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Protein

Histone-lysine N-methyltransferase SUV420H1

Gene

Suv420h1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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].PROSITE-ProRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

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 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:2444557. Suv420h1.

Subcellular locationi

GO - Cellular componenti

  • 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.
GenevisibleiQ3U8K7. MM.

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 – 8915Combined sources
Helixi91 – 944Combined sources
Helixi138 – 14811Combined sources
Helixi151 – 1588Combined sources
Helixi162 – 1676Combined sources
Helixi173 – 18715Combined sources
Helixi188 – 1903Combined sources
Beta strandi196 – 2016Combined sources
Beta strandi208 – 21710Combined sources
Beta strandi224 – 23512Combined sources
Helixi237 – 2437Combined sources
Turni246 – 2483Combined sources
Beta strandi253 – 2564Combined sources
Turni257 – 2604Combined sources
Beta strandi261 – 2677Combined sources
Helixi268 – 2714Combined sources
Beta strandi279 – 29618Combined sources
Turni310 – 3134Combined sources
Helixi315 – 3173Combined sources
Helixi323 – 3286Combined sources
Helixi331 – 3333Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiSGCLTRH.
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. AlignAdd to basket

Isoform 1 (identifier: Q3U8K7-1) [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
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. Curated
The sequence AAT00539.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC39834.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE23934.1 differs from that shown. Reason: Erroneous termination at position 3. Translated as Trp.Curated

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:
EMBLi
GenBanki
DDBJi
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_006531727.2. [Q3U8K7-1]
XP_006531791.1. XM_006531728.2. [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:
EMBLi
GenBanki
DDBJi
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_006531727.2. [Q3U8K7-1]
XP_006531791.1. XM_006531728.2. [Q3U8K7-1]
XP_006531794.1. XM_006531731.1. [Q3U8K7-5]
UniGeneiMm.278578.

3D structure databases

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

Protein-protein interaction databases

BioGridi230441. 3 interactions.

PTM databases

PhosphoSiteiQ3U8K7.

Proteomic databases

MaxQBiQ3U8K7.
PaxDbiQ3U8K7.
PRIDEiQ3U8K7.

Protocols and materials databases

DNASUi225888.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi51111.
MGIiMGI:2444557. Suv420h1.

Phylogenomic databases

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

Miscellaneous databases

ChiTaRSiSuv420h1. mouse.
NextBioi377853.
PROiQ3U8K7.
SOURCEiSearch...

Gene expression databases

BgeeiQ3U8K7.
ExpressionAtlasiQ3U8K7. baseline and differential.
GenevisibleiQ3U8K7. MM.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 84 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

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 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.