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Q3U8K7

- SV421_MOUSE

UniProt

Q3U8K7 - SV421_MOUSE

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Protein

Histone-lysine N-methyltransferase SUV420H1

Gene

Suv420h1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2). Plays a role in myogenesis by regulating the expression of target genes, such as EID3.2 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 PublicationPROSITE-ProRule annotation

GO - Molecular functioni

  1. histone methyltransferase activity (H4-K20 specific) Source: MGI

GO - Biological processi

  1. histone H4-K20 trimethylation Source: InterPro
  2. histone methylation Source: MGI
  3. muscle organ development Source: UniProtKB-KW
  4. regulation of transcription, DNA-templated Source: UniProtKB-KW
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Myogenesis, Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase SUV420H1 (EC:2.1.1.43)
Alternative name(s):
Suppressor of variegation 4-20 homolog 1
Short name:
Su(var)4-20 homolog 1
Short name:
Suv4-20h1
Gene namesi
Name:Suv420h1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:2444557. Suv420h1.

Subcellular locationi

Nucleus 1 Publication. Chromosome 1 Publication
Note: Associated with pericentric heterochromatin. CBX1 and CBX5 are required for the localization to pericentric heterochromatin.

GO - Cellular componenti

  1. condensed nuclear chromosome, centromeric region Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Disruption phenotypei

Partial muscle-specific knockout mice display several signs of muscular dystrophy including necrosis and an increased number of centrally nucleated myofibers. RNAi-mediated knockdown in C2C12 muscle cells causes reduced myogenic differentation of the cells.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 883883Histone-lysine N-methyltransferase SUV420H1PRO_0000281788Add
BLAST

Proteomic databases

MaxQBiQ3U8K7.
PaxDbiQ3U8K7.
PRIDEiQ3U8K7.

PTM databases

PhosphoSiteiQ3U8K7.

Expressioni

Gene expression databases

BgeeiQ3U8K7.
ExpressionAtlasiQ3U8K7. baseline and differential.
GenevestigatoriQ3U8K7.

Interactioni

Subunit structurei

Interacts with HP1 proteins CBX1, CBX3 and CBX5. Interacts with RB1 family proteins RB1, RBL1 and RBL2. Interacts (via C-terminus) with FRG1.4 Publications

Protein-protein interaction databases

BioGridi230441. 3 interactions.

Structurei

Secondary structure

1
883
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi75 – 8915
Helixi91 – 944
Helixi138 – 14811
Helixi151 – 1588
Helixi173 – 18715
Helixi188 – 1903
Beta strandi196 – 2016
Beta strandi208 – 21710
Beta strandi224 – 23512
Helixi237 – 2437
Turni246 – 2483
Beta strandi253 – 2564
Turni257 – 2604
Beta strandi261 – 2677
Helixi268 – 2714
Beta strandi279 – 29618
Turni310 – 3134
Helixi315 – 3173
Helixi323 – 3286
Helixi331 – 3333

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BUPX-ray2.17A/B70-336[»]
ProteinModelPortaliQ3U8K7.
SMRiQ3U8K7. Positions 72-334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini194 – 309116SETPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar4-20 subfamily.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG240704.
GeneTreeiENSGT00520000055640.
HOVERGENiHBG105761.
InParanoidiQ3U8K7.
KOiK11429.
OMAiKLEMGNL.
OrthoDBiEOG7MKW6P.
PhylomeDBiQ3U8K7.
TreeFamiTF106433.

Family and domain databases

InterProiIPR025790. Hist-Lys_N-MTase_Suvar4-20.
IPR001214. SET_dom.
[Graphical view]
PfamiPF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS51570. SAM_MT43_SUVAR420_2. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q3U8K7) [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
MKWLGDSKNM VVNGRRNGGK LSNDHQQNQS KLQQHSGKDT LKTGRNAVER
60 70 80 90 100
RSSRCHGNSG FEGQSRYVPS SGMSAKELCE NDDLATSLVL DPYLGFQTHK
110 120 130 140 150
MNTSAFPSRS SRHISKADSF SHNNPVRFRP IKGRQEELKE VIERFKKDEH
160 170 180 190 200
LEKAFKCLTS GEWARHYFLN KNKMQEKLFK EHVFIYLRMF ATDSGFEILP
210 220 230 240 250
CNRYSSEQNG AKIVATKEWK RNDKIELLVG CIAELSEIEE NMLLRHGEND
260 270 280 290 300
FSVMYSTRKN CAQLWLGPAA FINHDCRPNC KFVSTGRDTA CVKALRDIEP
310 320 330 340 350
GEEISCYYGD GFFGENNEFC ECYTCERRGT GAFKSRVGLP APAPVINSKY
360 370 380 390 400
GLRETDKRLN RLKKLGDSSK NSDSQSVSSN TDADTTQEKD NATSNRKSSV
410 420 430 440 450
GVKKSSKSRA LTRPSMPRVP AASNSTSPKL VHTNNPRVPK KLRKPAKPLL
460 470 480 490 500
SKIRLRNHCK RLDQKSASRK LEMGSLVLKE PKVVLYKNLP IKKEREPEGP
510 520 530 540 550
AHAAVGSGCL TRHAAREHRQ NHGRGAHSQG DSLPCTYTTR RSLRTRTGLK
560 570 580 590 600
ETTDIKLEPS PLDGYKNGIL EPCPDSGQQP TPEVLEELAP ETAHREEASQ
610 620 630 640 650
ECPKNDSCLS RKKFRQVKPV KHLAKTEDCS PEHSFPGKDG LPDLPGSHPD
660 670 680 690 700
QGEPSGTVRV PVSHTDSAPS PVGCSVVAPD SFTKDSFRTA QSKKKRRVTR
710 720 730 740 750
YDAQLILENS SGIPKLTLRR RHDSSSKTND HESDGVNSSK ISIKLSKDHD
760 770 780 790 800
SDSNLYVAKL SNGVSAGPGS SSTKLKIQLK RDEESRGPCA EGLHENGVCC
810 820 830 840 850
SDPLSLLESQ MEVDDYSQYE EDSTDESSSS EGEEEEEDCE DDFDDDFIPL
860 870 880
PPAKRLRLIV GKDSIDIDIS SRRREDQSLR LNA
Length:883
Mass (Da):98,580
Last modified:April 3, 2007 - v2
Checksum:i2B24461F582CC5F1
GO
Isoform 2 (identifier: Q3U8K7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     393-394: TS → SK
     395-883: Missing.

Show »
Length:394
Mass (Da):44,723
Checksum:i1425ECDBE1F767D7
GO
Isoform 3 (identifier: Q3U8K7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     104-126: Missing.

Show »
Length:860
Mass (Da):96,070
Checksum:i2EEE457CEE91A890
GO
Isoform 4 (identifier: Q3U8K7-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     328-883: Missing.

Show »
Length:327
Mass (Da):37,546
Checksum:i6400D6AAEEA26B99
GO
Isoform 5 (identifier: Q3U8K7-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     104-126: Missing.
     831-883: EGEEEEEDCEDDFDDDFIPLPPAKRLRLIVGKDSIDIDISSRRREDQSLRLNA → SGKAAEANCW

Note: No experimental confirmation available.

Show »
Length:817
Mass (Da):90,944
Checksum:i478C772F2EAFDEC4
GO

Sequence cautioni

The sequence AAH11214.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAT00539.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAC39834.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAE23934.1 differs from that shown. Reason: Erroneous termination at position 3. Translated as Trp.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531S → N in AAH75709. (PubMed:15489334)Curated
Sequence conflicti153 – 1531K → E in AAH11214. (PubMed:16141072)Curated
Sequence conflicti292 – 2921V → L in BAC39834. (PubMed:15145825)Curated
Sequence conflicti328 – 3281R → Q in BAE31010. (PubMed:16141072)Curated
Sequence conflicti428 – 4281P → A in AAH75709. (PubMed:15489334)Curated
Sequence conflicti472 – 4721E → G in BAC38817. (PubMed:15145825)Curated
Sequence conflicti521 – 5211N → S in AAH75709. (PubMed:15489334)Curated
Sequence conflicti590 – 5901P → H in BAC38817. (PubMed:15145825)Curated
Sequence conflicti595 – 5951R → G in BAE31010. (PubMed:16141072)Curated
Sequence conflicti664 – 6641H → Y in AAH75709. (PubMed:15489334)Curated
Sequence conflicti678 – 6781A → T in AAH75709. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei104 – 12623Missing in isoform 3 and isoform 5. 2 PublicationsVSP_024053Add
BLAST
Alternative sequencei328 – 883556Missing in isoform 4. 2 PublicationsVSP_024054Add
BLAST
Alternative sequencei393 – 3942TS → SK in isoform 2. 1 PublicationVSP_024055
Alternative sequencei395 – 883489Missing in isoform 2. 1 PublicationVSP_024056Add
BLAST
Alternative sequencei831 – 88353EGEEE…LRLNA → SGKAAEANCW in isoform 5. 1 PublicationVSP_024057Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY555192 mRNA. Translation: AAT00539.1. Different initiation.
AK036880 mRNA. Translation: BAC29617.1.
AK054093 mRNA. Translation: BAC35652.1.
AK082660 mRNA. Translation: BAC38565.1.
AK083227 mRNA. Translation: BAC38817.1.
AK087267 mRNA. Translation: BAC39834.1. Different initiation.
AK139255 mRNA. Translation: BAE23934.1. Sequence problems.
AK152179 mRNA. Translation: BAE31010.1.
BC011214 mRNA. Translation: AAH11214.1. Different initiation.
BC075709 mRNA. Translation: AAH75709.1.
CCDSiCCDS29399.1. [Q3U8K7-3]
CCDS50343.1. [Q3U8K7-1]
CCDS50344.1. [Q3U8K7-2]
CCDS50345.1. [Q3U8K7-4]
RefSeqiNP_001161356.1. NM_001167884.1. [Q3U8K7-4]
NP_001161357.1. NM_001167885.1. [Q3U8K7-1]
NP_001161358.1. NM_001167886.1. [Q3U8K7-3]
NP_001161359.1. NM_001167887.1. [Q3U8K7-1]
NP_001161360.1. NM_001167888.1. [Q3U8K7-4]
NP_001161361.1. NM_001167889.1. [Q3U8K7-2]
NP_659120.3. NM_144871.4. [Q3U8K7-3]
XP_006531790.1. XM_006531727.1. [Q3U8K7-1]
XP_006531791.1. XM_006531728.1. [Q3U8K7-1]
XP_006531794.1. XM_006531731.1. [Q3U8K7-5]
UniGeneiMm.278578.

Genome annotation databases

EnsembliENSMUST00000005518; ENSMUSP00000005518; ENSMUSG00000045098. [Q3U8K7-4]
ENSMUST00000052699; ENSMUSP00000060162; ENSMUSG00000045098. [Q3U8K7-2]
ENSMUST00000113968; ENSMUSP00000109601; ENSMUSG00000045098. [Q3U8K7-4]
ENSMUST00000113970; ENSMUSP00000109603; ENSMUSG00000045098. [Q3U8K7-2]
ENSMUST00000113972; ENSMUSP00000109605; ENSMUSG00000045098. [Q3U8K7-1]
ENSMUST00000113973; ENSMUSP00000109606; ENSMUSG00000045098. [Q3U8K7-1]
ENSMUST00000113974; ENSMUSP00000109607; ENSMUSG00000045098. [Q3U8K7-3]
ENSMUST00000113977; ENSMUSP00000109610; ENSMUSG00000045098. [Q3U8K7-3]
ENSMUST00000176262; ENSMUSP00000135563; ENSMUSG00000045098. [Q3U8K7-3]
GeneIDi225888.
KEGGimmu:225888.
UCSCiuc008fww.2. mouse. [Q3U8K7-4]
uc008fwz.2. mouse. [Q3U8K7-2]
uc008fxa.2. mouse. [Q3U8K7-1]
uc008fxc.2. mouse. [Q3U8K7-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY555192 mRNA. Translation: AAT00539.1 . Different initiation.
AK036880 mRNA. Translation: BAC29617.1 .
AK054093 mRNA. Translation: BAC35652.1 .
AK082660 mRNA. Translation: BAC38565.1 .
AK083227 mRNA. Translation: BAC38817.1 .
AK087267 mRNA. Translation: BAC39834.1 . Different initiation.
AK139255 mRNA. Translation: BAE23934.1 . Sequence problems.
AK152179 mRNA. Translation: BAE31010.1 .
BC011214 mRNA. Translation: AAH11214.1 . Different initiation.
BC075709 mRNA. Translation: AAH75709.1 .
CCDSi CCDS29399.1. [Q3U8K7-3 ]
CCDS50343.1. [Q3U8K7-1 ]
CCDS50344.1. [Q3U8K7-2 ]
CCDS50345.1. [Q3U8K7-4 ]
RefSeqi NP_001161356.1. NM_001167884.1. [Q3U8K7-4 ]
NP_001161357.1. NM_001167885.1. [Q3U8K7-1 ]
NP_001161358.1. NM_001167886.1. [Q3U8K7-3 ]
NP_001161359.1. NM_001167887.1. [Q3U8K7-1 ]
NP_001161360.1. NM_001167888.1. [Q3U8K7-4 ]
NP_001161361.1. NM_001167889.1. [Q3U8K7-2 ]
NP_659120.3. NM_144871.4. [Q3U8K7-3 ]
XP_006531790.1. XM_006531727.1. [Q3U8K7-1 ]
XP_006531791.1. XM_006531728.1. [Q3U8K7-1 ]
XP_006531794.1. XM_006531731.1. [Q3U8K7-5 ]
UniGenei Mm.278578.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4BUP X-ray 2.17 A/B 70-336 [» ]
ProteinModelPortali Q3U8K7.
SMRi Q3U8K7. Positions 72-334.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 230441. 3 interactions.

PTM databases

PhosphoSitei Q3U8K7.

Proteomic databases

MaxQBi Q3U8K7.
PaxDbi Q3U8K7.
PRIDEi Q3U8K7.

Protocols and materials databases

DNASUi 225888.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000005518 ; ENSMUSP00000005518 ; ENSMUSG00000045098 . [Q3U8K7-4 ]
ENSMUST00000052699 ; ENSMUSP00000060162 ; ENSMUSG00000045098 . [Q3U8K7-2 ]
ENSMUST00000113968 ; ENSMUSP00000109601 ; ENSMUSG00000045098 . [Q3U8K7-4 ]
ENSMUST00000113970 ; ENSMUSP00000109603 ; ENSMUSG00000045098 . [Q3U8K7-2 ]
ENSMUST00000113972 ; ENSMUSP00000109605 ; ENSMUSG00000045098 . [Q3U8K7-1 ]
ENSMUST00000113973 ; ENSMUSP00000109606 ; ENSMUSG00000045098 . [Q3U8K7-1 ]
ENSMUST00000113974 ; ENSMUSP00000109607 ; ENSMUSG00000045098 . [Q3U8K7-3 ]
ENSMUST00000113977 ; ENSMUSP00000109610 ; ENSMUSG00000045098 . [Q3U8K7-3 ]
ENSMUST00000176262 ; ENSMUSP00000135563 ; ENSMUSG00000045098 . [Q3U8K7-3 ]
GeneIDi 225888.
KEGGi mmu:225888.
UCSCi uc008fww.2. mouse. [Q3U8K7-4 ]
uc008fwz.2. mouse. [Q3U8K7-2 ]
uc008fxa.2. mouse. [Q3U8K7-1 ]
uc008fxc.2. mouse. [Q3U8K7-3 ]

Organism-specific databases

CTDi 51111.
MGIi MGI:2444557. Suv420h1.

Phylogenomic databases

eggNOGi NOG240704.
GeneTreei ENSGT00520000055640.
HOVERGENi HBG105761.
InParanoidi Q3U8K7.
KOi K11429.
OMAi KLEMGNL.
OrthoDBi EOG7MKW6P.
PhylomeDBi Q3U8K7.
TreeFami TF106433.

Miscellaneous databases

ChiTaRSi SUV420H1. mouse.
NextBioi 377853.
PROi Q3U8K7.
SOURCEi Search...

Gene expression databases

Bgeei Q3U8K7.
ExpressionAtlasi Q3U8K7. baseline and differential.
Genevestigatori Q3U8K7.

Family and domain databases

InterProi IPR025790. Hist-Lys_N-MTase_Suvar4-20.
IPR001214. SET_dom.
[Graphical view ]
Pfami PF00856. SET. 1 hit.
[Graphical view ]
SMARTi SM00317. SET. 1 hit.
[Graphical view ]
PROSITEi PS51570. SAM_MT43_SUVAR420_2. 1 hit.
PS50280. SET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin."
    Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G., Reinberg D., Jenuwein T.
    Genes Dev. 18:1251-1262(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH CBX1; CBX3 AND CBX5.
    Strain: C57BL/6.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Bone marrow, Cerebellum, Hippocampus, Lung, Oviduct and Vagina.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
    Strain: Czech II and FVB/N.
    Tissue: Mammary tumor and Salivary gland.
  4. "Role of the RB1 family in stabilizing histone methylation at constitutive heterochromatin."
    Gonzalo S., Garcia-Cao M., Fraga M.F., Schotta G., Peters A.H.F.M., Cotter S.E., Eguia R., Dean D.C., Esteller M., Jenuwein T., Blasco M.A.
    Nat. Cell Biol. 7:420-428(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RB1; RBL1 AND RBL2.
  5. Cited for: INTERACTION WITH RB1; RBL1 AND RBL2.
  6. "FSHD muscular dystrophy region gene 1 binds Suv4-20h1 histone methyltransferase and impairs myogenesis."
    Neguembor M.V., Xynos A., Onorati M.C., Caccia R., Bortolanza S., Godio C., Pistoni M., Corona D.F., Schotta G., Gabellini D.
    J. Mol. Cell Biol. 5:294-307(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FRG1, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiSV421_MOUSE
AccessioniPrimary (citable) accession number: Q3U8K7
Secondary accession number(s): Q3UTP6
, Q6DI74, Q6Q784, Q8BU67, Q8BUN0, Q8BUT7, Q8BW73, Q8BZ24, Q91X81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: October 29, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3