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Q15020

- SART3_HUMAN

UniProt

Q15020 - SART3_HUMAN

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Protein

Squamous cell carcinoma antigen recognized by T-cells 3

Gene

SART3

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

Functioni

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

  1. nucleotide binding Source: InterPro
  2. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. cell morphogenesis Source: Ensembl
  2. hematopoietic stem cell proliferation Source: Ensembl
  3. homeostasis of number of cells Source: Ensembl
  4. regulation of gene expression Source: MGI
  5. RNA processing Source: InterPro
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Squamous cell carcinoma antigen recognized by T-cells 3
Short name:
SART-3
Short name:
hSART-3
Alternative name(s):
Tat-interacting protein of 110 kDa
Short name:
Tip110
Gene namesi
Name:SART3
Synonyms:KIAA0156, TIP110
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:16860. SART3.

Subcellular locationi

Cytoplasm. Nucleus speckle
Note: Localized in speckles. Expressed in the nucleus of all of the malignant tumor cell lines tested and the majority of cancer tissues with various histologies, including squamous cell carcinomas (SCC), adenocarcinomas, melanomas and leukemias cells. However, this protein is undetectable in the nucleus of any cell lines of nonmalignant cells or normal tissues, except for the testis. Expressed in the cytoplasm of all the proliferating cells, including normal and malignant cells, but not in normal tissues, except for the testis and the fetal liver.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Disseminated superficial actinic porokeratosis 1 (DSAP1) [MIM:175900]: Autosomal 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.

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.
GenevestigatoriQ15020.

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. Interacts with HIV-1 Tat. Interacts with AGO1 and AGO2.3 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi115082. 80 interactions.
IntActiQ15020. 32 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, 701-877.
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
Regioni600 – 67071Required for nuclear localizationAdd
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.
GeneTreeiENSGT00730000111098.
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 (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

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.

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF387506 mRNA. Translation: AAK69347.1.
AB020880 mRNA. Translation: BAA78384.1.
D63879 mRNA. Translation: BAA09929.1.
AK290209 mRNA. Translation: BAF82898.1.
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.
CCDSiCCDS9117.1. [Q15020-1]
RefSeqiNP_055521.1. NM_014706.3. [Q15020-1]
UniGeneiHs.584842.

Genome annotation databases

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

Polymorphism databases

DMDMi74762140.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF387506 mRNA. Translation: AAK69347.1 .
AB020880 mRNA. Translation: BAA78384.1 .
D63879 mRNA. Translation: BAA09929.1 .
AK290209 mRNA. Translation: BAF82898.1 .
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 .
CCDSi CCDS9117.1. [Q15020-1 ]
RefSeqi NP_055521.1. NM_014706.3. [Q15020-1 ]
UniGenei Hs.584842.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DO4 NMR - A 791-877 [» ]
ProteinModelPortali Q15020.
SMRi Q15020. Positions 102-360, 701-877.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115082. 80 interactions.
IntActi Q15020. 32 interactions.
MINTi MINT-2867335.
STRINGi 9606.ENSP00000228284.

PTM databases

PhosphoSitei Q15020.

Polymorphism databases

DMDMi 74762140.

Proteomic databases

MaxQBi Q15020.
PaxDbi Q15020.
PeptideAtlasi Q15020.
PRIDEi Q15020.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000228284 ; ENSP00000228284 ; ENSG00000075856 . [Q15020-1 ]
ENST00000546611 ; ENSP00000448554 ; ENSG00000075856 . [Q15020-3 ]
ENST00000546728 ; ENSP00000449743 ; ENSG00000075856 . [Q15020-2 ]
GeneIDi 9733.
KEGGi hsa:9733.
UCSCi uc001tmy.1. human. [Q15020-1 ]
uc001tnb.3. human. [Q15020-3 ]

Organism-specific databases

CTDi 9733.
GeneCardsi GC12M108915.
HGNCi HGNC:16860. SART3.
HPAi HPA044322.
MIMi 175900. phenotype.
611684. gene.
neXtProti NX_Q15020.
PharmGKBi PA34948.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG321927.
GeneTreei ENSGT00730000111098.
HOGENOMi HOG000063708.
HOVERGENi HBG053888.
InParanoidi Q15020.
OMAi MERTEGS.
OrthoDBi EOG72ZCDB.
PhylomeDBi Q15020.
TreeFami TF317554.

Miscellaneous databases

ChiTaRSi SART3. human.
EvolutionaryTracei Q15020.
GeneWikii SART3.
GenomeRNAii 9733.
NextBioi 36616.
PROi Q15020.
SOURCEi Search...

Gene expression databases

Bgeei Q15020.
CleanExi HS_SART3.
ExpressionAtlasi Q15020. baseline and differential.
Genevestigatori Q15020.

Family and domain databases

Gene3Di 3.30.70.330. 2 hits.
InterProi IPR003107. HAT.
IPR008669. LSM_interact.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF05391. Lsm_interact. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view ]
SMARTi SM00386. HAT. 7 hits.
SM00360. RRM. 2 hits.
[Graphical view ]
PROSITEi PS50102. RRM. 2 hits.
[Graphical view ]
ProtoNeti Search...

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.
    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 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, Eye, Skin and Uterus.
  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-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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.
  8. 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.
  9. "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.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. "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].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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].
  16. "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].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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.
  19. "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
, Q2M2H0, Q58F06, Q8IUS1, Q96J95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 131 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