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Protein

Tuftelin-interacting protein 11

Gene

TFIP11

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

Functioni

Involved in pre-mRNA splicing, specifically in spliceosome disassembly during late-stage splicing events. Intron turnover seems to proceed through reactions in two lariat-intron associated complexes termed Intron Large (IL) and Intron Small (IS). In cooperation with DHX15 seems to mediate the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns. May play a role in the differentiation of ameloblasts and odontoblasts or in the forming of the enamel extracellular matrix.1 Publication

GO - Molecular functioni

GO - Biological processi

  • biomineral tissue development Source: UniProtKB-KW
  • mRNA splicing, via spliceosome Source: UniProtKB
  • negative regulation of DNA ligase activity Source: BHF-UCL
  • negative regulation of double-strand break repair via nonhomologous end joining Source: BHF-UCL
  • negative regulation of protein binding Source: BHF-UCL
  • negative regulation of protein complex assembly Source: BHF-UCL
  • protection from non-homologous end joining at telomere Source: BHF-UCL
  • regulation of transcription, DNA-templated Source: InterPro
  • RNA processing Source: UniProtKB
  • spliceosomal complex disassembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Biomineralization, mRNA processing, mRNA splicing

Names & Taxonomyi

Protein namesi
Recommended name:
Tuftelin-interacting protein 11
Alternative name(s):
Septin and tuftelin-interacting protein 1
Short name:
STIP-1
Gene namesi
Name:TFIP11
Synonyms:STIP
ORF Names:HSPC006
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:17165. TFIP11.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: In the nucleus localizes to unique speckle domains in close proximity to nuclear speckles and not identical to paraspeckles.By similarity

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • cytoplasm Source: UniProtKB-SubCell
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear speck Source: LIFEdb
  • nucleolus Source: BHF-UCL
  • proteinaceous extracellular matrix Source: Ensembl
  • spliceosomal complex Source: UniProtKB
  • U2-type post-mRNA release spliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38441.

Polymorphism and mutation databases

BioMutaiTFIP11.
DMDMi22096235.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 837837Tuftelin-interacting protein 11PRO_0000072501Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei59 – 591PhosphoserineCombined sources
Modified residuei98 – 981PhosphoserineCombined sources
Modified residuei144 – 1441PhosphoserineCombined sources
Modified residuei210 – 2101PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UBB9.
MaxQBiQ9UBB9.
PaxDbiQ9UBB9.
PeptideAtlasiQ9UBB9.
PRIDEiQ9UBB9.

PTM databases

iPTMnetiQ9UBB9.
PhosphoSiteiQ9UBB9.

Expressioni

Gene expression databases

BgeeiQ9UBB9.
CleanExiHS_TFIP11.
ExpressionAtlasiQ9UBB9. baseline and differential.
GenevisibleiQ9UBB9. HS.

Organism-specific databases

HPAiHPA027085.

Interactioni

Subunit structurei

Identified in the spliceosome C complex. Found in the Intron Large (IL) complex, a post-mRNA release spliceosomal complex containing the excised intron, U2, U5 and U6 snRNPs, and splicing factors. Interacts with TUFT1. Interacts with DHX15; indicative for a recruitment of DHX15 to the IL complex. Interacts with GCFC2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI2Q9NYB93EBI-1105213,EBI-743598
ADCK3Q8NI605EBI-1105213,EBI-745535
AIMP2Q131553EBI-1105213,EBI-745226
ALS2CR11Q53TS83EBI-1105213,EBI-739879
ARMCX1Q9P2913EBI-1105213,EBI-2843626
ATP5OP480473EBI-1105213,EBI-355815
BMFQ96LC93EBI-1105213,EBI-3919268
C1orf109Q9NX043EBI-1105213,EBI-8643161
C6orf165Q8IYR03EBI-1105213,EBI-749051
CARD9Q9H2573EBI-1105213,EBI-751319
CCDC116Q8IYX33EBI-1105213,EBI-744311
CCDC121Q6ZUS53EBI-1105213,EBI-2836982
CCDC146Q8IYE0-23EBI-1105213,EBI-10247802
CCDC151A5D8V73EBI-1105213,EBI-8466445
CCDC151A5D8V7-23EBI-1105213,EBI-10173824
CCDC42Q96M953EBI-1105213,EBI-747041
CCDC68Q9H2F93EBI-1105213,EBI-2813327
CCHCR1Q8TD31-33EBI-1105213,EBI-10175300
CCND3P302813EBI-1105213,EBI-375013
CCNG1P519593EBI-1105213,EBI-3905829
CCNL1Q9UK583EBI-1105213,EBI-2836773
CENPUQ71F233EBI-1105213,EBI-2515234
CEP57Q86XR83EBI-1105213,EBI-308614
CEP57L1Q8IYX83EBI-1105213,EBI-1104570
COX5BP106063EBI-1105213,EBI-1053725
EIF3AQ24JU43EBI-1105213,EBI-10239221
FAM13CQ8NE313EBI-1105213,EBI-751248
FAM156AQ8NDB63EBI-1105213,EBI-749727
FAM161AQ3B8203EBI-1105213,EBI-719941
FAM50BQ9Y2473EBI-1105213,EBI-742802
GCC1Q96CN93EBI-1105213,EBI-746252
GEMP550403EBI-1105213,EBI-744104
GNG4B1APZ03EBI-1105213,EBI-10175453
GOLGA1Q928053EBI-1105213,EBI-6164177
GPS2Q132273EBI-1105213,EBI-713355
HAUS1Q96CS23EBI-1105213,EBI-2514791
HMG20BQ9P0W23EBI-1105213,EBI-713401
HOOK1Q9UJC33EBI-1105213,EBI-746704
IKBIPQ70UQ03EBI-1105213,EBI-2557212
IMP3Q9NV313EBI-1105213,EBI-747481
KANSL1I3L4J33EBI-1105213,EBI-10178305
KRT20P359004EBI-1105213,EBI-742094
KRT6AP025384EBI-1105213,EBI-702198
KRT6BP042593EBI-1105213,EBI-740907
KRT6CP486683EBI-1105213,EBI-2564105
KRT8P057873EBI-1105213,EBI-297852
LATS1Q6PJG33EBI-1105213,EBI-10253976
LCA5LO954473EBI-1105213,EBI-8473670
LENG1Q96BZ83EBI-1105213,EBI-726510
LIN37Q96GY33EBI-1105213,EBI-748884
LMO1P258003EBI-1105213,EBI-8639312
LMO4P619683EBI-1105213,EBI-2798728
LOC729862Q0VAF83EBI-1105213,EBI-10226726
LOC729862Q0VAF93EBI-1105213,EBI-10226748
METTL17Q9H7H04EBI-1105213,EBI-749353
MTFR2Q6P4443EBI-1105213,EBI-10252703
NDC80O147773EBI-1105213,EBI-715849
NFU1Q9UMS03EBI-1105213,EBI-725252
OIP5O434823EBI-1105213,EBI-536879
PBX4Q9BYU13EBI-1105213,EBI-10302990
PDE4DIPQ8TBR03EBI-1105213,EBI-10240575
POLLQ9UGP5-23EBI-1105213,EBI-10320765
PPP1R18Q6NYC83EBI-1105213,EBI-2557469
PRPF31F1T0A53EBI-1105213,EBI-10177194
RCOR3Q9P2K33EBI-1105213,EBI-743428
RHNO1Q9BSD33EBI-1105213,EBI-9658624
RRP7AQ9Y3A43EBI-1105213,EBI-7223720
S100PP258153EBI-1105213,EBI-743700
SAP30BPQ9UHR53EBI-1105213,EBI-751683
SFR1Q86XK33EBI-1105213,EBI-1104535
SH2D4AQ9H7883EBI-1105213,EBI-747035
SH2D4AQ9H788-23EBI-1105213,EBI-10308083
SH3GLB1Q9Y3713EBI-1105213,EBI-2623095
SMARCE1Q969G33EBI-1105213,EBI-455078
SNRPBP14678-23EBI-1105213,EBI-372475
SNW1Q135733EBI-1105213,EBI-632715
SNX20Q7Z6143EBI-1105213,EBI-744896
SSX2IPQ9Y2D83EBI-1105213,EBI-2212028
STRNO438153EBI-1105213,EBI-1046642
TCAF1Q9Y4C23EBI-1105213,EBI-750484
TFPTG5E9B53EBI-1105213,EBI-10178002
THAP7Q9BT493EBI-1105213,EBI-741350
THAP8Q8NA923EBI-1105213,EBI-717429
TNNT1P138053EBI-1105213,EBI-726527
TRAF3IP3Q9Y2283EBI-1105213,EBI-765817
TSHZ3A1L0U73EBI-1105213,EBI-10171826
TSPYL4Q9UJ043EBI-1105213,EBI-308511
TXLNAP402223EBI-1105213,EBI-359793
VPS37CA5D8V63EBI-1105213,EBI-2559305
ZC2HC1CQ53FD03EBI-1105213,EBI-740767
ZFYVE26Q96H433EBI-1105213,EBI-10286915
ZGPATQ8N5A53EBI-1105213,EBI-3439227
ZGPATQ8N5A5-23EBI-1105213,EBI-10183064
ZMAT2Q96NC03EBI-1105213,EBI-2682299
ZNF417Q8TAU34EBI-1105213,EBI-740727
ZSCAN12O433093EBI-1105213,EBI-1210440

Protein-protein interaction databases

BioGridi117294. 143 interactions.
IntActiQ9UBB9. 117 interactions.
MINTiMINT-3078852.
STRINGi9606.ENSP00000383892.

Structurei

3D structure databases

ProteinModelPortaliQ9UBB9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini149 – 19547G-patchPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 5050Required for interaction with DHX15Add
BLAST
Regioni710 – 73425Required for nuclear speckle localizationBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi700 – 7056Nuclear localization signalBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi15 – 195Poly-Asp

Sequence similaritiesi

Belongs to the TFP11/STIP family.Curated
Contains 1 G-patch domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2184. Eukaryota.
ENOG410XP4Y. LUCA.
GeneTreeiENSGT00390000012739.
HOGENOMiHOG000230470.
HOVERGENiHBG055868.
InParanoidiQ9UBB9.
KOiK13103.
OMAiDECARVF.
OrthoDBiEOG79KPDZ.
PhylomeDBiQ9UBB9.
TreeFamiTF314887.

Family and domain databases

InterProiIPR000467. G_patch_dom.
IPR022783. GCFC_dom.
IPR024933. STIP.
IPR022159. STIP/TFIP11_N.
[Graphical view]
PfamiPF01585. G-patch. 1 hit.
PF07842. GCFC. 1 hit.
PF12457. TIP_N. 1 hit.
[Graphical view]
PIRSFiPIRSF017706. TFIP11. 1 hit.
SMARTiSM00443. G_patch. 1 hit.
[Graphical view]
PROSITEiPS50174. G_PATCH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UBB9-1) [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
MSLSHLYRDG EGRIDDDDDE RENFEITDWD LQNEFNPNRQ RHWQTKEEAT
60 70 80 90 100
YGVWAERDSD DERPSFGGKR ARDYSAPVNF ISAGLKKGAA EEAELEDSDD
110 120 130 140 150
EEKPVKQDDF PKDFGPRKLK TGGNFKPSQK GFAGGTKSFM DFGSWERHTK
160 170 180 190 200
GIGQKLLQKM GYVPGRGLGK NAQGIINPIE AKQRKGKGAV GAYGSERTTQ
210 220 230 240 250
SMQDFPVVDS EEEAEEEFQK ELSQWRKDPS GSKKKPKYSY KTVEELKAKG
260 270 280 290 300
RISKKLTAPQ KELSQVKVID MTGREQKVYY SYSQISHKHN VPDDGLPLQS
310 320 330 340 350
QQLPQSGKEA KAPGFALPEL EHNLQLLIDL TEQEIIQNDR QLQYERDMVV
360 370 380 390 400
NLFHELEKMT EVLDHEERVI SNLSKVLEMV EECERRMQPD CSNPLTLDEC
410 420 430 440 450
ARIFETLQDK YYEEYRMSDR VDLAVAIVYP LMKEYFKEWD PLKDCTYGTE
460 470 480 490 500
IISKWKSLLE NDQLLSHGGQ DLSADAFHRL IWEVWMPFVR NIVTQWQPRN
510 520 530 540 550
CDPMVDFLDS WVHIIPVWIL DNILDQLIFP KLQKEVENWN PLTDTVPIHS
560 570 580 590 600
WIHPWLPLMQ ARLEPLYSPI RSKLSSALQK WHPSDSSAKL ILQPWKDVFT
610 620 630 640 650
PGSWEAFMVK NIVPKLGMCL GELVINPHQQ HMDAFYWVID WEGMISVSSL
660 670 680 690 700
VGLLEKHFFP KWLQVLCSWL SNSPNYEEIT KWYLGWKSMF SDQVLAHPSV
710 720 730 740 750
KDKFNEALDI MNRAVSSNVG AYMQPGAREN IAYLTHTERR KDFQYEAMQE
760 770 780 790 800
RREAENMAQR GIGVAASSVP MNFKDLIETK AEEHNIVFMP VIGKRHEGKQ
810 820 830
LYTFGRIVIY IDRGVVFVQG EKTWVPTSLQ SLIDMAK
Length:837
Mass (Da):96,820
Last modified:May 1, 2000 - v1
Checksum:iF4C44F8411517289
GO
Isoform 2 (identifier: Q9UBB9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-641: Missing.
     642-663: EGMISVSSLVGLLEKHFFPKWL → MATSEILPSFVATMDASNFSFW

Note: No experimental confirmation available.
Show »
Length:196
Mass (Da):22,431
Checksum:i0E4DBC70BB97D704
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti177 – 1771N → S.
Corresponds to variant rs6005062 [ dbSNP | Ensembl ].
VAR_054069

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 641641Missing in isoform 2. 1 PublicationVSP_003998Add
BLAST
Alternative sequencei642 – 66322EGMIS…FPKWL → MATSEILPSFVATMDASNFS FW in isoform 2. 1 PublicationVSP_003999Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF070662 mRNA. Translation: AAD20968.1.
AL080147 mRNA. Translation: CAB45740.1.
AL050258 mRNA. Translation: CAB43360.1.
BT007274 mRNA. Translation: AAP35938.1.
CT841511 mRNA. Translation: CAJ86441.1.
Z95115, Z99714 Genomic DNA. Translation: CAI17979.1.
Z99714, Z95115 Genomic DNA. Translation: CAI17878.1.
CH471095 Genomic DNA. Translation: EAW59723.1.
BC011599 mRNA. Translation: AAH11599.1.
CCDSiCCDS13838.1. [Q9UBB9-1]
PIRiT12531.
RefSeqiNP_001008697.1. NM_001008697.1. [Q9UBB9-1]
NP_036275.1. NM_012143.2. [Q9UBB9-1]
XP_011528381.1. XM_011530079.1. [Q9UBB9-1]
UniGeneiHs.20225.

Genome annotation databases

EnsembliENST00000405938; ENSP00000384297; ENSG00000100109. [Q9UBB9-1]
ENST00000407148; ENSP00000385861; ENSG00000100109. [Q9UBB9-1]
ENST00000407431; ENSP00000383892; ENSG00000100109. [Q9UBB9-1]
ENST00000407690; ENSP00000384421; ENSG00000100109. [Q9UBB9-1]
ENST00000619735; ENSP00000480171; ENSG00000100109. [Q9UBB9-1]
GeneIDi24144.
KEGGihsa:24144.
UCSCiuc003acr.4. human. [Q9UBB9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF070662 mRNA. Translation: AAD20968.1.
AL080147 mRNA. Translation: CAB45740.1.
AL050258 mRNA. Translation: CAB43360.1.
BT007274 mRNA. Translation: AAP35938.1.
CT841511 mRNA. Translation: CAJ86441.1.
Z95115, Z99714 Genomic DNA. Translation: CAI17979.1.
Z99714, Z95115 Genomic DNA. Translation: CAI17878.1.
CH471095 Genomic DNA. Translation: EAW59723.1.
BC011599 mRNA. Translation: AAH11599.1.
CCDSiCCDS13838.1. [Q9UBB9-1]
PIRiT12531.
RefSeqiNP_001008697.1. NM_001008697.1. [Q9UBB9-1]
NP_036275.1. NM_012143.2. [Q9UBB9-1]
XP_011528381.1. XM_011530079.1. [Q9UBB9-1]
UniGeneiHs.20225.

3D structure databases

ProteinModelPortaliQ9UBB9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117294. 143 interactions.
IntActiQ9UBB9. 117 interactions.
MINTiMINT-3078852.
STRINGi9606.ENSP00000383892.

PTM databases

iPTMnetiQ9UBB9.
PhosphoSiteiQ9UBB9.

Polymorphism and mutation databases

BioMutaiTFIP11.
DMDMi22096235.

Proteomic databases

EPDiQ9UBB9.
MaxQBiQ9UBB9.
PaxDbiQ9UBB9.
PeptideAtlasiQ9UBB9.
PRIDEiQ9UBB9.

Protocols and materials databases

DNASUi24144.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000405938; ENSP00000384297; ENSG00000100109. [Q9UBB9-1]
ENST00000407148; ENSP00000385861; ENSG00000100109. [Q9UBB9-1]
ENST00000407431; ENSP00000383892; ENSG00000100109. [Q9UBB9-1]
ENST00000407690; ENSP00000384421; ENSG00000100109. [Q9UBB9-1]
ENST00000619735; ENSP00000480171; ENSG00000100109. [Q9UBB9-1]
GeneIDi24144.
KEGGihsa:24144.
UCSCiuc003acr.4. human. [Q9UBB9-1]

Organism-specific databases

CTDi24144.
GeneCardsiTFIP11.
HGNCiHGNC:17165. TFIP11.
HPAiHPA027085.
MIMi612747. gene.
neXtProtiNX_Q9UBB9.
PharmGKBiPA38441.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2184. Eukaryota.
ENOG410XP4Y. LUCA.
GeneTreeiENSGT00390000012739.
HOGENOMiHOG000230470.
HOVERGENiHBG055868.
InParanoidiQ9UBB9.
KOiK13103.
OMAiDECARVF.
OrthoDBiEOG79KPDZ.
PhylomeDBiQ9UBB9.
TreeFamiTF314887.

Miscellaneous databases

ChiTaRSiTFIP11. human.
GeneWikiiTFIP11.
GenomeRNAii24144.
PROiQ9UBB9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UBB9.
CleanExiHS_TFIP11.
ExpressionAtlasiQ9UBB9. baseline and differential.
GenevisibleiQ9UBB9. HS.

Family and domain databases

InterProiIPR000467. G_patch_dom.
IPR022783. GCFC_dom.
IPR024933. STIP.
IPR022159. STIP/TFIP11_N.
[Graphical view]
PfamiPF01585. G-patch. 1 hit.
PF07842. GCFC. 1 hit.
PF12457. TIP_N. 1 hit.
[Graphical view]
PIRSFiPIRSF017706. TFIP11. 1 hit.
SMARTiSM00443. G_patch. 1 hit.
[Graphical view]
PROSITEiPS50174. G_PATCH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Umbilical cord blood.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  3. "Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
    Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.
    Genome Res. 13:27-36(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Skin.
  9. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  10. "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-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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].
  13. "Isolation and characterization of post-splicing lariat-intron complexes."
    Yoshimoto R., Kataoka N., Okawa K., Ohno M.
    Nucleic Acids Res. 37:891-902(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SPLICEOSOME DISASSEMBLY, IDENTIFICATION IN THE INTRON LARGE COMPLEX, INTERACTION WITH DHX15.
  14. "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-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-98 AND SER-144, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-98 AND SER-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Identification of a novel component C2ORF3 in the lariat-intron complex: lack of C2ORF3 interferes with pre-mRNA splicing via intron turnover pathway."
    Yoshimoto R., Okawa K., Yoshida M., Ohno M., Kataoka N.
    Genes Cells 19:78-87(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GCFC2.
  19. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTFP11_HUMAN
AccessioniPrimary (citable) accession number: Q9UBB9
Secondary accession number(s): O95908
, Q20WL0, Q5H8V8, Q9UGV7, Q9Y2Q8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 150 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 22
    Human chromosome 22: 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.