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Q7Z3B3

- KANL1_HUMAN

UniProt

Q7Z3B3 - KANL1_HUMAN

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Protein
KAT8 regulatory NSL complex subunit 1
Gene
KANSL1, KIAA1267, MSL1V1, NSL1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription.2 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. chromatin organization Source: Reactome
  2. histone H4-K16 acetylation Source: UniProtKB
  3. histone H4-K5 acetylation Source: UniProtKB
  4. histone H4-K8 acetylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
KAT8 regulatory NSL complex subunit 1
Alternative name(s):
MLL1/MLL complex subunit KANSL1
MSL1 homolog 1
Short name:
hMSL1v1
NSL complex protein NSL1
Non-specific lethal 1 homolog
Gene namesi
Name:KANSL1
Synonyms:KIAA1267, MSL1V1, NSL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:24565. KANSL1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. MLL1 complex Source: UniProtKB
  2. histone acetyltransferase complex Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi852 – 8554RRRR → AAAA: Abolishes KAT8 histone acetyltransferase activity.
Mutagenesisi856 – 8594GESS → AAAA: Strongly reduces KAT8 histone acetyltransferase activity.
Mutagenesisi860 – 8634FDIN → AAAA: Strongly reduces KAT8 histone acetyltransferase activity.
Mutagenesisi864 – 8674NIVI → AAAA: Abolishes KAT8 histone acetyltransferase activity. 1 Publication
Mutagenesisi868 – 8714PMSV → AAAA: Reduces KAT8 histone acetyltransferase activity. 1 Publication
Mutagenesisi910 – 9101E → R: Abolishes interaction with KAT8. 1 Publication
Mutagenesisi917 – 9171F → R: No effect on interaction with KAT8. 1 Publication
Mutagenesisi921 – 9211H → R: Abolishes interaction with KAT8. 1 Publication

Organism-specific databases

Orphaneti363958. 17q21.31 microdeletion syndrome.
363965. Koolen-De Vries syndrome due to a point mutation.
PharmGKBiPA142671604.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11051105KAT8 regulatory NSL complex subunit 1
PRO_0000234565Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei104 – 1041N6-acetyllysine1 Publication
Modified residuei249 – 2491Phosphoserine1 Publication
Modified residuei268 – 2681Phosphoserine4 Publications
Modified residuei991 – 9911Phosphoserine2 Publications
Modified residuei1003 – 10031Phosphothreonine2 Publications
Modified residuei1045 – 10451Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ7Z3B3.
PaxDbiQ7Z3B3.
PRIDEiQ7Z3B3.

PTM databases

PhosphoSiteiQ7Z3B3.

Expressioni

Tissue specificityi

Expressed in the brain.1 Publication

Gene expression databases

ArrayExpressiQ7Z3B3.
BgeeiQ7Z3B3.
CleanExiHS_KIAA1267.
GenevestigatoriQ7Z3B3.

Organism-specific databases

HPAiHPA006874.
HPA007208.

Interactioni

Subunit structurei

Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Interacts with KAT8; the interaction is direct.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC85BQ158342EBI-740244,EBI-739674

Protein-protein interaction databases

BioGridi129744. 24 interactions.
IntActiQ7Z3B3. 20 interactions.
MINTiMINT-1183636.
STRINGi9606.ENSP00000262419.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi591 – 5933

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CY1X-ray1.50C/D585-598[»]
4CY2X-ray2.00D585-598[»]
ProteinModelPortaliQ7Z3B3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni850 – 88233Required for activation of KAT8 histone acetyltransferase activity
Add
BLAST
Regioni883 – 1105223Sufficient for interaction with KAT8
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili283 – 31432 Reviewed prediction
Add
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG87566.
HOVERGENiHBG080054.
InParanoidiQ7Z3B3.
OMAiTSANCDL.
OrthoDBiEOG7VQJF6.
PhylomeDBiQ7Z3B3.
TreeFamiTF336511.

Family and domain databases

InterProiIPR026180. NSL1.
IPR029332. PEHE_dom.
[Graphical view]
PANTHERiPTHR22443. PTHR22443. 1 hit.
PfamiPF15275. PEHE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q7Z3B3-1) [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

MAAMAPALTD AAAEAHHIRF KLAPPSSTLS PGSAENNGNA NILIAANGTK     50
RKAIAAEDPS LDFRNNPTKE DLGKLQPLVA SYLCSDVTSV PSKESLKLQG 100
VFSKQTVLKS HPLLSQSYEL RAELLGRQPV LEFSLENLRT MNTSGQTALP 150
QAPVNGLAKK LTKSSTHSDH DNSTSLNGGK RALTSSALHG GEMGGSESGD 200
LKGGMTNCTL PHRSLDVEHT TLYSNNSTAN KSSVNSMEQP ALQGSSRLSP 250
GTDSSSNLGG VKLEGKKSPL SSILFSALDS DTRITALLRR QADIESRARR 300
LQKRLQVVQA KQVERHIQHQ LGGFLEKTLS KLPNLESLRP RSQLMLTRKA 350
EAALRKAASE TTTSEGLSNF LKSNSISEEL ERFTASGIAN LRCSEQAFDS 400
DVTDSSSGGE SDIEEEELTR ADPEQRHVPL RRRSEWKWAA DRAAIVSRWN 450
WLQAHVSDLE YRIRQQTDIY KQIRANKGLI VLGEVPPPEH TTDLFLPLSS 500
EVKTDHGTDK LIESVSQPLE NHGARIIGHI SESLSTKSCG ALRPVNGVIN 550
TLQPVLADHI PGDSSDAEEQ LHKKQRLNLV SSSSDGTCVA ARTRPVLSCK 600
KRRLVRPNSI VPLSKKVHRN STIRPGCDVN PSCALCGSGS INTMPPEIHY 650
EAPLLERLSQ LDSCVHPVLA FPDDVPTSLH FQSMLKSQWQ NKPFDKIKPP 700
KKLSLKHRAP MPGSLPDSAR KDRHKLVSSF LTTAKLSHHQ TRPDRTHRQH 750
LDDVGAVPMV ERVTAPKAER LLNPPPPVHD PNHSKMRLRD HSSERSEVLK 800
HHTDMSSSSY LAATHHPPHS PLVRQLSTSS DSPAPASSSS QVTASTSQQP 850
VRRRRGESSF DINNIVIPMS VAATTRVEKL QYKEILTPSW REVDLQSLKG 900
SPDEENEEIE DLSDAAFAAL HAKCEEMERA RWLWTTSVPP QRRGSRSYRS 950
SDGRTTPQLG SANPSTPQPA SPDVSSSHSL SEYSHGQSPR SPISPELHSA 1000
PLTPVARDTP RHLASEDTRC STPELGLDEQ SVQPWERRTF PLAHSPQAEC 1050
EDQLDAQERA ARCTRRTSGS KTGRETEAAP TSPPIVPLKS RHLVAAATAQ 1100
RPTHR 1105
Length:1,105
Mass (Da):121,025
Last modified:May 31, 2011 - v2
Checksum:iB69D11BC522B9CAD
GO
Isoform 2 (identifier: Q7Z3B3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-669: Missing.
     670-673: AFPD → MFLA

Note: No experimental confirmation available.

Show »
Length:436
Mass (Da):48,445
Checksum:iEFA2A4A2BE70F67E
GO

Sequence cautioni

The sequence CAH10565.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti104 – 1041K → T.
Corresponds to variant rs17585974 [ dbSNP | Ensembl ].
VAR_049515
Natural varianti221 – 2211T → I.
Corresponds to variant rs17662853 [ dbSNP | Ensembl ].
VAR_049516
Natural varianti225 – 2251N → D.
Corresponds to variant rs35643216 [ dbSNP | Ensembl ].
VAR_049517
Natural varianti718 – 7181S → P.
Corresponds to variant rs34043286 [ dbSNP | Ensembl ].
VAR_049518
Natural varianti1010 – 10101P → L.4 Publications
Corresponds to variant rs7220988 [ dbSNP | Ensembl ].
VAR_026287
Natural varianti1085 – 10851I → T.
Corresponds to variant rs34579536 [ dbSNP | Ensembl ].
VAR_049519

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 669669Missing in isoform 2.
VSP_041132Add
BLAST
Alternative sequencei670 – 6734AFPD → MFLA in isoform 2.
VSP_041133

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti525 – 5251R → P in BAA86581. 1 Publication
Sequence conflicti525 – 5251R → P in BAF83948. 1 Publication
Sequence conflicti525 – 5251R → P in CAD97958. 1 Publication
Sequence conflicti525 – 5251R → P in AAH98376. 1 Publication
Sequence conflicti530 – 5301I → F in CAB70694. 1 Publication
Sequence conflicti683 – 6831S → G in CAH10565. 1 Publication
Sequence conflicti849 – 8491Missing in BAF83948. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB033093 mRNA. Translation: BAA86581.1.
AK291259 mRNA. Translation: BAF83948.1.
AL117476 mRNA. Translation: CAB55949.1.
AL137317 mRNA. Translation: CAB70694.1.
BX538006 mRNA. Translation: CAD97958.1.
BX648760 mRNA. Translation: CAH10565.1. Different initiation.
AC217773 Genomic DNA. No translation available.
CR936218 Genomic DNA. No translation available.
BC035892 mRNA. Translation: AAH35892.1.
BC098376 mRNA. Translation: AAH98376.1.
CCDSiCCDS11503.1. [Q7Z3B3-1]
PIRiT17259.
T46385.
RefSeqiNP_001180394.1. NM_001193465.1.
NP_001180395.1. NM_001193466.1.
NP_056258.1. NM_015443.3.
XP_005257289.2. XM_005257232.2.
XP_005257290.2. XM_005257233.2.
XP_006721886.1. XM_006721823.1.
XP_006721887.1. XM_006721824.1.
UniGeneiHs.648744.

Genome annotation databases

EnsembliENST00000262419; ENSP00000262419; ENSG00000120071. [Q7Z3B3-1]
ENST00000432791; ENSP00000387393; ENSG00000120071. [Q7Z3B3-1]
ENST00000572904; ENSP00000461484; ENSG00000120071. [Q7Z3B3-1]
ENST00000574590; ENSP00000461812; ENSG00000120071. [Q7Z3B3-1]
GeneIDi284058.
KEGGihsa:284058.
UCSCiuc002ikc.3. human. [Q7Z3B3-1]
uc010wkb.2. human. [Q7Z3B3-2]

Polymorphism databases

DMDMi334302834.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB033093 mRNA. Translation: BAA86581.1 .
AK291259 mRNA. Translation: BAF83948.1 .
AL117476 mRNA. Translation: CAB55949.1 .
AL137317 mRNA. Translation: CAB70694.1 .
BX538006 mRNA. Translation: CAD97958.1 .
BX648760 mRNA. Translation: CAH10565.1 . Different initiation.
AC217773 Genomic DNA. No translation available.
CR936218 Genomic DNA. No translation available.
BC035892 mRNA. Translation: AAH35892.1 .
BC098376 mRNA. Translation: AAH98376.1 .
CCDSi CCDS11503.1. [Q7Z3B3-1 ]
PIRi T17259.
T46385.
RefSeqi NP_001180394.1. NM_001193465.1.
NP_001180395.1. NM_001193466.1.
NP_056258.1. NM_015443.3.
XP_005257289.2. XM_005257232.2.
XP_005257290.2. XM_005257233.2.
XP_006721886.1. XM_006721823.1.
XP_006721887.1. XM_006721824.1.
UniGenei Hs.648744.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4CY1 X-ray 1.50 C/D 585-598 [» ]
4CY2 X-ray 2.00 D 585-598 [» ]
ProteinModelPortali Q7Z3B3.
ModBasei Search...

Protein-protein interaction databases

BioGridi 129744. 24 interactions.
IntActi Q7Z3B3. 20 interactions.
MINTi MINT-1183636.
STRINGi 9606.ENSP00000262419.

PTM databases

PhosphoSitei Q7Z3B3.

Polymorphism databases

DMDMi 334302834.

Proteomic databases

MaxQBi Q7Z3B3.
PaxDbi Q7Z3B3.
PRIDEi Q7Z3B3.

Protocols and materials databases

DNASUi 284058.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262419 ; ENSP00000262419 ; ENSG00000120071 . [Q7Z3B3-1 ]
ENST00000432791 ; ENSP00000387393 ; ENSG00000120071 . [Q7Z3B3-1 ]
ENST00000572904 ; ENSP00000461484 ; ENSG00000120071 . [Q7Z3B3-1 ]
ENST00000574590 ; ENSP00000461812 ; ENSG00000120071 . [Q7Z3B3-1 ]
GeneIDi 284058.
KEGGi hsa:284058.
UCSCi uc002ikc.3. human. [Q7Z3B3-1 ]
uc010wkb.2. human. [Q7Z3B3-2 ]

Organism-specific databases

CTDi 284058.
GeneCardsi GC17M044108.
GeneReviewsi KANSL1.
HGNCi HGNC:24565. KANSL1.
HPAi HPA006874.
HPA007208.
MIMi 612452. gene.
neXtProti NX_Q7Z3B3.
Orphaneti 363958. 17q21.31 microdeletion syndrome.
363965. Koolen-De Vries syndrome due to a point mutation.
PharmGKBi PA142671604.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG87566.
HOVERGENi HBG080054.
InParanoidi Q7Z3B3.
OMAi TSANCDL.
OrthoDBi EOG7VQJF6.
PhylomeDBi Q7Z3B3.
TreeFami TF336511.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.

Miscellaneous databases

GeneWikii KIAA1267.
GenomeRNAii 284058.
NextBioi 94492.
PROi Q7Z3B3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q7Z3B3.
Bgeei Q7Z3B3.
CleanExi HS_KIAA1267.
Genevestigatori Q7Z3B3.

Family and domain databases

InterProi IPR026180. NSL1.
IPR029332. PEHE_dom.
[Graphical view ]
PANTHERi PTHR22443. PTHR22443. 1 hit.
Pfami PF15275. PEHE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
    DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-1010.
    Tissue: Brain.
  2. "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] (ISOFORM 1), VARIANT LEU-1010.
    Tissue: Teratocarcinoma.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT LEU-1010.
    Tissue: Fetal kidney, Mammary cancer and Testis.
  4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1), VARIANT LEU-1010.
    Tissue: Leukocyte and PNS.
  6. "A genomic sequence analysis of the mouse and human microtubule-associated protein tau."
    Poorkaj P., Kas A., D'Souza I., Zhou Y., Pham Q., Stone M., Olson M.V., Schellenberg G.D.
    Mamm. Genome 12:700-712(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
    Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
    Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
  8. "A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16."
    Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.
    Mol. Cell. Biol. 25:9175-9188(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MULTIPROTEIN COMPLEX.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Nuclear pore components are involved in the transcriptional regulation of dosage compensation in Drosophila."
    Mendjan S., Taipale M., Kind J., Holz H., Gebhardt P., Schelder M., Vermeulen M., Buscaino A., Duncan K., Mueller J., Wilm M., Stunnenberg H.G., Saumweber H., Akhtar A.
    Mol. Cell 21:811-823(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NSL COMPLEX, INTERACTION WITH KAT8.
  11. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268; SER-991 AND THR-1003, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; SER-268 AND SER-1045, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex."
    Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L., Washburn M.P., Conaway J.W., Conaway R.C.
    J. Biol. Chem. 285:4268-4272(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, SUBCELLULAR LOCATION.
  16. "The nonspecific lethal complex is a transcriptional regulator in Drosophila."
    Raja S.J., Charapitsa I., Conrad T., Vaquerizas J.M., Gebhardt P., Holz H., Kadlec J., Fraterman S., Luscombe N.M., Akhtar A.
    Mol. Cell 38:827-841(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KAT8.
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268; SER-991 AND THR-1003, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1."
    Kadlec J., Hallacli E., Lipp M., Holz H., Sanchez-Weatherby J., Cusack S., Akhtar A.
    Nat. Struct. Mol. Biol. 18:142-149(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KAT8, MUTAGENESIS OF GLU-910; PHE-917 AND HIS-921.
  19. "Structural insight into the regulation of MOF in the male-specific lethal complex and the non-specific lethal complex."
    Huang J., Wan B., Wu L., Yang Y., Dou Y., Lei M.
    Cell Res. 22:1078-1081(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NSL COMPLEX, INTERACTION WITH KAT8, MUTAGENESIS OF 852-ARG--ARG-855; 856-GLY--SER-859; 860-PHE--ASN-863; 864-ASN--ILE-867 AND 868-PRO--VAL-871.

Entry informationi

Entry nameiKANL1_HUMAN
AccessioniPrimary (citable) accession number: Q7Z3B3
Secondary accession number(s): A8K5E4
, Q6AW85, Q8IYH1, Q9BRH0, Q9NTE7, Q9UFT0, Q9ULF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 31, 2011
Last modified: September 3, 2014
This is version 96 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 17
    Human chromosome 17: 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

External Data

Dasty 3

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