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Protein

Histone-lysine N-methyltransferase KMT5B

Gene

KMT5B

Organism
Homo sapiens (Human)
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. KMT5B is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By similarity). Plays a role in myogenesis by regulating the expression of target genes, such as EID3.By similarity1 Publication

Catalytic activityi

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

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 KMT5BCurated (EC:2.1.1.43)
Alternative name(s):
Lysine N-methyltransferase 5B
Lysine-specific methyltransferase 5BImported
Suppressor of variegation 4-20 homolog 1
Short name:
Su(var)4-20 homolog 1
Short name:
Suv4-20h1
Gene namesi
Name:KMT5BImported
Synonyms:SUV420H1
ORF Names:CGI-85
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:24283. KMT5B.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134958369.

Chemistry

ChEMBLiCHEMBL2321645.
GuidetoPHARMACOLOGYi2717.

Polymorphism and mutation databases

BioMutaiSUV420H1.
DMDMi332278247.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 885885Histone-lysine N-methyltransferase KMT5BPRO_0000281787Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki555 – 555Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ4FZB7.
PaxDbiQ4FZB7.
PRIDEiQ4FZB7.

PTM databases

iPTMnetiQ4FZB7.
PhosphoSiteiQ4FZB7.

Expressioni

Inductioni

Strongly down-regulated in breast cancer cells.1 Publication

Gene expression databases

BgeeiQ4FZB7.
ExpressionAtlasiQ4FZB7. baseline and differential.
GenevisibleiQ4FZB7. HS.

Organism-specific databases

HPAiHPA046139.

Interactioni

Subunit structurei

Interacts with HP1 proteins CBX1, CBX3 and CBX5. Interacts with RB1 family proteins RB1, RBL1 and RBL2 (By similarity). Interacts (via C-terminus) with FRG1.By similarity1 Publication

Protein-protein interaction databases

BioGridi119300. 5 interactions.
DIPiDIP-48656N.
IntActiQ4FZB7. 3 interactions.
STRINGi9606.ENSP00000305899.

Structurei

Secondary structure

1
885
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi74 – 9320Combined sources
Helixi134 – 14714Combined sources
Helixi150 – 1578Combined sources
Helixi161 – 1677Combined sources
Helixi172 – 18716Combined sources
Helixi191 – 1933Combined sources
Beta strandi195 – 2006Combined sources
Beta strandi207 – 21610Combined sources
Beta strandi223 – 23412Combined sources
Helixi236 – 2427Combined sources
Turni245 – 2473Combined sources
Beta strandi252 – 2554Combined sources
Turni256 – 2594Combined sources
Beta strandi260 – 2667Combined sources
Helixi267 – 2704Combined sources
Beta strandi278 – 2858Combined sources
Beta strandi288 – 2958Combined sources
Turni309 – 3124Combined sources
Helixi314 – 3163Combined sources
Helixi322 – 3276Combined sources
Helixi330 – 3323Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S8PX-ray1.85A/B63-335[»]
ProteinModelPortaliQ4FZB7.
SMRiQ4FZB7. Positions 71-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini193 – 308116SETPROSITE-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

eggNOGiKOG2589. Eukaryota.
ENOG410XPH8. LUCA.
HOVERGENiHBG105761.
InParanoidiQ4FZB7.
OrthoDBiEOG7MKW6P.
PhylomeDBiQ4FZB7.
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 (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q4FZB7-1) [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
MKWLGESKIM VVNGRRNGGK LSNDHQQNQS KLQHTGKDTL KAGKNAVERR
60 70 80 90 100
SNRCNGNSGF EGQSRYVPSS GMSAKELCEN DDLATSLVLD PYLGFQTHKM
110 120 130 140 150
NTSAFPSRSS RHFSKSDSFS HNNPVRFRPI KGRQEELKEV IERFKKDEHL
160 170 180 190 200
EKAFKCLTSG EWARHYFLNK NKMQEKLFKE HVFIYLRMFA TDSGFEILPC
210 220 230 240 250
NRYSSEQNGA KIVATKEWKR NDKIELLVGC IAELSEIEEN MLLRHGENDF
260 270 280 290 300
SVMYSTRKNC AQLWLGPAAF INHDCRPNCK FVSTGRDTAC VKALRDIEPG
310 320 330 340 350
EEISCYYGDG FFGENNEFCE CYTCERRGTG AFKSRVGLPA PAPVINSKYG
360 370 380 390 400
LRETDKRLNR LKKLGDSSKN SDSQSVSSNT DADTTQEKNN ATSNRKSSVG
410 420 430 440 450
VKKNSKSRTL TRQSMSRIPA SSNSTSSKLT HINNSRVPKK LKKPAKPLLS
460 470 480 490 500
KIKLRNHCKR LEQKNASRKL EMGNLVLKEP KVVLYKNLPI KKDKEPEGPA
510 520 530 540 550
QAAVASGCLT RHAAREHRQN PVRGAHSQGE SSPCTYITRR SVRTRTNLKE
560 570 580 590 600
ASDIKLEPNT LNGYKSSVTE PCPDSGEQLQ PAPVLQEEEL AHETAQKGEA
610 620 630 640 650
KCHKSDTGMS KKKSRQGKLV KQFAKIEEST PVHDSPGKDD AVPDLMGPHS
660 670 680 690 700
DQGEHSGTVG VPVSYTDCAP SPVGCSVVTS DSFKTKDSFR TAKSKKKRRI
710 720 730 740 750
TRYDAQLILE NNSGIPKLTL RRRHDSSSKT NDQENDGMNS SKISIKLSKD
760 770 780 790 800
HDNDNNLYVA KLNNGFNSGS GSSSTKLKIQ LKRDEENRGS YTEGLHENGV
810 820 830 840 850
CCSDPLSLLE SRMEVDDYSQ YEEESTDDSS SSEGDEEEDD YDDDFEDDFI
860 870 880
PLPPAKRLRL IVGKDSIDID ISSRRREDQS LRLNA
Length:885
Mass (Da):99,187
Last modified:May 3, 2011 - v4
Checksum:iB4D4812C1F1A64AB
GO
Isoform 2 (identifier: Q4FZB7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     392-393: TS → SK
     394-885: Missing.

Show »
Length:393
Mass (Da):44,617
Checksum:iDED229EA65E36B95
GO
Isoform 3 (identifier: Q4FZB7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     274-274: D → DLINS
     275-885: Missing.

Note: No experimental confirmation available.
Show »
Length:278
Mass (Da):31,959
Checksum:i12C45DFB622AA8AC
GO

Sequence cautioni

The sequence AAD34080.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAG36937.1 differs from that shown. Reason: Frameshift at positions 233, 249, 254 and 272. Curated
The sequence AAH98121.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated
The sequence AAI04484.1 differs from that shown. Reason: Frameshift at position 396. Curated
The sequence BAA90905.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741A → P in AAD34080 (PubMed:10810093).Curated
Sequence conflicti79 – 791E → G in AAD34080 (PubMed:10810093).Curated
Sequence conflicti99 – 991K → Q in AAD34080 (PubMed:10810093).Curated
Sequence conflicti108 – 1081R → W in AAG36937 (PubMed:11401438).Curated
Sequence conflicti123 – 1231N → K in AAD34080 (PubMed:10810093).Curated
Sequence conflicti135 – 1351E → G in AAD34080 (PubMed:10810093).Curated
Sequence conflicti469 – 4691K → E in BAA90905 (PubMed:14702039).Curated
Sequence conflicti483 – 4831V → A in BAA90905 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91I → N.1 Publication
Corresponds to variant rs2512606 [ dbSNP | Ensembl ].
VAR_047765

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei274 – 2741D → DLINS in isoform 3. 1 PublicationVSP_040034
Alternative sequencei275 – 885611Missing in isoform 3. 1 PublicationVSP_040035Add
BLAST
Alternative sequencei392 – 3932TS → SK in isoform 2. 2 PublicationsVSP_024051
Alternative sequencei394 – 885492Missing in isoform 2. 2 PublicationsVSP_024052Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP002992 Genomic DNA. No translation available.
BC002522 mRNA. Translation: AAH02522.2.
BC012933 mRNA. Translation: AAH12933.2.
BC065287 mRNA. Translation: AAH65287.1.
BC087834 mRNA. Translation: AAH87834.1.
BC098121 mRNA. Translation: AAH98121.1. Sequence problems.
BC099714 mRNA. Translation: AAH99714.1.
BC103498 mRNA. Translation: AAI03499.1.
BC104483 mRNA. Translation: AAI04484.1. Frameshift.
AF264782 mRNA. Translation: AAG36937.1. Frameshift.
AF151843 mRNA. Translation: AAD34080.1. Different initiation.
AK000046 mRNA. Translation: BAA90905.1. Different initiation.
AL512763 mRNA. Translation: CAC21680.1.
CCDSiCCDS31623.1. [Q4FZB7-1]
CCDS44660.1. [Q4FZB7-2]
RefSeqiNP_001287838.1. NM_001300909.1.
NP_057112.3. NM_016028.4.
NP_060105.3. NM_017635.4.
XP_005274092.2. XM_005274035.2.
XP_011543393.1. XM_011545091.1.
XP_011543395.1. XM_011545093.1.
XP_011543396.1. XM_011545094.1.
UniGeneiHs.632120.

Genome annotation databases

EnsembliENST00000304363; ENSP00000305899; ENSG00000110066.
ENST00000401547; ENSP00000385965; ENSG00000110066.
ENST00000405515; ENSP00000385640; ENSG00000110066.
ENST00000615954; ENSP00000484858; ENSG00000110066.
GeneIDi51111.
UCSCiuc001onm.2. human. [Q4FZB7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP002992 Genomic DNA. No translation available.
BC002522 mRNA. Translation: AAH02522.2.
BC012933 mRNA. Translation: AAH12933.2.
BC065287 mRNA. Translation: AAH65287.1.
BC087834 mRNA. Translation: AAH87834.1.
BC098121 mRNA. Translation: AAH98121.1. Sequence problems.
BC099714 mRNA. Translation: AAH99714.1.
BC103498 mRNA. Translation: AAI03499.1.
BC104483 mRNA. Translation: AAI04484.1. Frameshift.
AF264782 mRNA. Translation: AAG36937.1. Frameshift.
AF151843 mRNA. Translation: AAD34080.1. Different initiation.
AK000046 mRNA. Translation: BAA90905.1. Different initiation.
AL512763 mRNA. Translation: CAC21680.1.
CCDSiCCDS31623.1. [Q4FZB7-1]
CCDS44660.1. [Q4FZB7-2]
RefSeqiNP_001287838.1. NM_001300909.1.
NP_057112.3. NM_016028.4.
NP_060105.3. NM_017635.4.
XP_005274092.2. XM_005274035.2.
XP_011543393.1. XM_011545091.1.
XP_011543395.1. XM_011545093.1.
XP_011543396.1. XM_011545094.1.
UniGeneiHs.632120.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S8PX-ray1.85A/B63-335[»]
ProteinModelPortaliQ4FZB7.
SMRiQ4FZB7. Positions 71-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119300. 5 interactions.
DIPiDIP-48656N.
IntActiQ4FZB7. 3 interactions.
STRINGi9606.ENSP00000305899.

Chemistry

ChEMBLiCHEMBL2321645.
GuidetoPHARMACOLOGYi2717.

PTM databases

iPTMnetiQ4FZB7.
PhosphoSiteiQ4FZB7.

Polymorphism and mutation databases

BioMutaiSUV420H1.
DMDMi332278247.

Proteomic databases

MaxQBiQ4FZB7.
PaxDbiQ4FZB7.
PRIDEiQ4FZB7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304363; ENSP00000305899; ENSG00000110066.
ENST00000401547; ENSP00000385965; ENSG00000110066.
ENST00000405515; ENSP00000385640; ENSG00000110066.
ENST00000615954; ENSP00000484858; ENSG00000110066.
GeneIDi51111.
UCSCiuc001onm.2. human. [Q4FZB7-1]

Organism-specific databases

CTDi51111.
GeneCardsiSUV420H1.
HGNCiHGNC:24283. KMT5B.
HPAiHPA046139.
MIMi610881. gene.
neXtProtiNX_Q4FZB7.
PharmGKBiPA134958369.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2589. Eukaryota.
ENOG410XPH8. LUCA.
HOVERGENiHBG105761.
InParanoidiQ4FZB7.
OrthoDBiEOG7MKW6P.
PhylomeDBiQ4FZB7.
TreeFamiTF106433.

Miscellaneous databases

ChiTaRSiSUV420H1. human.
GeneWikiiSUV420H1.
GenomeRNAii51111.
NextBioi53865.
PROiQ4FZB7.
SOURCEiSearch...

Gene expression databases

BgeeiQ4FZB7.
ExpressionAtlasiQ4FZB7. baseline and differential.
GenevisibleiQ4FZB7. HS.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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 1; 2 AND 3), VARIANT ASN-9.
    Tissue: Mammary gland, Placenta, Testis and Uterus.
  3. "The sequence and gene characterization of a 400-kb candidate region for IDDM4 on chromosome 11q13."
    Twells R.C.J., Metzker M.L., Brown S.D., Cox R., Garey C., Hammond H., Hey P.J., Levy E., Nakagawa Y., Philips M.S., Todd J.A., Hess J.F.
    Genomics 72:231-242(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-275 (ISOFORM 1).
  4. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-885 (ISOFORM 2).
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 442-884.
    Tissue: Colon.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 592-885.
    Tissue: Testis.
  7. "Loss of DNA methylation and histone H4 lysine 20 trimethylation in human breast cancer cells is associated with aberrant expression of DNA methyltransferase 1, Suv4-20h2 histone methyltransferase and methyl-binding proteins."
    Tryndyak V.P., Kovalchuk O., Pogribny I.P.
    Cancer Biol. Ther. 5:65-70(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "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, SUBCELLULAR LOCATION.
  9. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKMT5B_HUMAN
AccessioniPrimary (citable) accession number: Q4FZB7
Secondary accession number(s): B7WNX7
, Q3SX56, Q4V775, Q6P150, Q96E44, Q9BUL0, Q9H022, Q9H2K3, Q9NXV3, Q9Y393
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: May 3, 2011
Last modified: May 11, 2016
This is version 105 of the entry and version 4 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.