690        700
ASPRTGKGKW KRKSAGGGPS RAGSPRRTSK KTKVEPYSLT AQQSSLIRED 
       710        720        730        740        750
KSNAKLWNEV LASLKDRPAS GSPFQLFLSK VEETFQCICC QELVFRPITT 
       760        770        780        790        800
VCQHNVCKDC LDRSFRAQVF SCPACRYDLG RSYAMQVNQP LQTVLNQLFP 

GYGNGR

Show »

Length:806

Mass (Da):91,116

Checksum:ⁱBFE365939E846398

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

A0A087WVR3	A0A087WVR3_HUMAN	RING-type E3 ubiquitin transferase RING-type E3 ubiquitin transferase, EC 2.3.2.27	UHRF1 hCG_23497	806	Annotation score:
A0A087WTW0	A0A087WTW0_HUMAN	RING-type E3 ubiquitin transferase RING-type E3 ubiquitin transferase, EC 2.3.2.27	UHRF1	857	Annotation score:
A0A087WWG9	A0A087WWG9_HUMAN	E3 ubiquitin-protein ligase UHRF1 E3 ubiquitin-protein ligase UHRF1	UHRF1	496	Annotation score:

Sequence cautionⁱ

The sequence BAB15177 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	383	K → E in BAF82078 (PubMed:14702039).Curated	1
Sequence conflictⁱ	383	K → N in AAF28469 (PubMed:10646863).Curated	1
Sequence conflictⁱ	457	A → S in AAF28469 (PubMed:10646863).Curated	1
Sequence conflictⁱ	675	S → N in BAF82078 (PubMed:14702039).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_022554	240	D → H1 PublicationCorresponds to variant dbSNP:rs17886098Ensembl.	1
Natural variantⁱVAR_022555	379	E → K2 PublicationsCorresponds to variant dbSNP:rs17885791Ensembl.	1
Natural variantⁱVAR_022556	638	A → T2 PublicationsCorresponds to variant dbSNP:rs2307209Ensembl.	1
Natural variantⁱVAR_022557	642	T → M1 PublicationCorresponds to variant dbSNP:rs17884843Ensembl.	1
Natural variantⁱVAR_022558	713	L → F1 PublicationCorresponds to variant dbSNP:rs17883563Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_044394	1	M → MGVFAVPPLSSDTM in isoform 2. 1 Publication		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF129507 mRNA Translation: AAF28469.1 AB177623 mRNA Translation: BAF36719.1 AB177624 mRNA Translation: BAF36720.1 AB075601 mRNA Translation: BAC20576.1 AF274048 mRNA Translation: AAK55744.1 EF560733 mRNA Translation: ABQ59043.1 AK025578 mRNA Translation: BAB15177.1 Different initiation. AK289389 mRNA Translation: BAF82078.1 AK314579 mRNA Translation: BAG37156.1 AY787925 Genomic DNA Translation: AAV40831.1 AC027319 Genomic DNA No translation available. AC053467 Genomic DNA Translation: AAF64067.1 CH471139 Genomic DNA Translation: EAW69187.1 BC113875 mRNA Translation: AAI13876.2
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS74262.1 [Q96T88-2] CCDS74263.1 [Q96T88-1]
NCBI Reference Sequences More...RefSeqⁱ	NP_001041666.1, NM_001048201.2 [Q96T88-1] NP_001276979.1, NM_001290050.1 [Q96T88-1] NP_001276980.1, NM_001290051.1 [Q96T88-1] NP_001276981.1, NM_001290052.1 [Q96T88-1] NP_037414.3, NM_013282.4

Genome annotation databases

Ensemblⁱ	ENST00000612630; ENSP00000484739; ENSG00000276043 [Q96T88-1] ENST00000615884; ENSP00000478601; ENSG00000276043 [Q96T88-1] ENST00000616255; ENSP00000478348; ENSG00000276043 [Q96T88-1] ENST00000624301; ENSP00000485604; ENSG00000276043 [Q96T88-1] ENST00000650932; ENSP00000498698; ENSG00000276043 [Q96T88-1]
GeneIDⁱ	29128
KEGGⁱ	hsa:29128
UCSC genome browser More...UCSCⁱ	uc032hkj.2, human [Q96T88-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q96T88	RING-type E3 ubiquitin transferase		HUMAN		857	UniRef100_Q96T88
cDNA FLJ60383, highly similar to Ubiquitin-like PHD and RING fingerdomain-containing protein 1		HUMAN		408
+7

Protein	Similar proteins		Species	Score	Length	Source
Q96T88	RING-type E3 ubiquitin transferase		HUMAN		857	UniRef90_Q96T88
RING-type E3 ubiquitin transferase		PONAB		857
RING-type E3 ubiquitin transferase		GORGO		793
cDNA FLJ60383, highly similar to Ubiquitin-like PHD and RING fingerdomain-containing protein 1		HUMAN		408
RING-type E3 ubiquitin transferase		PONAB		793
+14

Protein	Similar proteins		Species	Score	Length	Source
Q96T88	E3 ubiquitin-protein ligase UHRF1		BOVIN		786	UniRef50_Q96T88
RING-type E3 ubiquitin transferase		HUMAN		857
RING-type E3 ubiquitin transferase		PONAB		857
RING-type E3 ubiquitin transferase		GORGO		793
RING-type E3 ubiquitin transferase		FUKDA		833
+475

Cross-referencesⁱ

Web resourcesⁱ

NIEHS-SNPs

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF129507 mRNA Translation: AAF28469.1 AB177623 mRNA Translation: BAF36719.1 AB177624 mRNA Translation: BAF36720.1 AB075601 mRNA Translation: BAC20576.1 AF274048 mRNA Translation: AAK55744.1 EF560733 mRNA Translation: ABQ59043.1 AK025578 mRNA Translation: BAB15177.1 Different initiation. AK289389 mRNA Translation: BAF82078.1 AK314579 mRNA Translation: BAG37156.1 AY787925 Genomic DNA Translation: AAV40831.1 AC027319 Genomic DNA No translation available. AC053467 Genomic DNA Translation: AAF64067.1 CH471139 Genomic DNA Translation: EAW69187.1 BC113875 mRNA Translation: AAI13876.2
CCDSⁱ	CCDS74262.1 [Q96T88-2] CCDS74263.1 [Q96T88-1]
RefSeqⁱ	NP_001041666.1, NM_001048201.2 [Q96T88-1] NP_001276979.1, NM_001290050.1 [Q96T88-1] NP_001276980.1, NM_001290051.1 [Q96T88-1] NP_001276981.1, NM_001290052.1 [Q96T88-1] NP_037414.3, NM_013282.4

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
	2FAZ	X-ray	2.00	A/B	1-76	[»]
	2L3R	NMR	-	A	126-285	[»]
	2LGG	NMR	-	A	298-366	[»]
	2LGK	NMR	-	A	298-366	[»]
	2LGL	NMR	-	A	298-366	[»]
	2PB7	X-ray	1.90	A	408-643	[»]
	3ASK	X-ray	2.90	A/B/C/D	134-367	[»]
	3ASL	X-ray	1.41	A	298-367	[»]
	3BI7	X-ray	1.70	A	414-617	[»]
	3CLZ	X-ray	2.20	A/B/C/D	414-617	[»]
	3DB3	X-ray	2.40	A	126-285	[»]
	3DB4	X-ray	2.40	A	126-285	[»]
	3DWH	X-ray	1.95	A	414-617	[»]
	3FL2	X-ray	1.75	A	672-793	[»]
	3SHB	X-ray	1.80	A	298-366	[»]
	3SOU	X-ray	1.80	A/B	298-367	[»]
	3SOW	X-ray	1.95	A/B	298-367	[»]
	3SOX	X-ray	2.65	A/B	298-367	[»]
	3T6R	X-ray	1.95	A/B	299-364	[»]
	3ZVY	X-ray	1.95	A/B	296-367	[»]
	3ZVZ	X-ray	1.45	B	314-367	[»]
	4GY5	X-ray	2.96	A/B/C/D	134-366	[»]
	4QQD	X-ray	2.28	A/B	126-285	[»]
	5C6D	X-ray	2.29	C/D	634-665	[»]
	5IAY	NMR	-	A	134-285	[»]
				B	642-657	[»]
	5XPI	X-ray	2.20	A	127-283	[»]
	5YY9	X-ray	2.65	A/B	123-285	[»]
	5YYA	X-ray	1.70	A	123-285	[»]
	6B9M	X-ray	1.68	D	638-678	[»]
	6IIW	X-ray	1.70	A	299-366	[»]
	6VCS	X-ray	1.70	A/B/E	414-617	[»]
	6VED	NMR	-	A	133-300	[»]
	6VYJ	X-ray	1.39	A	122-283	[»]
	6W92	X-ray	1.30	A	122-283	[»]
BMRBⁱ	Q96T88
SASBDBⁱ	Q96T88
SMRⁱ	Q96T88
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	118893, 123 interactors
IntActⁱ	Q96T88, 36 interactors
MINTⁱ	Q96T88
STRINGⁱ	9606.ENSP00000479617

Chemistry databases

BindingDBⁱ	Q96T88
ChEMBLⁱ	CHEMBL2424510

PTM databases

GlyGenⁱ	Q96T88, 1 site, 1 O-linked glycan (1 site)
iPTMnetⁱ	Q96T88
PhosphoSitePlusⁱ	Q96T88
SwissPalmⁱ	Q96T88

Genetic variation databases

BioMutaⁱ	UHRF1
DMDMⁱ	67462077

Proteomic databases

EPDⁱ	Q96T88
jPOSTⁱ	Q96T88
MassIVEⁱ	Q96T88
MaxQBⁱ	Q96T88
PeptideAtlasⁱ	Q96T88
PRIDEⁱ	Q96T88
ProteomicsDBⁱ	78215 [Q96T88-1]

Protocols and materials databases

Antibodypediaⁱ	72541, 397 antibodies
The DNASU plasmid repository More...DNASUⁱ	29128

Genome annotation databases

Ensemblⁱ	ENST00000612630; ENSP00000484739; ENSG00000276043 [Q96T88-1] ENST00000615884; ENSP00000478601; ENSG00000276043 [Q96T88-1] ENST00000616255; ENSP00000478348; ENSG00000276043 [Q96T88-1] ENST00000624301; ENSP00000485604; ENSG00000276043 [Q96T88-1] ENST00000650932; ENSP00000498698; ENSG00000276043 [Q96T88-1]
GeneIDⁱ	29128
KEGGⁱ	hsa:29128
UCSCⁱ	uc032hkj.2, human [Q96T88-1]

Organism-specific databases

CTDⁱ	29128
DisGeNETⁱ	29128
GeneCardsⁱ	UHRF1
HGNCⁱ	HGNC:12556, UHRF1
HPAⁱ	ENSG00000276043, Tissue enriched (lymphoid)
MIMⁱ	607990, gene
neXtProtⁱ	NX_Q96T88
OpenTargetsⁱ	ENSG00000276043
PharmGKBⁱ	PA37196
VEuPathDBⁱ	HostDB:ENSG00000276043
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG502QRDQ, Eukaryota
GeneTreeⁱ	ENSGT00390000008296
HOGENOMⁱ	CLU_022357_0_0_1
InParanoidⁱ	Q96T88
OrthoDBⁱ	705927at2759
PhylomeDBⁱ	Q96T88

Enzyme and pathway databases

UniPathwayⁱ	UPA00143
PathwayCommonsⁱ	Q96T88
Reactomeⁱ	R-HSA-5334118, DNA methylation
SignaLinkⁱ	Q96T88
SIGNORⁱ	Q96T88

Miscellaneous databases

BioGRID-ORCSⁱ	29128, 40 hits in 206 CRISPR screens
ChiTaRSⁱ	UHRF1, human
EvolutionaryTraceⁱ	Q96T88
GeneWikiⁱ	UHRF1
GenomeRNAiⁱ	29128
Pharosⁱ	Q96T88, Tbio
Protein Ontology More...PROⁱ	PR:Q96T88
RNActⁱ	Q96T88, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000276043, Expressed in oocyte and 170 other tissues
ExpressionAtlasⁱ	Q96T88, baseline and differential
Genevisibleⁱ	Q96T88, HS

Family and domain databases

DisProtⁱ	DP01651
Gene3Dⁱ	2.30.280.10, 1 hit 3.30.40.10, 1 hit
IDEALⁱ	IID00327
InterProⁱ	View protein in InterPro IPR015947, PUA-like_sf IPR036987, SRA-YDG_sf IPR003105, SRA_YDG IPR021991, TTD_dom IPR000626, Ubiquitin-like_dom IPR029071, Ubiquitin-like_domsf IPR011011, Znf_FYVE_PHD IPR001965, Znf_PHD IPR019787, Znf_PHD-finger IPR001841, Znf_RING IPR013083, Znf_RING/FYVE/PHD IPR017907, Znf_RING_CS
Pfamⁱ	View protein in Pfam PF00628, PHD, 1 hit PF02182, SAD_SRA, 1 hit PF12148, TTD, 1 hit PF00240, ubiquitin, 1 hit
SMARTⁱ	View protein in SMART SM00249, PHD, 1 hit SM00184, RING, 2 hits SM00466, SRA, 1 hit SM00213, UBQ, 1 hit
SUPFAMⁱ	SSF54236, SSF54236, 1 hit SSF57903, SSF57903, 1 hit SSF88697, SSF88697, 1 hit
PROSITEⁱ	View protein in PROSITE PS50053, UBIQUITIN_2, 1 hit PS51015, YDG, 1 hit PS01359, ZF_PHD_1, 1 hit PS50016, ZF_PHD_2, 1 hit PS00518, ZF_RING_1, 1 hit PS50089, ZF_RING_2, 2 hits
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	UHRF1_HUMAN
Accessionⁱ	Q96T88Primary (citable) accession number: Q96T88 Secondary accession number(s): A0JBR2 Q9P1U7
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
	Last sequence update:	December 1, 2001
	Last modified:	September 29, 2021
	This is version 190 of the entry and version 1 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, Reference proteome

Documents

Human chromosome 19
Human chromosome 19: entries, gene names and cross-references to MIM
Human entries with genetic variants
List of human entries with genetic variants
Human variants curated from literature reports
Index of human variants curated from literature reports
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

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UniProtKB - Q96T88 (UHRF1_HUMAN)

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E3 ubiquitin-protein ligase UHRF1

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 <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

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

Miscellaneous databases

Chemistry databases

Genetic variation 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

Q96T88

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

Miscellaneous 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

Compositional bias

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

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Proteomic databases

Protocols and materials databases

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Organism-specific databases

Phylogenomic databases

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Functionⁱ

Catalytic activityⁱ

Pathwayⁱ: protein ubiquitination

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

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ