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Q7Z3B3 (KANL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:KANSL1
Synonyms:KIAA1267, MSL1V1, NSL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1105 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.15 Ref.19

Subunit structure

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. Ref.7 Ref.8 Ref.10 Ref.15 Ref.16 Ref.18 Ref.19

Subcellular location

Nucleus Ref.15.

Tissue specificity

Expressed in the brain. Ref.6

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CCDC85BQ158342EBI-740244,EBI-739674

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7Z3B3-1)

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.
Isoform 2 (identifier: Q7Z3B3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-669: Missing.
     670-673: AFPD → MFLA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11051105KAT8 regulatory NSL complex subunit 1
PRO_0000234565

Regions

Region850 – 88233Required for activation of KAT8 histone acetyltransferase activity
Region883 – 1105223Sufficient for interaction with KAT8
Coiled coil283 – 31432 Potential

Amino acid modifications

Modified residue1041N6-acetyllysine Ref.14
Modified residue2491Phosphoserine Ref.12
Modified residue2681Phosphoserine Ref.11 Ref.12 Ref.13 Ref.17
Modified residue9911Phosphoserine Ref.11 Ref.17
Modified residue10031Phosphothreonine Ref.11 Ref.17
Modified residue10451Phosphoserine Ref.12

Natural variations

Alternative sequence1 – 669669Missing in isoform 2.
VSP_041132
Alternative sequence670 – 6734AFPD → MFLA in isoform 2.
VSP_041133
Natural variant1041K → T.
Corresponds to variant rs17585974 [ dbSNP | Ensembl ].
VAR_049515
Natural variant2211T → I.
Corresponds to variant rs17662853 [ dbSNP | Ensembl ].
VAR_049516
Natural variant2251N → D.
Corresponds to variant rs35643216 [ dbSNP | Ensembl ].
VAR_049517
Natural variant7181S → P.
Corresponds to variant rs34043286 [ dbSNP | Ensembl ].
VAR_049518
Natural variant10101P → L. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs7220988 [ dbSNP | Ensembl ].
VAR_026287
Natural variant10851I → T.
Corresponds to variant rs34579536 [ dbSNP | Ensembl ].
VAR_049519

Experimental info

Mutagenesis852 – 8554RRRR → AAAA: Abolishes KAT8 histone acetyltransferase activity.
Mutagenesis856 – 8594GESS → AAAA: Strongly reduces KAT8 histone acetyltransferase activity.
Mutagenesis860 – 8634FDIN → AAAA: Strongly reduces KAT8 histone acetyltransferase activity.
Mutagenesis864 – 8674NIVI → AAAA: Abolishes KAT8 histone acetyltransferase activity. Ref.19
Mutagenesis868 – 8714PMSV → AAAA: Reduces KAT8 histone acetyltransferase activity. Ref.19
Mutagenesis9101E → R: Abolishes interaction with KAT8. Ref.18
Mutagenesis9171F → R: No effect on interaction with KAT8. Ref.18
Mutagenesis9211H → R: Abolishes interaction with KAT8. Ref.18
Sequence conflict5251R → P in BAA86581. Ref.1
Sequence conflict5251R → P in BAF83948. Ref.2
Sequence conflict5251R → P in CAD97958. Ref.3
Sequence conflict5251R → P in AAH98376. Ref.4
Sequence conflict5301I → F in CAB70694. Ref.3
Sequence conflict6831S → G in CAH10565. Ref.3
Sequence conflict8491Missing in BAF83948. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 31, 2011. Version 2.
Checksum: B69D11BC522B9CAD

FASTA1,105121,025
        10         20         30         40         50         60 
MAAMAPALTD AAAEAHHIRF KLAPPSSTLS PGSAENNGNA NILIAANGTK RKAIAAEDPS 

        70         80         90        100        110        120 
LDFRNNPTKE DLGKLQPLVA SYLCSDVTSV PSKESLKLQG VFSKQTVLKS HPLLSQSYEL 

       130        140        150        160        170        180 
RAELLGRQPV LEFSLENLRT MNTSGQTALP QAPVNGLAKK LTKSSTHSDH DNSTSLNGGK 

       190        200        210        220        230        240 
RALTSSALHG GEMGGSESGD LKGGMTNCTL PHRSLDVEHT TLYSNNSTAN KSSVNSMEQP 

       250        260        270        280        290        300 
ALQGSSRLSP GTDSSSNLGG VKLEGKKSPL SSILFSALDS DTRITALLRR QADIESRARR 

       310        320        330        340        350        360 
LQKRLQVVQA KQVERHIQHQ LGGFLEKTLS KLPNLESLRP RSQLMLTRKA EAALRKAASE 

       370        380        390        400        410        420 
TTTSEGLSNF LKSNSISEEL ERFTASGIAN LRCSEQAFDS DVTDSSSGGE SDIEEEELTR 

       430        440        450        460        470        480 
ADPEQRHVPL RRRSEWKWAA DRAAIVSRWN WLQAHVSDLE YRIRQQTDIY KQIRANKGLI 

       490        500        510        520        530        540 
VLGEVPPPEH TTDLFLPLSS EVKTDHGTDK LIESVSQPLE NHGARIIGHI SESLSTKSCG 

       550        560        570        580        590        600 
ALRPVNGVIN TLQPVLADHI PGDSSDAEEQ LHKKQRLNLV SSSSDGTCVA ARTRPVLSCK 

       610        620        630        640        650        660 
KRRLVRPNSI VPLSKKVHRN STIRPGCDVN PSCALCGSGS INTMPPEIHY EAPLLERLSQ 

       670        680        690        700        710        720 
LDSCVHPVLA FPDDVPTSLH FQSMLKSQWQ NKPFDKIKPP KKLSLKHRAP MPGSLPDSAR 

       730        740        750        760        770        780 
KDRHKLVSSF LTTAKLSHHQ TRPDRTHRQH LDDVGAVPMV ERVTAPKAER LLNPPPPVHD 

       790        800        810        820        830        840 
PNHSKMRLRD HSSERSEVLK HHTDMSSSSY LAATHHPPHS PLVRQLSTSS DSPAPASSSS 

       850        860        870        880        890        900 
QVTASTSQQP VRRRRGESSF DINNIVIPMS VAATTRVEKL QYKEILTPSW REVDLQSLKG 

       910        920        930        940        950        960 
SPDEENEEIE DLSDAAFAAL HAKCEEMERA RWLWTTSVPP QRRGSRSYRS SDGRTTPQLG 

       970        980        990       1000       1010       1020 
SANPSTPQPA SPDVSSSHSL SEYSHGQSPR SPISPELHSA PLTPVARDTP RHLASEDTRC 

      1030       1040       1050       1060       1070       1080 
STPELGLDEQ SVQPWERRTF PLAHSPQAEC EDQLDAQERA ARCTRRTSGS KTGRETEAAP 

      1090       1100 
TSPPIVPLKS RHLVAAATAQ RPTHR 

« Hide

Isoform 2 [UniParc].

Checksum: EFA2A4A2BE70F67E
Show »

FASTA43648,445

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11503.1. [Q7Z3B3-1]
PIRT17259.
T46385.
RefSeqNP_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.
UniGeneHs.648744.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4CY1X-ray1.50C/D585-598[»]
4CY2X-ray2.00D585-598[»]
ProteinModelPortalQ7Z3B3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid129744. 24 interactions.
IntActQ7Z3B3. 20 interactions.
MINTMINT-1183636.
STRING9606.ENSP00000262419.

PTM databases

PhosphoSiteQ7Z3B3.

Polymorphism databases

DMDM334302834.

Proteomic databases

MaxQBQ7Z3B3.
PaxDbQ7Z3B3.
PRIDEQ7Z3B3.

Protocols and materials databases

DNASU284058.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262419; ENSP00000262419; ENSG00000120071. [Q7Z3B3-1]
ENST00000432791; ENSP00000387393; ENSG00000120071. [Q7Z3B3-1]
ENST00000572904; ENSP00000461484; ENSG00000120071. [Q7Z3B3-1]
ENST00000574590; ENSP00000461812; ENSG00000120071. [Q7Z3B3-1]
GeneID284058.
KEGGhsa:284058.
UCSCuc002ikc.3. human. [Q7Z3B3-1]
uc010wkb.2. human. [Q7Z3B3-2]

Organism-specific databases

CTD284058.
GeneCardsGC17M044108.
GeneReviewsKANSL1.
HGNCHGNC:24565. KANSL1.
HPAHPA006874.
HPA007208.
MIM612452. gene.
neXtProtNX_Q7Z3B3.
Orphanet363958. 17q21.31 microdeletion syndrome.
363965. Koolen-De Vries syndrome due to a point mutation.
PharmGKBPA142671604.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG87566.
HOVERGENHBG080054.
InParanoidQ7Z3B3.
OMATSANCDL.
OrthoDBEOG7VQJF6.
PhylomeDBQ7Z3B3.
TreeFamTF336511.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.

Gene expression databases

ArrayExpressQ7Z3B3.
BgeeQ7Z3B3.
CleanExHS_KIAA1267.
GenevestigatorQ7Z3B3.

Family and domain databases

InterProIPR026180. NSL1.
IPR029332. PEHE_dom.
[Graphical view]
PANTHERPTHR22443. PTHR22443. 1 hit.
PfamPF15275. PEHE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiKIAA1267.
GenomeRNAi284058.
NextBio94492.
PROQ7Z3B3.
SOURCESearch...

Entry information

Entry nameKANL1_HUMAN
AccessionPrimary (citable) accession number: Q7Z3B3
Secondary accession number(s): A8K5E4 expand/collapse secondary AC list , Q6AW85, Q8IYH1, Q9BRH0, Q9NTE7, Q9UFT0, Q9ULF3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 31, 2011
Last modified: July 9, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM