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Q9BZ95 (NSD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase NSD3

EC=2.1.1.43
Alternative name(s):
Nuclear SET domain-containing protein 3
Protein whistle
WHSC1-like 1 isoform 9 with methyltransferase activity to lysine
Wolf-Hirschhorn syndrome candidate 1-like protein 1
Short name=WHSC1-like protein 1
Gene names
Name:WHSC1L1
Synonyms:NSD3
ORF Names:DC28
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1437 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone methyltransferase. Preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression. Ref.9

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.9

Subunit structure

Interacts with BRD4. Ref.11

Subcellular location

Nucleus By similarity. Chromosome By similarity.

Tissue specificity

Highly expressed in brain, heart and skeletal muscle. Expressed at lower level in liver and lung. Ref.2

Involvement in disease

Defects in WHSC1L1 may be involved in non small cell lung carcinomas (NSCLC). Amplified or overexpressed in NSCLC. Ref.8

A chromosomal aberration involving WHSC1L1 is found in childhood acute myeloid leukemia. Translocation t(8;11)(p11.2;p15) with NUP98.

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily.

Contains 1 AWS domain.

Contains 4 PHD-type zinc fingers.

Contains 1 post-SET domain.

Contains 2 PWWP domains.

Contains 1 SET domain.

Sequence caution

The sequence AAG44637.1 differs from that shown. Reason: Frameshift at several positions.

The sequence AAI07735.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAA91110.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BZ95-1)

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: Q9BZ95-2)

The sequence of this isoform differs from the canonical sequence as follows:
     871-919: Missing.
Isoform 3 (identifier: Q9BZ95-3)

The sequence of this isoform differs from the canonical sequence as follows:
     620-645: ASEISDSCKPLKKRSRASTDVEMTSS → SADRGVQGSVRFSDSSVSAAIEETVD
     646-1437: Missing.
Isoform 4 (identifier: Q9BZ95-4)

The sequence of this isoform differs from the canonical sequence as follows:
     67-129: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14371437Histone-lysine N-methyltransferase NSD3
PRO_0000259521

Regions

Domain270 – 33364PWWP 1
Domain960 – 102263PWWP 2
Domain1093 – 114351AWS
Domain1145 – 1262118SET
Domain1269 – 128517Post-SET
Zinc finger701 – 74848PHD-type 1
Zinc finger749 – 80557PHD-type 2
Zinc finger862 – 95594PHD-type 3
Zinc finger1321 – 136848PHD-type 4; atypical
Coiled coil1033 – 106937 Potential

Amino acid modifications

Modified residue1501Phosphoserine Ref.12
Modified residue7901N6-acetyllysine Ref.10

Natural variations

Alternative sequence67 – 12963Missing in isoform 4.
VSP_021427
Alternative sequence620 – 64526ASEIS…EMTSS → SADRGVQGSVRFSDSSVSAA IEETVD in isoform 3.
VSP_021428
Alternative sequence646 – 1437792Missing in isoform 3.
VSP_021429
Alternative sequence871 – 91949Missing in isoform 2.
VSP_021430
Natural variant1861T → M.
Corresponds to variant rs13034 [ dbSNP | Ensembl ].
VAR_061215
Natural variant3831R → P.
Corresponds to variant rs2234552 [ dbSNP | Ensembl ].
VAR_028950

Experimental info

Sequence conflict4361G → R in AAI15007. Ref.6
Sequence conflict5781R → G in AAI15007. Ref.6
Sequence conflict8291G → E in CAC28350. Ref.2
Sequence conflict8291G → E in CAC28351. Ref.2
Sequence conflict9261C → R in AAI15007. Ref.6
Sequence conflict13081K → R in AAI15007. Ref.6
Sequence conflict14301D → G in AAI15007. Ref.6

Secondary structure

........................................... 1437
Helix Strand Turn

Details...

Sequences

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

Last modified June 1, 2001. Version 1.
Checksum: 87E54997A996F7CC

FASTA1,437161,613
        10         20         30         40         50         60 
MDFSFSFMQG IMGNTIQQPP QLIDSANIRQ EDAFDNNSDI AEDGGQTPYE ATLQQGFQYP 

        70         80         90        100        110        120 
ATTEDLPPLT NGYPSSISVY ETQTKYQSYN QYPNGSANGF GAVRNFSPTD YYHSEIPNTR 

       130        140        150        160        170        180 
PHEILEKPSP PQPPPPPSVP QTVIPKKTGS PEIKLKITKT IQNGRELFES SLCGDLLNEV 

       190        200        210        220        230        240 
QASEHTKSKH ESRKEKRKKS NKHDSSRSEE RKSHKIPKLE PEEQNRPNER VDTVSEKPRE 

       250        260        270        280        290        300 
EPVLKEEAPV QPILSSVPTT EVSTGVKFQV GDLVWSKVGT YPWWPCMVSS DPQLEVHTKI 

       310        320        330        340        350        360 
NTRGAREYHV QFFSNQPERA WVHEKRVREY KGHKQYEELL AEATKQASNH SEKQKIRKPR 

       370        380        390        400        410        420 
PQRERAQWDI GIAHAEKALK MTREERIEQY TFIYIDKQPE EALSQAKKSV ASKTEVKKTR 

       430        440        450        460        470        480 
RPRSVLNTQP EQTNAGEVAS SLSSTEIRRH SQRRHTSAEE EEPPPVKIAW KTAAARKSLP 

       490        500        510        520        530        540 
ASITMHKGSL DLQKCNMSPV VKIEQVFALQ NATGDGKFID QFVYSTKGIG NKTEISVRGQ 

       550        560        570        580        590        600 
DRLIISTPNQ RNEKPTQSVS SPEATSGSTG SVEKKQQRRS IRTRSESEKS TEVVPKKKIK 

       610        620        630        640        650        660 
KEQVETVPQA TVKTGLQKGA SEISDSCKPL KKRSRASTDV EMTSSAYRDT SDSDSRGLSD 

       670        680        690        700        710        720 
LQVGFGKQVD SPSATADADV SDVQSMDSSL SRRGTGMSKK DTVCQICESS GDSLIPCEGE 

       730        740        750        760        770        780 
CCKHFHLECL GLASLPDSKF ICMECKTGQH PCFSCKVSGK DVKRCSVGAC GKFYHEACVR 

       790        800        810        820        830        840 
KFPTAIFESK GFRCPQHCCS ACSMEKDIHK ASKGRMMRCL RCPVAYHSGD ACIAAGSMLV 

       850        860        870        880        890        900 
SSYILICSNH SKRSSNSSAV NVGFCFVCAR GLIVQDHSDP MFSSYAYKSH YLLNESNRAE 

       910        920        930        940        950        960 
LMKLPMIPSS SASKKKCEKG GRLLCCESCP ASFHPECLSI EMPEGCWNCN DCKAGKKLHY 

       970        980        990       1000       1010       1020 
KQIVWVKLGN YRWWPAEICN PRSVPLNIQG LKHDLGDFPV FFFGSHDYYW VHQGRVFPYV 

      1030       1040       1050       1060       1070       1080 
EGDKSFAEGQ TSINKTFKKA LEEAAKRFQE LKAQRESKEA LEIEKNSRKP PPYKHIKANK 

      1090       1100       1110       1120       1130       1140 
VIGKVQIQVA DLSEIPRCNC KPADENPCGL ESECLNRMLQ YECHPQVCPA GDRCQNQCFT 

      1150       1160       1170       1180       1190       1200 
KRLYPDAEII KTERRGWGLR TKRSIKKGEF VNEYVGELID EEECRLRIKR AHENSVTNFY 

      1210       1220       1230       1240       1250       1260 
MLTVTKDRII DAGPKGNYSR FMNHSCNPNC ETQKWTVNGD VRVGLFALCD IPAGMELTFN 

      1270       1280       1290       1300       1310       1320 
YNLDCLGNGR TECHCGADNC SGFLGVRPKS ACASTNEEKA KNAKLKQKRR KIKTEPKQMH 

      1330       1340       1350       1360       1370       1380 
EDYCFQCGDG GELVMCDKKD CPKAYHLLCL NLTQPPYGKW ECPWHQCDEC SSAAVSFCEF 

      1390       1400       1410       1420       1430 
CPHSFCKDHE KGALVPSALE GRLCCSEHDP MAPVSPEYWS KIKCKWESQD HGEEVKE 

« Hide

Isoform 2 [UniParc].

Checksum: 0832BD51DAB0DCFF
Show »

FASTA1,388156,070
Isoform 3 [UniParc].

Checksum: DE98E24AB088AC91
Show »

FASTA64572,621
Isoform 4 [UniParc].

Checksum: 3013E618C16E19E0
Show »

FASTA1,374154,519

References

« Hide 'large scale' references
[1]"WHSC1L1, on human chromosome 8p11.2, closely resembles WHSC1 and maps to a duplicated region shared with 4p16.3."
Stec I., van Ommen G.-J.B., den Dunnen J.T.
Genomics 76:5-8(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
[2]"NSD3, a new SET domain-containing gene, maps to 8p12 and is amplified in human breast cancer cell lines."
Angrand P.-O., Apiou F., Stewart F., Dutrillaux B., Losson R., Chambon P.
Genomics 74:79-88(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY.
[3]"A novel gene from human dendritic cells."
Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Dendritic cell.
[4]"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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-383 (ISOFORM 4).
Tissue: Brain and Teratocarcinoma.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 AND 3).
Tissue: Brain and Placenta.
[7]"NUP98 is fused to the NSD3 gene in acute myeloid leukemia associated with t(8;11)(p11.2;p15)."
Rosati R., La Starza R., Veronese A., Aventin A., Schwienbacher C., Vallespi T., Negrini M., Martelli M.F., Mecucci C.
Blood 99:3857-3860(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH NUP98.
[8]"High-resolution genomic profiles of human lung cancer."
Tonon G., Wong K.-K., Maulik G., Brennan C., Feng B., Zhang Y., Khatry D.B., Protopopov A., You M.J., Aguirre A.J., Martin E.S., Yang Z., Ji H., Chin L., Depinho R.A.
Proc. Natl. Acad. Sci. U.S.A. 102:9625-9630(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN NSCLC.
[9]"Characterization of a novel WHSC1-associated SET domain protein with H3K4 and H3K27 methyltransferase activity."
Kim S.M., Kee H.J., Eom G.H., Choe N.W., Kim J.Y., Kim Y.S., Kim S.K., Kook H., Kook H., Seo S.B.
Biochem. Biophys. Res. Commun. 345:318-323(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY, FUNCTION.
[10]"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-790, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"The Brd4 extraterminal domain confers transcription activation independent of pTEFb by recruiting multiple proteins, including NSD3."
Rahman S., Sowa M.E., Ottinger M., Smith J.A., Shi Y., Harper J.W., Howley P.M.
Mol. Cell. Biol. 31:2641-2652(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BRD4.
[12]"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-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Solution structure of second PWWP domain of WHSC1L1 protein."
RIKEN structural genomics initiative (RSGI)
Submitted (DEC-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 957-1053.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF332468 mRNA. Translation: AAK00354.1.
AF332469 mRNA. Translation: AAK00355.1.
AJ295990 mRNA. Translation: CAC28350.1.
AJ295991 mRNA. Translation: CAC28351.1.
AJ295992 mRNA. Translation: CAC28352.1.
AF255649 mRNA. Translation: AAG44637.1. Frameshift.
AK000360 mRNA. Translation: BAA91110.1. Different initiation.
AK022560 mRNA. Translation: BAB14099.1.
AK127594 mRNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63320.1.
CH471080 Genomic DNA. Translation: EAW63321.1.
BC012059 mRNA. Translation: AAH12059.1.
BC062631 mRNA. Translation: AAH62631.1.
BC101717 mRNA. Translation: AAI01718.1.
BC107734 mRNA. Translation: AAI07735.1. Sequence problems.
BC113469 mRNA. Translation: AAI13470.1.
BC115006 mRNA. Translation: AAI15007.1.
RefSeqNP_060248.2. NM_017778.2.
NP_075447.1. NM_023034.1.
XP_005273605.1. XM_005273548.1.
UniGeneHs.434966.
Hs.608111.
Hs.655314.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DAQNMR-A957-1053[»]
4GNDX-ray2.27A/C1310-1413[»]
4GNEX-ray1.47A1310-1413[»]
4GNFX-ray1.55A1310-1413[»]
4GNGX-ray1.73A/D1310-1413[»]
ProteinModelPortalQ9BZ95.
SMRQ9BZ95. Positions 263-390, 699-834, 919-955, 957-1285, 1316-1413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120250. 19 interactions.
IntActQ9BZ95. 16 interactions.
MINTMINT-4830664.

PTM databases

PhosphoSiteQ9BZ95.

Polymorphism databases

DMDM74761342.

Proteomic databases

PaxDbQ9BZ95.
PRIDEQ9BZ95.

Protocols and materials databases

DNASU54904.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316985; ENSP00000313410; ENSG00000147548. [Q9BZ95-3]
ENST00000317025; ENSP00000313983; ENSG00000147548. [Q9BZ95-1]
ENST00000433384; ENSP00000393284; ENSG00000147548. [Q9BZ95-2]
GeneID54904.
KEGGhsa:54904.
UCSCuc003xli.3. human. [Q9BZ95-1]
uc003xlj.3. human. [Q9BZ95-3]
uc010lwe.3. human. [Q9BZ95-2]

Organism-specific databases

CTD54904.
GeneCardsGC08M038151.
HGNCHGNC:12767. WHSC1L1.
HPACAB013721.
HPA005659.
HPA018893.
MIM607083. gene.
neXtProtNX_Q9BZ95.
PharmGKBPA37370.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2940.
HOVERGENHBG079979.
InParanoidQ9BZ95.
KOK11425.
OMAMEKDIHK.
OrthoDBEOG7Z69BG.
PhylomeDBQ9BZ95.
TreeFamTF329088.

Gene expression databases

ArrayExpressQ9BZ95.
BgeeQ9BZ95.
GenevestigatorQ9BZ95.

Family and domain databases

Gene3D3.30.40.10. 3 hits.
InterProIPR006560. AWS.
IPR003616. Post-SET_dom.
IPR000313. PWWP_dom.
IPR001214. SET_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF00855. PWWP. 2 hits.
PF00856. SET. 1 hit.
[Graphical view]
SMARTSM00570. AWS. 1 hit.
SM00249. PHD. 5 hits.
SM00508. PostSET. 1 hit.
SM00293. PWWP. 2 hits.
SM00184. RING. 2 hits.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 3 hits.
PROSITEPS51215. AWS. 1 hit.
PS50868. POST_SET. 1 hit.
PS50812. PWWP. 2 hits.
PS50280. SET. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSWHSC1L1. human.
EvolutionaryTraceQ9BZ95.
GeneWikiWHSC1L1.
GenomeRNAi54904.
NextBio57940.
PROQ9BZ95.
SOURCESearch...

Entry information

Entry nameNSD3_HUMAN
AccessionPrimary (citable) accession number: Q9BZ95
Secondary accession number(s): D3DSX1 expand/collapse secondary AC list , Q1RMD3, Q3B796, Q6ZSA5, Q9BYU8, Q9BYU9, Q9H2M8, Q9H9W9, Q9NXA6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 123 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

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 8

Human chromosome 8: entries, gene names and cross-references to MIM