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Protein

Something about silencing protein 10

Gene

UTP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Essential for gene silencing: has a role in the structure of silenced chromatin. Plays a role in the developing brain (By similarity).By similarity

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Developmental protein

Names & Taxonomyi

Protein namesi
Recommended name:
Something about silencing protein 10
Alternative name(s):
Charged amino acid-rich leucine zipper 1
Short name:
CRL1
Disrupter of silencing SAS10
UTP3 homolog
Gene namesi
Name:UTP3
Synonyms:CRLZ1, SAS10Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:24477. UTP3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162408779.

Polymorphism and mutation databases

BioMutaiUTP3.
DMDMi76364208.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 479479Something about silencing protein 10PRO_0000114326Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371PhosphoserineCombined sources
Modified residuei144 – 1441N6-acetyllysineBy similarity
Modified residuei150 – 1501PhosphoserineCombined sources
Modified residuei362 – 3621PhosphothreonineCombined sources
Modified residuei365 – 3651PhosphoserineCombined sources
Modified residuei368 – 3681PhosphoserineCombined sources
Modified residuei385 – 3851CitrullineBy similarity

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Phosphoprotein

Proteomic databases

EPDiQ9NQZ2.
MaxQBiQ9NQZ2.
PaxDbiQ9NQZ2.
PeptideAtlasiQ9NQZ2.
PRIDEiQ9NQZ2.

PTM databases

iPTMnetiQ9NQZ2.
PhosphoSiteiQ9NQZ2.

Expressioni

Gene expression databases

BgeeiQ9NQZ2.
CleanExiHS_UTP3.
GenevisibleiQ9NQZ2. HS.

Organism-specific databases

HPAiHPA035655.
HPA041453.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CDCA7LQ96GN53EBI-714067,EBI-5278764
DVL3Q929973EBI-714067,EBI-739789

Protein-protein interaction databases

BioGridi121342. 29 interactions.
IntActiQ9NQZ2. 10 interactions.
MINTiMINT-1410460.
STRINGi9606.ENSP00000254803.

Structurei

3D structure databases

ProteinModelPortaliQ9NQZ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi72 – 16493Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the SAS10 family.Curated

Phylogenomic databases

eggNOGiKOG3118. Eukaryota.
ENOG410XSPX. LUCA.
GeneTreeiENSGT00500000044947.
HOGENOMiHOG000047611.
HOVERGENiHBG074329.
InParanoidiQ9NQZ2.
KOiK14767.
OMAiVTWVEAF.
OrthoDBiEOG754HQD.
PhylomeDBiQ9NQZ2.
TreeFamiTF315177.

Family and domain databases

InterProiIPR007146. Sas10/Utp3/C1D.
IPR018972. Sas10_C_dom.
[Graphical view]
PfamiPF09368. Sas10. 1 hit.
PF04000. Sas10_Utp3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NQZ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVGRSRRRGA AKWAAVRAKA GPTLTDENGD DLGLPPSPGD TSYYQDQVDD
60 70 80 90 100
FHEARSRAAL AKGWNEVQSG DEEDGEEEEE EVLALDMDDE DDEDGGNAGE
110 120 130 140 150
EEEEENADDD GGSSVQSEAE ASVDPSLSWG QRKKLYYDTD YGSKSRGRQS
160 170 180 190 200
QQEAEEEERE EEEEAQIIQR RLAQALQEDD FGVAWVEAFA KPVPQVDEAE
210 220 230 240 250
TRVVKDLAKV SVKEKLKMLR KESPELLELI EDLKVKLTEV KDELEPLLEL
260 270 280 290 300
VEQGIIPPGK GSQYLRTKYN LYLNYCSNIS FYLILKARRV PAHGHPVIER
310 320 330 340 350
LVTYRNLINK LSVVDQKLSS EIRHLLTLKD DAVKKELIPK AKSTKPKPKS
360 370 380 390 400
VSKTSAAACA VTDLSDDSDF DEKAKLKYYK EIEDRQKLKR KKEENSTEEQ
410 420 430 440 450
ALEDQNAKRA ITYQIAKNRG LTPRRKKIDR NPRVKHREKF RRAKIRRRGQ
460 470
VREVRKEEQR YSGELSGIRA GVKKSIKLK
Length:479
Mass (Da):54,558
Last modified:October 1, 2000 - v1
Checksum:iB4A842785342766D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091D → G in CAG38575 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231T → M.
Corresponds to variant rs16845385 [ dbSNP | Ensembl ].
VAR_051897

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF271212 mRNA. Translation: AAF91408.1.
AL136590 mRNA. Translation: CAB66525.1.
CR533544 mRNA. Translation: CAG38575.1.
AK026909 mRNA. Translation: BAB15588.1.
BC004546 mRNA. Translation: AAH04546.1.
CCDSiCCDS3546.1.
RefSeqiNP_065101.1. NM_020368.2.
UniGeneiHs.322901.

Genome annotation databases

EnsembliENST00000254803; ENSP00000254803; ENSG00000132467.
GeneIDi57050.
KEGGihsa:57050.
UCSCiuc003hfo.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF271212 mRNA. Translation: AAF91408.1.
AL136590 mRNA. Translation: CAB66525.1.
CR533544 mRNA. Translation: CAG38575.1.
AK026909 mRNA. Translation: BAB15588.1.
BC004546 mRNA. Translation: AAH04546.1.
CCDSiCCDS3546.1.
RefSeqiNP_065101.1. NM_020368.2.
UniGeneiHs.322901.

3D structure databases

ProteinModelPortaliQ9NQZ2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121342. 29 interactions.
IntActiQ9NQZ2. 10 interactions.
MINTiMINT-1410460.
STRINGi9606.ENSP00000254803.

PTM databases

iPTMnetiQ9NQZ2.
PhosphoSiteiQ9NQZ2.

Polymorphism and mutation databases

BioMutaiUTP3.
DMDMi76364208.

Proteomic databases

EPDiQ9NQZ2.
MaxQBiQ9NQZ2.
PaxDbiQ9NQZ2.
PeptideAtlasiQ9NQZ2.
PRIDEiQ9NQZ2.

Protocols and materials databases

DNASUi57050.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254803; ENSP00000254803; ENSG00000132467.
GeneIDi57050.
KEGGihsa:57050.
UCSCiuc003hfo.3. human.

Organism-specific databases

CTDi57050.
GeneCardsiUTP3.
HGNCiHGNC:24477. UTP3.
HPAiHPA035655.
HPA041453.
MIMi611614. gene.
neXtProtiNX_Q9NQZ2.
PharmGKBiPA162408779.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3118. Eukaryota.
ENOG410XSPX. LUCA.
GeneTreeiENSGT00500000044947.
HOGENOMiHOG000047611.
HOVERGENiHBG074329.
InParanoidiQ9NQZ2.
KOiK14767.
OMAiVTWVEAF.
OrthoDBiEOG754HQD.
PhylomeDBiQ9NQZ2.
TreeFamiTF315177.

Miscellaneous databases

ChiTaRSiUTP3. human.
GeneWikiiUTP3.
GenomeRNAii57050.
NextBioi62816.
PROiQ9NQZ2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NQZ2.
CleanExiHS_UTP3.
GenevisibleiQ9NQZ2. HS.

Family and domain databases

InterProiIPR007146. Sas10/Utp3/C1D.
IPR018972. Sas10_C_dom.
[Graphical view]
PfamiPF09368. Sas10. 1 hit.
PF04000. Sas10_Utp3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human and mouse homologs of yeast SAS10 disrupter of silencing gene."
    Frye R.A.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: SpleenImported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: AmygdalaImported.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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.
    , 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].
    Tissue: ColonImported.
  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].
    Tissue: LungImported.
  6. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-365 AND SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; THR-362; SER-365 AND SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-37; SER-365 AND SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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; SER-365 AND SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSAS10_HUMAN
AccessioniPrimary (citable) accession number: Q9NQZ2
Secondary accession number(s): Q6FI82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 1, 2000
Last modified: April 13, 2016
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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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. SIMILARITY comments
    Index of protein domains and families

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.