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Q9NRC8

- SIR7_HUMAN

UniProt

Q9NRC8 - SIR7_HUMAN

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Protein
NAD-dependent protein deacetylase sirtuin-7
Gene
SIRT7, SIR2L7
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

NAD-dependent protein deacetylase that specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac). In contrast to other histone deacetylases, displays selectivity for a single histone mark, H3K18Ac, directly linked to control of gene expression. H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors. SIRT7 thereby acts as a transcription repressor. Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed phenotype of cancer cells. These data suggest that SIRT7 may play a key role in oncogenic transformation by suppresses expression of tumor suppressor genes by locus-specific deacetylation of H3K18Ac at promoter regions. Also required to restore the transcription of ribosomal RNA (rRNA) at the exit from mitosis: promotes the association of RNA polymerase I with the rDNA promoter region and coding region. Stimulates transcription activity of the RNA polymerase I complex. May also deacetylate p53/TP53 and promotes cell survival, however such data need additional confirmation.3 Publications

Catalytic activityi

NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.1 Publication

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei187 – 1871Proton acceptor
Metal bindingi195 – 1951Zinc By similarity
Metal bindingi198 – 1981Zinc By similarity
Metal bindingi225 – 2251Zinc By similarity
Metal bindingi228 – 2281Zinc By similarity
Binding sitei315 – 3151NAD; via amide nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi107 – 12620NAD By similarity
Add
BLAST
Nucleotide bindingi167 – 1704NAD By similarity
Nucleotide bindingi268 – 2703NAD By similarity
Nucleotide bindingi297 – 2993NAD By similarity

GO - Molecular functioni

  1. NAD+ binding Source: InterPro
  2. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB
  3. chromatin binding Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
  5. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. histone H3 deacetylation Source: UniProtKB
  2. histone H4 deacetylation Source: GOC
  3. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  4. positive regulation of transcription on exit from mitosis Source: UniProtKB
  5. rRNA transcription Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, NAD, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
NAD-dependent protein deacetylase sirtuin-7 (EC:3.5.1.-)
Alternative name(s):
Regulatory protein SIR2 homolog 7
SIR2-like protein 7
Gene namesi
Name:SIRT7
Synonyms:SIR2L7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:14935. SIRT7.

Subcellular locationi

Cytoplasm. Nucleusnucleolus
Note: Located close to the nuclear membrane when in the cytoplasm. Associated with chromatin. Associated with rDNA promoter and transcribed region. Associated with nucleolar organizer regions during mitosis.6 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleolus Source: UniProtKB
  3. nucleolus organizer region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi111 – 1111S → A: Abolishes activation of pre-rRNA synthesis. 2 Publications
Mutagenesisi187 – 1871H → Y: Abolishes deacetylase activity and activation of pre-rRNA synthesis. 2 Publications

Organism-specific databases

PharmGKBiPA37940.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 400400NAD-dependent protein deacetylase sirtuin-7
PRO_0000110271Add
BLAST

Post-translational modificationi

Phosphorylated during mitosis Inferred.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NRC8.
PaxDbiQ9NRC8.
PRIDEiQ9NRC8.

Expressioni

Gene expression databases

ArrayExpressiQ9NRC8.
BgeeiQ9NRC8.
CleanExiHS_SIRT7.
GenevestigatoriQ9NRC8.

Organism-specific databases

HPAiCAB037261.

Interactioni

Subunit structurei

Interacts with UBTF and the RNA polymerase I complex. Interacts with components of the B-WICH complex, such as MYBBP1A, SMARCA5/SNF2H and BAZ1B/WSTF. Interacts with ELK4, leading to stabilization at target promoters for H3K18Ac deacetylation. Interacts with histone H2A and/or histone H2B.4 Publications

Protein-protein interaction databases

BioGridi119602. 661 interactions.
DIPiDIP-59906N.
IntActiQ9NRC8. 2 interactions.
MINTiMINT-1424083.
STRINGi9606.ENSP00000329466.

Structurei

3D structure databases

ProteinModelPortaliQ9NRC8.
SMRiQ9NRC8. Positions 77-339.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini90 – 331242Deacetylase sirtuin-type
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi8 – 7467Arg-rich
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0846.
HOGENOMiHOG000231240.
HOVERGENiHBG060028.
InParanoidiQ9NRC8.
KOiK11417.
OMAiWFGRGCA.
OrthoDBiEOG7M98GV.
PhylomeDBiQ9NRC8.
TreeFamiTF106184.

Family and domain databases

Gene3Di3.40.50.1220. 2 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR026590. Ssirtuin_cat_dom.
[Graphical view]
PANTHERiPTHR11085. PTHR11085. 1 hit.
PfamiPF02146. SIR2. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
PROSITEiPS50305. SIRTUIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NRC8-1) [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

MAAGGLSRSE RKAAERVRRL REEQQRERLR QVSRILRKAA AERSAEEGRL    50
LAESADLVTE LQGRSRRREG LKRRQEEVCD DPEELRGKVR ELASAVRNAK 100
YLVVYTGAGI STAASIPDYR GPNGVWTLLQ KGRSVSAADL SEAEPTLTHM 150
SITRLHEQKL VQHVVSQNCD GLHLRSGLPR TAISELHGNM YIEVCTSCVP 200
NREYVRVFDV TERTALHRHQ TGRTCHKCGT QLRDTIVHFG ERGTLGQPLN 250
WEAATEAASR ADTILCLGSS LKVLKKYPRL WCMTKPPSRR PKLYIVNLQW 300
TPKDDWAALK LHGKCDDVMR LLMAELGLEI PAYSRWQDPI FSLATPLRAG 350
EEGSHSRKSL CRSREEAPPG DRGAPLSSAP ILGGWFGRGC TKRTKRKKVT 400
Length:400
Mass (Da):44,898
Last modified:October 1, 2000 - v1
Checksum:i55D7736A864AFE6F
GO
Isoform 2 (identifier: Q9NRC8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     162-183: QHVVSQNCDGLHLRSGLPRTAI → RALGGWYTCQGPGRAPWCPVGN
     184-400: Missing.

Note: No experimental confirmation available.

Show »
Length:183
Mass (Da):20,404
Checksum:iEC211D79031585C2
GO
Isoform 3 (identifier: Q9NRC8-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: MAAGGLSRSERKAAERVRRLREEQQRERLR → MPGPRRRSPSACP
     336-400: WQDPIFSLATPLRAGEEGSHSRKSLCRSREEAPPGDRGAPLSSAPILGGWFGRGCTKRTKRKKVT → VL

Note: No experimental confirmation available.

Show »
Length:320
Mass (Da):35,851
Checksum:iC0E80615256EEA7A
GO

Sequence cautioni

The sequence CAB70848.2 differs from that shown. Reason:

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3030MAAGG…RERLR → MPGPRRRSPSACP in isoform 3.
VSP_044396Add
BLAST
Alternative sequencei162 – 18322QHVVS…PRTAI → RALGGWYTCQGPGRAPWCPV GN in isoform 2.
VSP_008736Add
BLAST
Alternative sequencei184 – 400217Missing in isoform 2.
VSP_008737Add
BLAST
Alternative sequencei336 – 40065WQDPI…RKKVT → VL in isoform 3.
VSP_044397Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711L → Q in BAG52860. 1 Publication
Sequence conflicti384 – 3841G → S in BAF82954. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF233395 mRNA. Translation: AAF43431.1.
AK002027 mRNA. Translation: BAA92044.1.
AK094326 mRNA. Translation: BAG52860.1.
AK290265 mRNA. Translation: BAF82954.1.
AC145207 Genomic DNA. No translation available.
BC017305 mRNA. Translation: AAH17305.1.
BC101791 mRNA. Translation: AAI01792.1.
BC101793 mRNA. Translation: AAI01794.1.
AL137626 mRNA. Translation: CAB70848.2. Sequence problems.
CCDSiCCDS11792.1. [Q9NRC8-1]
PIRiT46324.
RefSeqiNP_057622.1. NM_016538.2. [Q9NRC8-1]
UniGeneiHs.514636.

Genome annotation databases

EnsembliENST00000328666; ENSP00000329466; ENSG00000187531. [Q9NRC8-1]
GeneIDi51547.
KEGGihsa:51547.
UCSCiuc002kcj.2. human. [Q9NRC8-1]

Polymorphism databases

DMDMi38258650.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF233395 mRNA. Translation: AAF43431.1 .
AK002027 mRNA. Translation: BAA92044.1 .
AK094326 mRNA. Translation: BAG52860.1 .
AK290265 mRNA. Translation: BAF82954.1 .
AC145207 Genomic DNA. No translation available.
BC017305 mRNA. Translation: AAH17305.1 .
BC101791 mRNA. Translation: AAI01792.1 .
BC101793 mRNA. Translation: AAI01794.1 .
AL137626 mRNA. Translation: CAB70848.2 . Sequence problems.
CCDSi CCDS11792.1. [Q9NRC8-1 ]
PIRi T46324.
RefSeqi NP_057622.1. NM_016538.2. [Q9NRC8-1 ]
UniGenei Hs.514636.

3D structure databases

ProteinModelPortali Q9NRC8.
SMRi Q9NRC8. Positions 77-339.
ModBasei Search...

Protein-protein interaction databases

BioGridi 119602. 661 interactions.
DIPi DIP-59906N.
IntActi Q9NRC8. 2 interactions.
MINTi MINT-1424083.
STRINGi 9606.ENSP00000329466.

Chemistry

ChEMBLi CHEMBL2163184.

Polymorphism databases

DMDMi 38258650.

Proteomic databases

MaxQBi Q9NRC8.
PaxDbi Q9NRC8.
PRIDEi Q9NRC8.

Protocols and materials databases

DNASUi 51547.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000328666 ; ENSP00000329466 ; ENSG00000187531 . [Q9NRC8-1 ]
GeneIDi 51547.
KEGGi hsa:51547.
UCSCi uc002kcj.2. human. [Q9NRC8-1 ]

Organism-specific databases

CTDi 51547.
GeneCardsi GC17M079869.
HGNCi HGNC:14935. SIRT7.
HPAi CAB037261.
MIMi 606212. gene.
neXtProti NX_Q9NRC8.
PharmGKBi PA37940.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0846.
HOGENOMi HOG000231240.
HOVERGENi HBG060028.
InParanoidi Q9NRC8.
KOi K11417.
OMAi WFGRGCA.
OrthoDBi EOG7M98GV.
PhylomeDBi Q9NRC8.
TreeFami TF106184.

Miscellaneous databases

ChiTaRSi SIRT7. human.
GeneWikii SIRT7.
GenomeRNAii 51547.
NextBioi 35463912.
PROi Q9NRC8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NRC8.
Bgeei Q9NRC8.
CleanExi HS_SIRT7.
Genevestigatori Q9NRC8.

Family and domain databases

Gene3Di 3.40.50.1220. 2 hits.
InterProi IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR026590. Ssirtuin_cat_dom.
[Graphical view ]
PANTHERi PTHR11085. PTHR11085. 1 hit.
Pfami PF02146. SIR2. 1 hit.
[Graphical view ]
SUPFAMi SSF52467. SSF52467. 1 hit.
PROSITEi PS50305. SIRTUIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Phylogenetic classification of prokaryotic and eukaryotic Sir-2 like proteins."
    Frye R.A.
    Biochem. Biophys. Res. Commun. 273:793-798(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Spleen.
  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] (ISOFORMS 1; 2 AND 3).
    Tissue: Cerebellum, Colon and Placenta.
  3. "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].
  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).
    Tissue: Liver and Lymph.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 128-400 (ISOFORM 1).
    Tissue: Testis.
  6. "Isolation of a SIR-like gene, SIR-T8, that is overexpressed in thyroid carcinoma cell lines and tissues."
    de Nigris F., Cerutti J., Morelli C., Califano D., Chiariotti L., Viglietto G., Santelli G., Fusco A.
    Br. J. Cancer 86:917-923(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "'SIRT8' expressed in thyroid cancer is actually SIRT7."
    Frye R.A.
    Br. J. Cancer 87:1479-1479(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SHOWS THAT SIR-T8 IS SIRT7.
  8. "Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins."
    Michishita E., Park J.Y., Burneskis J.M., Barrett J.C., Horikawa I.
    Mol. Biol. Cell 16:4623-4635(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription."
    Ford E., Voit R., Liszt G., Magin C., Grummt I., Guarente L.
    Genes Dev. 20:1075-1080(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A RNA POLYMERASE I COMPLEX, INTERACTION WITH HISTONE H2A AND/OR HISTONE H2B, MUTAGENESIS OF SER-111 AND HIS-187, SUBCELLULAR LOCATION.
  10. "Involvement of SIRT7 in resumption of rDNA transcription at the exit from mitosis."
    Grob A., Roussel P., Wright J.E., McStay B., Hernandez-Verdun D., Sirri V.
    J. Cell Sci. 122:489-498(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UBTF, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  11. "Functional proteomics establishes the interaction of SIRT7 with chromatin remodeling complexes and expands its role in regulation of RNA polymerase I transcription."
    Tsai Y.C., Greco T.M., Boonmee A., Miteva Y., Cristea I.M.
    Mol. Cell. Proteomics 11:M111.015156.01-M111.015156.17(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MYBBP1A; SMARCA5 AND BAZ1B, MUTAGENESIS OF SER-111.
  12. Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH ELK4, MUTAGENESIS OF HIS-187.

Entry informationi

Entry nameiSIR7_HUMAN
AccessioniPrimary (citable) accession number: Q9NRC8
Secondary accession number(s): A8K2K0
, B3KSU8, Q3MIK4, Q9NSZ6, Q9NUS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 121 of the entry and version 1 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

Miscellaneous

Overexpressed in human thyroid carcinoma cell lines and tissues, but not in adenomas.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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