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Protein

Squamous cell carcinoma antigen recognized by T-cells 3

Gene

SART3

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

Functioni

U6 snRNP-binding protein that functions as a recycling factor of the splicing machinery. Promotes the initial reassembly of U4 and U6 snRNPs following their ejection from the spliceosome during its maturation (PubMed:12032085). Also binds U6atac snRNPs and may function as a recycling factor for U4atac/U6atac spliceosomal snRNP, an initial step in the assembly of U12-type spliceosomal complex. The U12-type spliceosomal complex plays a role in the splicing of introns with non-canonical splice sites (PubMed:14749385). May also function as a substrate-targeting factor for deubiquitinases like USP4 and USP15. Recruits USP4 to ubiquitinated PRPF3 within the U4/U5/U6 tri-snRNP complex, promoting PRPF3 deubiquitination and thereby regulating the spliceosome U4/U5/U6 tri-snRNP spliceosomal complex disassembly (PubMed:20595234). May also recruit the deubiquitinase USP15 to histone H2B and mediate histone deubiquitination, thereby regulating gene expression and/or DNA repair (PubMed:24526689). May play a role in hematopoiesis probably through transcription regulation of specific genes including MYC (By similarity).By similarity4 Publications
Regulates Tat transactivation activity through direct interaction. May be a cellular factor for HIV-1 gene expression and viral replication.1 Publication

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • U4 snRNA binding Source: UniProtKB
  • U6atac snRNA binding Source: UniProtKB
  • U6 snRNA binding Source: UniProtKB
  • ubiquitin-specific protease binding Source: UniProtKB

GO - Biological processi

  • cell morphogenesis Source: Ensembl
  • hematopoietic stem cell proliferation Source: Ensembl
  • homeostasis of number of cells Source: Ensembl
  • mRNA splicing, via spliceosome Source: UniProtKB
  • nucleosome assembly Source: UniProtKB
  • positive regulation of histone deubiquitination Source: UniProtKB
  • regulation of gene expression Source: MGI
  • spliceosomal snRNP assembly Source: UniProtKB
  • spliceosomal tri-snRNP complex assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Squamous cell carcinoma antigen recognized by T-cells 3Curated
Short name:
SART-3Imported
Alternative name(s):
Tat-interacting protein of 110 kDa1 Publication
Short name:
Tip1101 Publication
p110 nuclear RNA-binding protein1 Publication
Gene namesi
Name:SART3Imported
Synonyms:KIAA0156Imported, TIP1101 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:16860. SART3.

Subcellular locationi

GO - Cellular componenti

  • Cajal body Source: UniProtKB
  • cytoplasm Source: UniProtKB-SubCell
  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Disseminated superficial actinic porokeratosis 1 (DSAP1)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAutosomal dominant disorder, characterized by multiple superficial keratotic lesions surrounded by a slightly raised keratotic border, developing during the third or fourth decade of life on sun-exposed areas of skin.

See also OMIM:175900
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti591 – 5911V → M in DSAP1. 1 Publication
VAR_038683

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi175900. phenotype.
PharmGKBiPA34948.

Polymorphism and mutation databases

BioMutaiSART3.
DMDMi74762140.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed7 Publications
Chaini2 – 963962Squamous cell carcinoma antigen recognized by T-cells 3PRO_0000223313Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine7 Publications
Modified residuei10 – 101Phosphoserine1 Publication
Modified residuei16 – 161Phosphoserine1 Publication
Modified residuei852 – 8521Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15020.
PaxDbiQ15020.
PeptideAtlasiQ15020.
PRIDEiQ15020.

PTM databases

PhosphoSiteiQ15020.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ15020.
CleanExiHS_SART3.
ExpressionAtlasiQ15020. baseline and differential.
GenevisibleiQ15020. HS.

Organism-specific databases

HPAiHPA044322.

Interactioni

Subunit structurei

Component of the 7SK snRNP complex at least composed of P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, BCDIN3, SART3 proteins and 7SK and U6 snRNAs (PubMed:17643375). Interacts with AGO1 and AGO2 (PubMed:17932509). Interacts with PRPF3 and USP4; the interaction with PRPF3 is direct and recruits USP4 to its substrate PRPF3 (PubMed:15314151, PubMed:20595234). Interacts with USP15; the interaction is direct (PubMed:24526689). Interacts with HIV-1 Tat (PubMed:11959860).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RNPS1Q152875EBI-308619,EBI-395959

Protein-protein interaction databases

BioGridi115082. 82 interactions.
IntActiQ15020. 33 interactions.
MINTiMINT-2867335.
STRINGi9606.ENSP00000228284.

Structurei

Secondary structure

1
963
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi803 – 8075Combined sources
Helixi814 – 8218Combined sources
Turni822 – 8243Combined sources
Beta strandi827 – 8348Combined sources
Beta strandi840 – 85011Combined sources
Helixi851 – 86111Combined sources
Beta strandi864 – 8685Combined sources
Beta strandi870 – 8756Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DO4NMR-A791-877[»]
ProteinModelPortaliQ15020.
SMRiQ15020. Positions 102-360, 702-877.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15020.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati126 – 15833HAT 1Add
BLAST
Repeati164 – 19532HAT 2Add
BLAST
Repeati201 – 23737HAT 3Add
BLAST
Repeati242 – 27534HAT 4Add
BLAST
Repeati324 – 35633HAT 5Add
BLAST
Repeati359 – 39133HAT 6Add
BLAST
Repeati394 – 43037HAT 7Add
BLAST
Repeati487 – 52034HAT 8Add
BLAST
Domaini704 – 78279RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini801 – 87878RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 351350Mediates interaction with PRPF31 PublicationAdd
BLAST
Regioni487 – 52034Required for interaction with USP41 PublicationAdd
BLAST
Regioni537 – 953417Necessary and sufficient for U6 snRNA binding1 PublicationAdd
BLAST
Regioni600 – 67071Required for nuclear localization1 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili21 – 4626Sequence AnalysisAdd
BLAST
Coiled coili82 – 11029Sequence AnalysisAdd
BLAST
Coiled coili559 – 61961Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi601 – 61717Nuclear localization signalSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi89 – 924Poly-Glu
Compositional biasi612 – 6165Poly-Lys

Sequence similaritiesi

Contains 8 HAT repeats.Curated
Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG321927.
GeneTreeiENSGT00790000123030.
HOGENOMiHOG000063708.
HOVERGENiHBG053888.
InParanoidiQ15020.
OMAiMERTEGS.
OrthoDBiEOG72ZCDB.
PhylomeDBiQ15020.
TreeFamiTF317554.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR003107. HAT.
IPR008669. LSM_interact.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF05391. Lsm_interact. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00386. HAT. 7 hits.
SM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15020-1) [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
MATAAETSAS EPEAESKAGP KADGEEDEVK AARTRRKVLS RAVAAATYKT
60 70 80 90 100
MGPAWDQQEE GVSESDGDEY AMASSAESSP GEYEWEYDEE EEKNQLEIER
110 120 130 140 150
LEEQLSINVY DYNCHVDLIR LLRLEGELTK VRMARQKMSE IFPLTEELWL
160 170 180 190 200
EWLHDEISMA QDGLDREHVY DLFEKAVKDY ICPNIWLEYG QYSVGGIGQK
210 220 230 240 250
GGLEKVRSVF ERALSSVGLH MTKGLALWEA YREFESAIVE AARLEKVHSL
260 270 280 290 300
FRRQLAIPLY DMEATFAEYE EWSEDPIPES VIQNYNKALQ QLEKYKPYEE
310 320 330 340 350
ALLQAEAPRL AEYQAYIDFE MKIGDPARIQ LIFERALVEN CLVPDLWIRY
360 370 380 390 400
SQYLDRQLKV KDLVLSVHNR AIRNCPWTVA LWSRYLLAME RHGVDHQVIS
410 420 430 440 450
VTFEKALNAG FIQATDYVEI WQAYLDYLRR RVDFKQDSSK ELEELRAAFT
460 470 480 490 500
RALEYLKQEV EERFNESGDP SCVIMQNWAR IEARLCNNMQ KARELWDSIM
510 520 530 540 550
TRGNAKYANM WLEYYNLERA HGDTQHCRKA LHRAVQCTSD YPEHVCEVLL
560 570 580 590 600
TMERTEGSLE DWDIAVQKTE TRLARVNEQR MKAAEKEAAL VQQEEEKAEQ
610 620 630 640 650
RKRARAEKKA LKKKKKIRGP EKRGADEDDE KEWGDDEEEQ PSKRRRVENS
660 670 680 690 700
IPAAGETQNV EVAAGPAGKC AAVDVEPPSK QKEKAASLKR DMPKVLHDSS
710 720 730 740 750
KDSITVFVSN LPYSMQEPDT KLRPLFEACG EVVQIRPIFS NRGDFRGYCY
760 770 780 790 800
VEFKEEKSAL QALEMDRKSV EGRPMFVSPC VDKSKNPDFK VFRYSTSLEK
810 820 830 840 850
HKLFISGLPF SCTKEELEEI CKAHGTVKDL RLVTNRAGKP KGLAYVEYEN
860 870 880 890 900
ESQASQAVMK MDGMTIKENI IKVAISNPPQ RKVPEKPETR KAPGGPMLLP
910 920 930 940 950
QTYGARGKGR TQLSLLPRAL QRPSAAAPQA ENGPAAAPAV AAPAATEAPK
960
MSNADFAKLF LRK
Length:963
Mass (Da):109,935
Last modified:November 1, 1996 - v1
Checksum:i06B26CEB8B19102A
GO
Isoform 2 (identifier: Q15020-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     351-364: SQYLDRQLKVKDLV → RSTTESKGFGFICT
     365-963: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Inactive in U4/U6 snRNP recycling.1 Publication
Show »
Length:364
Mass (Da):41,829
Checksum:iD86B2562A7FA2E4E
GO
Isoform 3 (identifier: Q15020-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     105-129: LSINVYDYNCHVDLIRLLRLEGELT → VGPGVGSGHLPVFQVLGSPCPGPPP
     130-963: Missing.

Note: No experimental confirmation available.
Show »
Length:129
Mass (Da):13,773
Checksum:iB41FC49C1C5E4C33
GO
Isoform 4 (identifier: Q15020-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     401-436: Missing.

Note: No experimental confirmation available.
Show »
Length:927
Mass (Da):105,584
Checksum:iA4D08EF2F14CFC93
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231D → E.1 Publication
Corresponds to variant rs2072579 [ dbSNP | Ensembl ].
VAR_038802
Natural varianti591 – 5911V → M in DSAP1. 1 Publication
VAR_038683
Natural varianti621 – 6211E → D.
Corresponds to variant rs2287546 [ dbSNP | Ensembl ].
VAR_038684

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei105 – 12925LSINV…EGELT → VGPGVGSGHLPVFQVLGSPC PGPPP in isoform 3. 1 PublicationVSP_017248Add
BLAST
Alternative sequencei130 – 963834Missing in isoform 3. 1 PublicationVSP_017249Add
BLAST
Alternative sequencei351 – 36414SQYLD…VKDLV → RSTTESKGFGFICT in isoform 2. 1 PublicationVSP_017250Add
BLAST
Alternative sequencei365 – 963599Missing in isoform 2. 1 PublicationVSP_017251Add
BLAST
Alternative sequencei401 – 43636Missing in isoform 4. 1 PublicationVSP_057284Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020880 mRNA. Translation: BAA78384.1.
AF387506 mRNA. Translation: AAK69347.1.
D63879 mRNA. Translation: BAA09929.1.
AK290209 mRNA. Translation: BAF82898.1.
AC008119 Genomic DNA. No translation available.
AC010206 Genomic DNA. No translation available.
KF455716 Genomic DNA. No translation available.
KF511170 Genomic DNA. No translation available.
BC032601 mRNA. Translation: AAH32601.1.
BC041638 mRNA. Translation: AAH41638.1.
BC093784 mRNA. Translation: AAH93784.1.
BC103706 mRNA. Translation: AAI03707.1.
BC111983 mRNA. Translation: AAI11984.1.
BC143253 mRNA. Translation: AAI43254.1.
CCDSiCCDS9117.1. [Q15020-1]
RefSeqiNP_055521.1. NM_014706.3. [Q15020-1]
UniGeneiHs.584842.

Genome annotation databases

EnsembliENST00000228284; ENSP00000228284; ENSG00000075856. [Q15020-1]
ENST00000431469; ENSP00000414453; ENSG00000075856. [Q15020-4]
ENST00000546611; ENSP00000448554; ENSG00000075856. [Q15020-3]
ENST00000546728; ENSP00000449743; ENSG00000075856. [Q15020-2]
GeneIDi9733.
KEGGihsa:9733.
UCSCiuc001tmy.1. human. [Q15020-1]
uc001tnb.3. human. [Q15020-3]
uc010swx.1. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020880 mRNA. Translation: BAA78384.1.
AF387506 mRNA. Translation: AAK69347.1.
D63879 mRNA. Translation: BAA09929.1.
AK290209 mRNA. Translation: BAF82898.1.
AC008119 Genomic DNA. No translation available.
AC010206 Genomic DNA. No translation available.
KF455716 Genomic DNA. No translation available.
KF511170 Genomic DNA. No translation available.
BC032601 mRNA. Translation: AAH32601.1.
BC041638 mRNA. Translation: AAH41638.1.
BC093784 mRNA. Translation: AAH93784.1.
BC103706 mRNA. Translation: AAI03707.1.
BC111983 mRNA. Translation: AAI11984.1.
BC143253 mRNA. Translation: AAI43254.1.
CCDSiCCDS9117.1. [Q15020-1]
RefSeqiNP_055521.1. NM_014706.3. [Q15020-1]
UniGeneiHs.584842.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DO4NMR-A791-877[»]
ProteinModelPortaliQ15020.
SMRiQ15020. Positions 102-360, 702-877.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115082. 82 interactions.
IntActiQ15020. 33 interactions.
MINTiMINT-2867335.
STRINGi9606.ENSP00000228284.

PTM databases

PhosphoSiteiQ15020.

Polymorphism and mutation databases

BioMutaiSART3.
DMDMi74762140.

Proteomic databases

MaxQBiQ15020.
PaxDbiQ15020.
PeptideAtlasiQ15020.
PRIDEiQ15020.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000228284; ENSP00000228284; ENSG00000075856. [Q15020-1]
ENST00000431469; ENSP00000414453; ENSG00000075856. [Q15020-4]
ENST00000546611; ENSP00000448554; ENSG00000075856. [Q15020-3]
ENST00000546728; ENSP00000449743; ENSG00000075856. [Q15020-2]
GeneIDi9733.
KEGGihsa:9733.
UCSCiuc001tmy.1. human. [Q15020-1]
uc001tnb.3. human. [Q15020-3]
uc010swx.1. human.

Organism-specific databases

CTDi9733.
GeneCardsiGC12M108915.
HGNCiHGNC:16860. SART3.
HPAiHPA044322.
MIMi175900. phenotype.
611684. gene.
neXtProtiNX_Q15020.
PharmGKBiPA34948.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG321927.
GeneTreeiENSGT00790000123030.
HOGENOMiHOG000063708.
HOVERGENiHBG053888.
InParanoidiQ15020.
OMAiMERTEGS.
OrthoDBiEOG72ZCDB.
PhylomeDBiQ15020.
TreeFamiTF317554.

Miscellaneous databases

ChiTaRSiSART3. human.
EvolutionaryTraceiQ15020.
GeneWikiiSART3.
GenomeRNAii9733.
NextBioi35481156.
PROiQ15020.
SOURCEiSearch...

Gene expression databases

BgeeiQ15020.
CleanExiHS_SART3.
ExpressionAtlasiQ15020. baseline and differential.
GenevisibleiQ15020. HS.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR003107. HAT.
IPR008669. LSM_interact.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF05391. Lsm_interact. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00386. HAT. 7 hits.
SM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a gene coding for a protein possessing shared tumor epitopes capable of inducing HLA-A24-restricted cytotoxic T lymphocytes in cancer patients."
    Yang D., Nakao M., Shichijo S., Sasatomi T., Takasu H., Matsumoto H., Mori K., Hayashi A., Yamana H., Shirouzu K., Itoh K.
    Cancer Res. 59:4056-4063(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
  2. "HIV-1 Tat protein-mediated transactivation of the HIV-1 long terminal repeat promoter is potentiated by a novel nuclear Tat-interacting protein of 110 kDa, Tip110."
    Liu Y., Li J., Kim B.O., Pace B.S., He J.J.
    J. Biol. Chem. 277:23854-23863(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH TAT, REGION.
    Tissue: Fetal brain.
  3. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
    DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  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] (ISOFORM 1), VARIANT GLU-23.
    Tissue: Thalamus.
  5. "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].
  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; 3 AND 4).
    Tissue: Brain, Eye, Skin and Uterus.
  7. "p110, a novel human U6 snRNP protein and U4/U6 snRNP recycling factor."
    Bell M., Schreiner S., Damianov A., Reddy R., Bindereif A.
    EMBO J. 21:2724-2735(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Targeting of U4/U6 small nuclear RNP assembly factor SART3/p110 to Cajal bodies."
    Stanek D., Rader S.D., Klingauf M., Neugebauer K.M.
    J. Cell Biol. 160:505-516(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Recycling of the U12-type spliceosome requires p110, a component of the U6atac snRNP."
    Damianov A., Schreiner S., Bindereif A.
    Mol. Cell. Biol. 24:1700-1708(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Human U4/U6 snRNP recycling factor p110: mutational analysis reveals the function of the tetratricopeptide repeat domain in recycling."
    Medenbach J., Schreiner S., Liu S., Luhrmann R., Bindereif A.
    Mol. Cell. Biol. 24:7392-7401(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 2), INTERACTION WITH PRPF3, REGION.
  11. "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-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
    Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
    EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AGO1 AND AGO2.
  13. Bienvenut W.V., Dhillon A.S., Kolch W.
    Submitted (FEB-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-17; 121-130; 233-243; 295-322; 329-335; 350-356; 360-370; 452-463; 494-502; 555-568; 646-669; 758-768 AND 911-918, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hepatoma.
  14. "Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme."
    Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C., Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B., Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B.
    Mol. Cell 27:262-274(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE 7SK SNRNP COMPLEX.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  18. "The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control reversible ubiquitination at the spliceosome."
    Song E.J., Werner S.L., Neubauer J., Stegmeier F., Aspden J., Rio D., Harper J.W., Elledge S.J., Kirschner M.W., Rape M.
    Genes Dev. 24:1434-1447(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRPF3 AND USP4, REGION.
  19. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  22. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  23. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  24. "The U4/U6 recycling factor SART3 has histone chaperone activity and associates with USP15 to regulate H2B deubiquitination."
    Long L., Thelen J.P., Furgason M., Haj-Yahya M., Brik A., Cheng D., Peng J., Yao T.
    J. Biol. Chem. 289:8916-8930(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH USP15.
  25. "Solution structure of the RNA binding domain of squamous cell carcinoma antigen recognized by T cells 3."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 791-877.
  26. "A mutation in SART3 gene in a Chinese pedigree with disseminated superficial actinic porokeratosis."
    Zhang Z.H., Niu Z.M., Yuan W.T., Zhao J.J., Jiang F.X., Zhang J., Chai B., Cui F., Chen W., Lian C.H., Xiang L.H., Xu S.J., Liu W.D., Zheng Z.Z., Huang W.
    Br. J. Dermatol. 152:658-663(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DSAP1 MET-591.

Entry informationi

Entry nameiSART3_HUMAN
AccessioniPrimary (citable) accession number: Q15020
Secondary accession number(s): A8K2E4
, B7ZKM0, Q2M2H0, Q58F06, Q8IUS1, Q96J95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 137 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

3D-structure, Complete proteome, Direct protein sequencing, 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
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.