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Protein

KAT8 regulatory NSL complex subunit 2

Gene

KANSL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.1 Publication

GO - Biological processi

  • histone H4-K16 acetylation Source: UniProtKB
  • histone H4-K5 acetylation Source: UniProtKB
  • histone H4-K8 acetylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Enzyme and pathway databases

ReactomeiR-HSA-3214847. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
KAT8 regulatory NSL complex subunit 2
Alternative name(s):
NSL complex protein NSL2
Non-specific lethal 2 homolog
Gene namesi
Name:KANSL2
Synonyms:C12orf41, NSL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:26024. KANSL2.

Subcellular locationi

GO - Cellular componenti

  • histone acetyltransferase complex Source: UniProtKB
  • NSL complex Source: GO_Central
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485371.

Polymorphism and mutation databases

BioMutaiKANSL2.
DMDMi296439400.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492KAT8 regulatory NSL complex subunit 2PRO_0000278292Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei131 – 1311PhosphothreonineCombined sources
Modified residuei147 – 1471PhosphoserineCombined sources
Modified residuei149 – 1491PhosphoserineCombined sources
Modified residuei168 – 1681PhosphoserineBy similarity
Modified residuei172 – 1721PhosphoserineBy similarity
Modified residuei175 – 1751PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9H9L4.
MaxQBiQ9H9L4.
PaxDbiQ9H9L4.
PeptideAtlasiQ9H9L4.
PRIDEiQ9H9L4.

PTM databases

iPTMnetiQ9H9L4.
PhosphoSiteiQ9H9L4.

Expressioni

Gene expression databases

BgeeiQ9H9L4.
CleanExiHS_C12orf41.
ExpressionAtlasiQ9H9L4. baseline and differential.
GenevisibleiQ9H9L4. HS.

Organism-specific databases

HPAiHPA038497.
HPA038498.

Interactioni

Subunit structurei

Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
WDR5P619642EBI-2560840,EBI-540834

Protein-protein interaction databases

BioGridi120274. 15 interactions.
IntActiQ9H9L4. 10 interactions.
MINTiMINT-3069347.
STRINGi9606.ENSP00000415436.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CY2X-ray2.00C406-417[»]
ProteinModelPortaliQ9H9L4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiENOG410II1C. Eukaryota.
ENOG4110KNV. LUCA.
GeneTreeiENSGT00650000093346.
HOGENOMiHOG000008519.
HOVERGENiHBG057179.
InParanoidiQ9H9L4.
KOiK18401.
PhylomeDBiQ9H9L4.
TreeFamiTF324169.

Family and domain databases

InterProiIPR026316. NSL2.
IPR025927. Potential_DNA-bd.
[Graphical view]
PANTHERiPTHR13453. PTHR13453. 1 hit.
PfamiPF13891. zf-C3Hc3H. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H9L4-1) [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
MNRIRIHVLP TNRGRITPVP RSQEPLSCAF THRPCSHPRL EGQEFCIKHI
60 70 80 90 100
LEDKNAPFKQ CSYISTKNGK RCPNAAPKPE KKDGVSFCAE HVRRNALALH
110 120 130 140 150
AQMKKTNPGP VGETLLCQLS SYAKTELGSQ TPESSRSEAS RILDEDSWSD
160 170 180 190 200
GEQEPITVDQ TWRGDPDSEA DSIDSDQEDP LKHAGVYTAE EVALIMREKL
210 220 230 240 250
IRLQSLYIDQ FKRLQHLLKE KKRRYLHNRK VEHEALGSSL LTGPEGLLAK
260 270 280 290 300
ERENLKRLKC LRRYRQRYGV EALLHRQLKE RRMLATDGAA QQAHTTRSSQ
310 320 330 340 350
RCLAFVDDVR CSNQSLPMTR HCLTHICQDT NQVLFKCCQG SEEVPCNKPV
360 370 380 390 400
PVSLSEDPCC PLHFQLPPQM YKPEQVLSVP DDLEAGPMDL YLSAAELQPT
410 420 430 440 450
ESLPLEFSDD LDVVGDGMQC PPSPLLFDPS LTLEDHLVKE IAEDPVDILG
460 470 480 490
QMQMAGDGCR SQGSRNSEKA SAPLSQSGLA TANGKPEPTS IS
Length:492
Mass (Da):55,042
Last modified:May 18, 2010 - v3
Checksum:i738607766A98A87A
GO
Isoform 2 (identifier: Q9H9L4-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     145-155: EDSWSDGEQEP → MLVSTQQKKWP
     156-492: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:155
Mass (Da):17,402
Checksum:iAAEB542928DA6C9D
GO

Sequence cautioni

The sequence AAH09746.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH13900.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA91169.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.Curated
The sequence BAB14211.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAD39126.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti108 – 1081P → L in BAA91169 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti313 – 3131N → S.1 Publication
Corresponds to variant rs17238800 [ dbSNP | Ensembl ].
VAR_030767
Natural varianti445 – 4451P → T.2 Publications
Corresponds to variant rs3741628 [ dbSNP | Ensembl ].
VAR_030768

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei145 – 15511EDSWSDGEQEP → MLVSTQQKKWP in isoform 2. 2 PublicationsVSP_042530Add
BLAST
Alternative sequencei156 – 492337Missing in isoform 2. 2 PublicationsVSP_042531Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000443 mRNA. Translation: BAA91169.1. Sequence problems.
AK022732 mRNA. Translation: BAB14211.1. Different initiation.
AL834467 mRNA. Translation: CAD39126.1. Sequence problems.
AC079951 Genomic DNA. No translation available.
BC009746 mRNA. Translation: AAH09746.1. Different initiation.
BC013900 mRNA. Translation: AAH13900.1. Different initiation.
CCDSiCCDS44869.1. [Q9H9L4-1]
RefSeqiNP_060292.3. NM_017822.3. [Q9H9L4-1]
UniGeneiHs.505412.

Genome annotation databases

EnsembliENST00000420613; ENSP00000415436; ENSG00000139620. [Q9H9L4-1]
ENST00000546701; ENSP00000448131; ENSG00000139620. [Q9H9L4-4]
GeneIDi54934.
KEGGihsa:54934.
UCSCiuc001rrx.4. human. [Q9H9L4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000443 mRNA. Translation: BAA91169.1. Sequence problems.
AK022732 mRNA. Translation: BAB14211.1. Different initiation.
AL834467 mRNA. Translation: CAD39126.1. Sequence problems.
AC079951 Genomic DNA. No translation available.
BC009746 mRNA. Translation: AAH09746.1. Different initiation.
BC013900 mRNA. Translation: AAH13900.1. Different initiation.
CCDSiCCDS44869.1. [Q9H9L4-1]
RefSeqiNP_060292.3. NM_017822.3. [Q9H9L4-1]
UniGeneiHs.505412.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CY2X-ray2.00C406-417[»]
ProteinModelPortaliQ9H9L4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120274. 15 interactions.
IntActiQ9H9L4. 10 interactions.
MINTiMINT-3069347.
STRINGi9606.ENSP00000415436.

PTM databases

iPTMnetiQ9H9L4.
PhosphoSiteiQ9H9L4.

Polymorphism and mutation databases

BioMutaiKANSL2.
DMDMi296439400.

Proteomic databases

EPDiQ9H9L4.
MaxQBiQ9H9L4.
PaxDbiQ9H9L4.
PeptideAtlasiQ9H9L4.
PRIDEiQ9H9L4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000420613; ENSP00000415436; ENSG00000139620. [Q9H9L4-1]
ENST00000546701; ENSP00000448131; ENSG00000139620. [Q9H9L4-4]
GeneIDi54934.
KEGGihsa:54934.
UCSCiuc001rrx.4. human. [Q9H9L4-1]

Organism-specific databases

CTDi54934.
GeneCardsiKANSL2.
H-InvDBHIX0010586.
HGNCiHGNC:26024. KANSL2.
HPAiHPA038497.
HPA038498.
MIMi615488. gene.
neXtProtiNX_Q9H9L4.
PharmGKBiPA143485371.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410II1C. Eukaryota.
ENOG4110KNV. LUCA.
GeneTreeiENSGT00650000093346.
HOGENOMiHOG000008519.
HOVERGENiHBG057179.
InParanoidiQ9H9L4.
KOiK18401.
PhylomeDBiQ9H9L4.
TreeFamiTF324169.

Enzyme and pathway databases

ReactomeiR-HSA-3214847. HATs acetylate histones.

Miscellaneous databases

ChiTaRSiKANSL2. human.
GeneWikiiC12orf41.
GenomeRNAii54934.
PROiQ9H9L4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H9L4.
CleanExiHS_C12orf41.
ExpressionAtlasiQ9H9L4. baseline and differential.
GenevisibleiQ9H9L4. HS.

Family and domain databases

InterProiIPR026316. NSL2.
IPR025927. Potential_DNA-bd.
[Graphical view]
PANTHERiPTHR13453. PTHR13453. 1 hit.
PfamiPF13891. zf-C3Hc3H. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-492 (ISOFORM 1), VARIANT THR-445.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Melanoma.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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), VARIANTS SER-313 AND THR-445.
    Tissue: Ovary and Placenta.
  5. "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.
  6. "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.
  7. "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-147 AND SER-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147 AND SER-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiKANL2_HUMAN
AccessioniPrimary (citable) accession number: Q9H9L4
Secondary accession number(s): Q8N3B5, Q96CV0, Q9NX51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: May 18, 2010
Last modified: July 6, 2016
This is version 105 of the entry and version 3 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 12
    Human chromosome 12: 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

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.