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Protein

E3 SUMO-protein ligase ZNF451

Gene

ZNF451

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 SUMO-protein ligase; has a preference for SUMO2 and SUMO3 and facilitates UBE2I/UBC9-mediated sumoylation of target proteins (PubMed:26524493, PubMed:26524494). Plays a role in protein SUMO2 modification in response to stress caused by DNA damage and by proteasome inhibitors (in vitro). Required for MCM4 sumoylation (By similarity). Has no activity with SUMO1 (PubMed:26524493). Preferentially transfers an additional SUMO2 chain onto the SUMO2 consensus site 'Lys-11' (PubMed:26524493). Negatively regulates transcriptional activation mediated by the SMAD4 complex in response to TGF-beta signaling. Inhibits EP300-mediated acetylation of histone H3 at 'Lys-9' (PubMed:24324267). Plays a role in regulating the transcription of AR targets (PubMed:18656483).By similarity4 Publications

Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.2 Publications
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri169 – 195C2H2-type 1PROSITE-ProRule annotationAdd BLAST27
Zinc fingeri253 – 277C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri315 – 337C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri362 – 386C2H2-type 4PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri498 – 521C2H2-type 5PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri531 – 554C2H2-type 6PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri606 – 631C2H2-type 7; atypicalPROSITE-ProRule annotationAdd BLAST26
Zinc fingeri636 – 659C2H2-type 8PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri667 – 690C2H2-type 9PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri753 – 776C2H2-type 10PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri789 – 812C2H2-type 11PROSITE-ProRule annotationAdd BLAST24

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • RNA polymerase II transcription corepressor activity Source: UniProtKB
  • SUMO ligase activity Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: GO_Central

GO - Biological processi

  • negative regulation of histone H3-K9 acetylation Source: UniProtKB
  • negative regulation of transcription initiation from RNA polymerase II promoter Source: UniProtKB
  • negative regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
  • protein sumoylation Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000112200-MONOMER.
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 SUMO-protein ligase ZNF4511 Publication (EC:6.3.2.-2 Publications)
Alternative name(s):
Coactivator for steroid receptors1 Publication
Zinc finger protein 451
Gene namesi
Name:ZNF451
Synonyms:COASTER1 Publication, KIAA0576, KIAA1702
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21091. ZNF451.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi31 – 34IQFV → AQAA: Nearly abolishes E3 SUMO-protein ligase activity (in vitro). 1 Publication4
Mutagenesisi37G → GGSGG: Nearly abolishes E3 SUMO-protein ligase activity (in vitro). 1 Publication1
Mutagenesisi38 – 41PLRP → ALRA: Reduces E3 SUMO-protein ligase activity by 97% (in vitro). 1 Publication4
Mutagenesisi38 – 41PLRP → GLRG: Nearly abolishes E3 SUMO-protein ligase activity (in vitro). 1 Publication4
Mutagenesisi39L → LGSGG: Nearly abolishes E3 SUMO-protein ligase activity (in vitro). 1 Publication1
Mutagenesisi40R → A: Reduces E3 SUMO-protein ligase activity by 96% (in vitro). 1 Publication1
Mutagenesisi46 – 49IDLV → ADAA: Nearly abolishes E3 SUMO-protein ligase activity (in vitro). 1 Publication4
Mutagenesisi48 – 49LV → AA: Impairs interaction with SUMO1. No effect on negative regulation of SMAD4-mediated transcription activation. 2 Publications2
Mutagenesisi188G → E: Mildly reduces E3 SUMO-protein ligase activity. 1 Publication1
Mutagenesisi192R → E: Mildly reduces E3 SUMO-protein ligase activity. 1 Publication1
Mutagenesisi706K → R: No effect on negative regulation of SMAD4-mediated transcription activation. 1 Publication1

Organism-specific databases

DisGeNETi26036.
OpenTargetsiENSG00000112200.
PharmGKBiPA134967635.

Polymorphism and mutation databases

BioMutaiZNF451.
DMDMi37999825.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000475981 – 1061E3 SUMO-protein ligase ZNF451Add BLAST1061

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki75Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki106Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki153Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei155PhosphoserineCombined sources1
Modified residuei158Omega-N-methylarginineCombined sources1
Cross-linki288Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki423Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei432PhosphoserineCombined sources1
Cross-linki434Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki464Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki664Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki706Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki706Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki779Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki817Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki827Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki832Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki843Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki845Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki852Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki993Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Isoform 3 (identifier: Q9Y4E5-4)
Cross-linki130Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki490Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki522Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationi

Sumoylated. Predominantly sumoylated on the N-terminal region that is important for interaction with SUMO1 and SUMO2 (PubMed:18656483, PubMed:26524493, PubMed:26524494). Sumoylation is important for localization in nuclear granules; desumoylation leads to diffuse nucleoplasmic location (PubMed:18656483). Autosumoylated (in vitro) (PubMed:26524493, PubMed:26524494). Sumoylation enhances E3 SUMO-protein ligase activity (PubMed:26524494).3 Publications

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9Y4E5.
PaxDbiQ9Y4E5.
PeptideAtlasiQ9Y4E5.
PRIDEiQ9Y4E5.

PTM databases

iPTMnetiQ9Y4E5.
PhosphoSitePlusiQ9Y4E5.

Expressioni

Gene expression databases

BgeeiENSG00000112200.
CleanExiHS_ZNF451.
ExpressionAtlasiQ9Y4E5. baseline and differential.
GenevisibleiQ9Y4E5. HS.

Organism-specific databases

HPAiHPA015692.
HPA028838.

Interactioni

Subunit structurei

Homooligomer. Interacts (via N-terminal region) with SUMO1 (PubMed:18656483). Interacts (via N-terminal region) with SUMO2 (PubMed:18656483, PubMed:26524494). Interacts simultaneously with two SUMO2 chains (PubMed:26524493, PubMed:26524494). Identified in a complex with SUMO2 and UBE2I/UBC9, where one ZNF451 interacts with one UBE2I/UBC9 and two SUMO2 chains, one bound to the UBE2I/UBC9 active site and the other to another region of the same UBE2I/UBC9 molecule (PubMed:26524493, PubMed:26524494). Interacts (via C-terminus) with ubiquitin (PubMed:18656483). Interacts (via N-terminal zinc-finger domains) with SMAD4 (via MH2 domain). Interacts with SMAD2 and SMAD3. Identified in a complex that contains at least ZNF451, SMAD2, SMAD3 and SMAD4. Interacts with EP300. Inhibits interaction between EP300 and the SMAD4 complex (PubMed:24324267).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
UBE2IP632793EBI-747230,EBI-80168

Protein-protein interaction databases

BioGridi117502. 30 interactors.
DIPiDIP-51264N.
IntActiQ9Y4E5. 20 interactors.
MINTiMINT-1197511.
STRINGi9606.ENSP00000359740.

Structurei

Secondary structure

11061
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 40Combined sources9
Beta strandi42 – 47Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5D2MX-ray2.40G2-56[»]
ProteinModelPortaliQ9Y4E5.
SMRiQ9Y4E5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 344Important for interaction with SUMO1 and SUMO21 PublicationAdd BLAST344
Regioni1 – 246Sufficient for E3 SUMO-protein ligase activity1 PublicationAdd BLAST246
Regioni30 – 37Interaction with SUMO2 11 Publication8
Regioni42 – 50Interaction with SUMO2 21 Publication9
Regioni168 – 525Important for interaction with SMAD41 PublicationAdd BLAST358
Regioni1050 – 1061Important for ubiquitin binding1 PublicationAdd BLAST12

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi38 – 41PLRPCurated4

Domaini

Binds UBE2I/UBC9 and two SUMO2 molecules via its N-terminus. The most N-terminal region interacts with the SUMO2 chain that is covalently bound to the UBE2I/UBC9 active site, while the second region interacts with another SUMO2 that is non-covalently associated with the same UBE2I/UBC9 chain.1 Publication1 Publication

Sequence similaritiesi

Contains 11 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri169 – 195C2H2-type 1PROSITE-ProRule annotationAdd BLAST27
Zinc fingeri253 – 277C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri315 – 337C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri362 – 386C2H2-type 4PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri498 – 521C2H2-type 5PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri531 – 554C2H2-type 6PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri606 – 631C2H2-type 7; atypicalPROSITE-ProRule annotationAdd BLAST26
Zinc fingeri636 – 659C2H2-type 8PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri667 – 690C2H2-type 9PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri753 – 776C2H2-type 10PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri789 – 812C2H2-type 11PROSITE-ProRule annotationAdd BLAST24

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITHH. Eukaryota.
ENOG41116BX. LUCA.
GeneTreeiENSGT00390000011354.
HOVERGENiHBG057364.
InParanoidiQ9Y4E5.
OMAiESVLLYC.
OrthoDBiEOG091G017Z.
PhylomeDBiQ9Y4E5.
TreeFamiTF331947.

Family and domain databases

InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 12 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 9 hits.
PS50157. ZINC_FINGER_C2H2_2. 5 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y4E5-1) [UniParc]FASTAAdd 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
MGDPGSEIIE SVPPAGPEAS ESTTDENEDD IQFVSEGPLR PVLEYIDLVS
60 70 80 90 100
SDDEEPSTSY TDENIKRKDH IDYQKDKVAL TLARLARHVE VEKQQKEEKN
110 120 130 140 150
RAFREKIDFQ HAHGLQELEF IRGHSDTEAA RLCVDQWLKM PGLKTGTINC
160 170 180 190 200
GTKSSFRRGG HTWVSGKPIL CPIMHCNKEF DNGHLLLGHL KRFDHSPCDP
210 220 230 240 250
TITLHGPFFS SFACVVCYKK FVTQQQYRDH LFDKEATDDG HNNNLLPQII
260 270 280 290 300
QCFACPNCFL LFSRKEECSK HMSGKNHFHQ SFKLGDNKGI AHPISFPSFA
310 320 330 340 350
KKLLISLCKD VPFQVKCVAC HKTLRSHMEL TAHFRVHCRN AGPVAVAEKS
360 370 380 390 400
ITQVAEKFIL RGYCPDCNQV FVDETSTQNH KQNSGHKVRV INSVEESVLL
410 420 430 440 450
YCHSSEGNKD PSSDLHLLLD QSKFSSLKRT MSIKESSSLE CIAIPKKKMN
460 470 480 490 500
LKDKSHEGVA CVQKEKSVVK TWFCECNQRF PSEDAVEKHV FSANTMGYKC
510 520 530 540 550
VVCGKVCDDS GVIRLHMSRI HGGAHLNNFL FWCRTCKKEL TRKDTIMAHV
560 570 580 590 600
TEFHNGHRYF YEMDEVEGET LPSSSTTLDN LTANKPSSAI TVIDHSPANS
610 620 630 640 650
SPRGKWQCRI CEDMFDSQEY VKQHCMSLAS HKFHRYSCAH CRKPFHKIET
660 670 680 690 700
LYRHCQDEHD NEIKIKYFCG LCDLIFNVEE AFLSHYEEHH SIDYVFVSEK
710 720 730 740 750
TETSIKTEDD FPVIETSNQL TCGCRESYIC KVNRKEDYSR CLQIMLDKGK
760 770 780 790 800
LWFRCSLCSA TAQNLTDMNT HIHQVHKEKS DEEEQQYVIK CGTCTKAFHD
810 820 830 840 850
PESAQQHFHR KHCFLQKPSV AHFGSEKSNL YKFTASASHT ERKLKQAINY
860 870 880 890 900
SKSLDMEKGV ENDLSYQNIE EEIVELPDLD YLRTMTHIVF VDFDNWSNFF
910 920 930 940 950
GHLPGHLNQG TFIWGFQGGN TNWKPPLNCK IYNYLNRIGC FFLHPRCSKR
960 970 980 990 1000
KDAADFAICM HAGRLDEQLP KQIPFTILSG DQGFLELENQ FKKTQRPAHI
1010 1020 1030 1040 1050
LNPHHLEGDM MCALLNSISD TTKECDSDDN MGAKNTSIGE EFISTEDVEL
1060
EEAIRRSLEE M
Length:1,061
Mass (Da):121,484
Last modified:October 24, 2003 - v2
Checksum:i8F0446B9FBFF28FA
GO
Isoform 2 (identifier: Q9Y4E5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     870-917: Missing.

Show »
Length:1,013
Mass (Da):115,776
Checksum:i47F3AEA54D754CBB
GO
Isoform 3 (identifier: Q9Y4E5-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     63-1061: ENIKRKDHID...EAIRRSLEEM → RMPESKVPSS...DSPERHGYKN

Show »
Length:559
Mass (Da):63,021
Checksum:i4939846709AC5536
GO

Sequence cautioni

The sequence AAH21712 differs from that shown. Intron retention.Curated
The sequence AAH42450 differs from that shown. Contaminating sequence.Curated
The sequence AAH58853 differs from that shown. Contaminating sequence.Curated
The sequence BAA25502 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAB21793 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti169I → T in AAL17975 (Ref. 1) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_03531263 – 1061ENIKR…SLEEM → RMPESKVPSSENHRPEMCSS CNVPLPIGDSSSFSGSCSSS PERIVSQTSSVENPLENQKN DQNNSDTKISETETLKSSQN FQTLPSSPLLVPQESLASSE VKENLRIDSSSASQHGRDAI LYLQTQVAEMSRVIRDLQSR SCFRFHHSRPSENSSVPWDI STSKEENLSTVEEETDYKSP SADDKGQPSDPSQSSFTGLL KRMEQRGVIKRVTLQSEAES CEGKPDCVTSKKRLVPPLHP LLRIATTEVFKDPADCHPSS FMGHRVYPVAKDTSPFQPNP PAEGPIVEALEHSKRGNTTS PLDSTSKEMEVMGCRFYHAA SIAARAASYMAYMTQYQRKL WEDMEDLVHDPEFDRGKARC IISDGMDAGLWQLCTTRDIM DSVVRVMAMAIDYRRQAWLR LTSLTKKTQEKISHLPFDGT SLFGQDVKAVVAEDNNIKEN DYKDHKYYNQHRYFYSHDQK AHYHNRGYSKGDWYKPRNHP YRYRKKGDSPERHGYKN in isoform 3. 2 PublicationsAdd BLAST999
Alternative sequenceiVSP_008624870 – 917Missing in isoform 2. 1 PublicationAdd BLAST48

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY055204 mRNA. Translation: AAL17975.1.
AB011148 mRNA. Translation: BAA25502.1. Different initiation.
AB051489 mRNA. Translation: BAB21793.1. Different initiation.
AL136311, AL450489 Genomic DNA. Translation: CAI20516.1.
AL450489, AL136311 Genomic DNA. Translation: CAH71220.1.
AL450489 Genomic DNA. Translation: CAH71222.1.
BC021712 mRNA. Translation: AAH21712.2. Sequence problems.
BC042450 mRNA. Translation: AAH42450.1. Sequence problems.
BC058853 mRNA. Translation: AAH58853.1. Sequence problems.
CCDSiCCDS43477.1. [Q9Y4E5-1]
CCDS4960.1. [Q9Y4E5-2]
CCDS59026.1. [Q9Y4E5-4]
PIRiT00341.
RefSeqiNP_001026794.1. NM_001031623.2. [Q9Y4E5-1]
NP_056370.2. NM_015555.2. [Q9Y4E5-2]
UniGeneiHs.485628.
Hs.705485.

Genome annotation databases

EnsembliENST00000357489; ENSP00000350083; ENSG00000112200. [Q9Y4E5-2]
ENST00000370706; ENSP00000359740; ENSG00000112200. [Q9Y4E5-1]
ENST00000370708; ENSP00000359742; ENSG00000112200. [Q9Y4E5-4]
GeneIDi26036.
KEGGihsa:26036.
UCSCiuc003pdm.3. human. [Q9Y4E5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY055204 mRNA. Translation: AAL17975.1.
AB011148 mRNA. Translation: BAA25502.1. Different initiation.
AB051489 mRNA. Translation: BAB21793.1. Different initiation.
AL136311, AL450489 Genomic DNA. Translation: CAI20516.1.
AL450489, AL136311 Genomic DNA. Translation: CAH71220.1.
AL450489 Genomic DNA. Translation: CAH71222.1.
BC021712 mRNA. Translation: AAH21712.2. Sequence problems.
BC042450 mRNA. Translation: AAH42450.1. Sequence problems.
BC058853 mRNA. Translation: AAH58853.1. Sequence problems.
CCDSiCCDS43477.1. [Q9Y4E5-1]
CCDS4960.1. [Q9Y4E5-2]
CCDS59026.1. [Q9Y4E5-4]
PIRiT00341.
RefSeqiNP_001026794.1. NM_001031623.2. [Q9Y4E5-1]
NP_056370.2. NM_015555.2. [Q9Y4E5-2]
UniGeneiHs.485628.
Hs.705485.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5D2MX-ray2.40G2-56[»]
ProteinModelPortaliQ9Y4E5.
SMRiQ9Y4E5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117502. 30 interactors.
DIPiDIP-51264N.
IntActiQ9Y4E5. 20 interactors.
MINTiMINT-1197511.
STRINGi9606.ENSP00000359740.

PTM databases

iPTMnetiQ9Y4E5.
PhosphoSitePlusiQ9Y4E5.

Polymorphism and mutation databases

BioMutaiZNF451.
DMDMi37999825.

Proteomic databases

EPDiQ9Y4E5.
PaxDbiQ9Y4E5.
PeptideAtlasiQ9Y4E5.
PRIDEiQ9Y4E5.

Protocols and materials databases

DNASUi26036.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357489; ENSP00000350083; ENSG00000112200. [Q9Y4E5-2]
ENST00000370706; ENSP00000359740; ENSG00000112200. [Q9Y4E5-1]
ENST00000370708; ENSP00000359742; ENSG00000112200. [Q9Y4E5-4]
GeneIDi26036.
KEGGihsa:26036.
UCSCiuc003pdm.3. human. [Q9Y4E5-1]

Organism-specific databases

CTDi26036.
DisGeNETi26036.
GeneCardsiZNF451.
HGNCiHGNC:21091. ZNF451.
HPAiHPA015692.
HPA028838.
MIMi615708. gene.
neXtProtiNX_Q9Y4E5.
OpenTargetsiENSG00000112200.
PharmGKBiPA134967635.
HUGEiSearch...
Search...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITHH. Eukaryota.
ENOG41116BX. LUCA.
GeneTreeiENSGT00390000011354.
HOVERGENiHBG057364.
InParanoidiQ9Y4E5.
OMAiESVLLYC.
OrthoDBiEOG091G017Z.
PhylomeDBiQ9Y4E5.
TreeFamiTF331947.

Enzyme and pathway databases

UniPathwayiUPA00886.
BioCyciZFISH:ENSG00000112200-MONOMER.

Miscellaneous databases

ChiTaRSiZNF451. human.
GeneWikiiZNF451.
GenomeRNAii26036.
PROiQ9Y4E5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000112200.
CleanExiHS_ZNF451.
ExpressionAtlasiQ9Y4E5. baseline and differential.
GenevisibleiQ9Y4E5. HS.

Family and domain databases

InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 12 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 9 hits.
PS50157. ZINC_FINGER_C2H2_2. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiZN451_HUMAN
AccessioniPrimary (citable) accession number: Q9Y4E5
Secondary accession number(s): Q5VVE9
, Q5VVF1, Q86YE4, Q8N380, Q8TD15, Q9C0G1, Q9NQM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: October 24, 2003
Last modified: November 2, 2016
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.