SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q16630

- CPSF6_HUMAN

UniProt

Q16630 - CPSF6_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Cleavage and polyadenylation specificity factor subunit 6

Gene
CPSF6, CFIM68
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Component of the cleavage factor Im complex (CFIm) that plays a key role in pre-mRNA 3'-processing. Involved in association with NUDT21/CPSF5 in pre-MRNA 3'-end poly(A) site cleavage and poly(A) addition. CPSF6 binds to cleavage and polyadenylation RNA substrates and promotes RNA looping.5 Publications

GO - Molecular functioni

  1. mRNA binding Source: UniProtKB
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. mRNA polyadenylation Source: UniProtKB
  2. mRNA processing Source: UniProtKB
  3. protein tetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_121141. Signaling by FGFR1 fusion mutants.

Names & Taxonomyi

Protein namesi
Recommended name:
Cleavage and polyadenylation specificity factor subunit 6
Alternative name(s):
Cleavage and polyadenylation specificity factor 68 kDa subunit
Short name:
CFIm68
Short name:
CPSF 68 kDa subunit
Pre-mRNA cleavage factor Im 68 kDa subunit
Protein HPBRII-4/7
Gene namesi
Name:CPSF6
Synonyms:CFIM68
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:13871. CPSF6.

Subcellular locationi

Nucleus
Note: In punctate subnuclear structures localized adjacent to nuclear speckles, called paraspeckles.3 Publications

GO - Cellular componenti

  1. mRNA cleavage factor complex Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. paraspeckles Source: UniProtKB
  4. ribonucleoprotein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi84 – 841Y → A: Reduces affinity for UGUA RNA by 40%; when associated with A-128. 1 Publication
Mutagenesisi86 – 861G → V: Abolishes interaction with NUDT21/CPSF5; when associated with V-87. 1 Publication
Mutagenesisi87 – 871N → V: Abolishes interaction with NUDT21/CPSF5; when associated with V-86. 1 Publication
Mutagenesisi90 – 912WW → AA: Reduces affinity for UGUA RNA by 70%. Strongly reduced affinity for UGUA RNA; when associated with A-94.
Mutagenesisi94 – 941D → A: Strongly reduced affinity for UGUA RNA; when associated with 90-A-A-91. 1 Publication
Mutagenesisi111 – 1111E → A: Reduces affinity for UGUA RNA by 85%. 1 Publication
Mutagenesisi126 – 1261F → A: Increases affinity for UGUA RNA by 40%. 1 Publication
Mutagenesisi128 – 1281L → A: Reduces affinity for UGUA RNA by 40%; when associated with A-84. 1 Publication

Organism-specific databases

PharmGKBiPA26846.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 551551Cleavage and polyadenylation specificity factor subunit 6PRO_0000081521Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei404 – 4041Phosphothreonine1 Publication
Modified residuei407 – 4071Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ16630.
PaxDbiQ16630.
PeptideAtlasiQ16630.
PRIDEiQ16630.

PTM databases

PhosphoSiteiQ16630.

Expressioni

Gene expression databases

ArrayExpressiQ16630.
BgeeiQ16630.
CleanExiHS_CPSF6.
GenevestigatoriQ16630.

Organism-specific databases

HPAiHPA039973.

Interactioni

Subunit structurei

Component of the cleavage factor Im (CFIm) complex, composed at least of NUDT21/CPSF5 and CPSF6 or CPSF7. Within the cleavage factor Im complex, the NUDT21/CPSF5 homodimer is at the core of a heterotetramer, and is clasped by two additional subunits (CPSF6 or CPSF7). Interacts with NUDT21/CPSF5, SFRS3, SFRS7, SNRNP70 and TRA2B/SFRS10.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NUDT21O438095EBI-358410,EBI-355720
PLSCR1O151622EBI-358410,EBI-740019
WWP1Q9H0M03EBI-358410,EBI-742157

Protein-protein interaction databases

BioGridi116238. 62 interactions.
DIPiDIP-34501N.
IntActiQ16630. 28 interactions.
MINTiMINT-1153789.
STRINGi9606.ENSP00000391774.

Structurei

Secondary structure

1
551
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi84 – 874
Helixi94 – 1029
Turni103 – 1053
Beta strandi112 – 1165
Turni118 – 1203
Beta strandi123 – 1297
Helixi134 – 14310
Helixi144 – 1463
Beta strandi149 – 1513
Beta strandi155 – 1584
Helixi161 – 17010

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P5TX-ray2.70L/M/N/O/P/Q80-161[»]
3P6YX-ray2.90C/D/G/H/K/L/O/P80-161[»]
3Q2SX-ray2.90C/D13-235[»]
3Q2TX-ray3.06C/D13-235[»]
4B4NX-ray1.81B276-290[»]
ProteinModelPortaliQ16630.
SMRiQ16630. Positions 80-158.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 16181RRMAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni81 – 16181Necessary for interaction with NUDT21/CPSF5Add
BLAST
Regioni510 – 55142Sufficient for nuclear targetingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi208 – 398191Pro-richAdd
BLAST
Compositional biasi490 – 55162Arg-richAdd
BLAST

Sequence similaritiesi

Belongs to the RRM CPSF6/7 family.

Phylogenomic databases

eggNOGiNOG313287.
HOGENOMiHOG000111137.
KOiK14398.
OMAiSAPNVVY.
OrthoDBiEOG74TX09.
PhylomeDBiQ16630.
TreeFamiTF316430.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q16630-1) [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

MADGVDHIDI YADVGEEFNQ EAEYGGHDQI DLYDDVISPS ANNGDAPEDR    50
DYMDTLPPTV GDDVGKGAAP NVVYTYTGKR IALYIGNLTW WTTDEDLTEA 100
VHSLGVNDIL EIKFFENRAN GQSKGFALVG VGSEASSKKL MDLLPKRELH 150
GQNPVVTPCN KQFLSQFEMQ SRKTTQSGQM SGEGKAGPPG GSSRAAFPQG 200
GRGRGRFPGA VPGGDRFPGP AGPGGPPPPF PAGQTPPRPP LGPPGPPGPP 250
GPPPPGQVLP PPLAGPPNRG DRPPPPVLFP GQPFGQPPLG PLPPGPPPPV 300
PGYGPPPGPP PPQQGPPPPP GPFPPRPPGP LGPPLTLAPP PHLPGPPPGA 350
PPPAPHVNPA FFPPPTNSGM PTSDSRGPPP TDPYGRPPPY DRGDYGPPGR 400
EMDTARTPLS EAEFEEIMNR NRAISSSAIS RAVSDASAGD YGSAIETLVT 450
AISLIKQSKV SADDRCKVLI SSLQDCLHGI ESKSYGSGSR RERSRERDHS 500
RSREKSRRHK SRSRDRHDDY YRERSRERER HRDRDRDRDR ERDREREYRH 550
R 551
Length:551
Mass (Da):59,210
Last modified:February 7, 2006 - v2
Checksum:i721A5DA1B456AA79
GO
Isoform 2 (identifier: Q16630-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     231-231: P → PGNLIKHLVKGTRPLFLETRIPWHMGHSIEEIPIFGLK

Show »
Length:588
Mass (Da):63,471
Checksum:i1F2B7051251A7E52
GO
Isoform 3 (identifier: Q16630-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     188-260: Missing.

Show »
Length:478
Mass (Da):52,326
Checksum:i464F41AA4386F880
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei188 – 26073Missing in isoform 3. VSP_017191Add
BLAST
Alternative sequencei231 – 2311P → PGNLIKHLVKGTRPLFLETR IPWHMGHSIEEIPIFGLK in isoform 2. VSP_017192

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91D → N in CAA47751. 1 Publication
Sequence conflicti9 – 91D → N in CAA47752. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X67336 Genomic DNA. Translation: CAA47751.1.
X67337 mRNA. Translation: CAA47752.1.
AK223568 mRNA. Translation: BAD97288.1.
AK292024 mRNA. Translation: BAF84713.1.
CH471054 Genomic DNA. Translation: EAW97215.1.
BC000714 mRNA. Translation: AAH00714.1.
BC005000 mRNA. Translation: AAH05000.1.
CCDSiCCDS8988.1. [Q16630-1]
PIRiS57447.
RefSeqiNP_008938.2. NM_007007.2. [Q16630-1]
XP_005268646.1. XM_005268589.1. [Q16630-2]
UniGeneiHs.369606.

Genome annotation databases

EnsembliENST00000266679; ENSP00000266679; ENSG00000111605. [Q16630-2]
ENST00000435070; ENSP00000391774; ENSG00000111605. [Q16630-1]
GeneIDi11052.
KEGGihsa:11052.
UCSCiuc001sut.4. human. [Q16630-1]
uc001suu.4. human. [Q16630-2]

Polymorphism databases

DMDMi88909266.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X67336 Genomic DNA. Translation: CAA47751.1 .
X67337 mRNA. Translation: CAA47752.1 .
AK223568 mRNA. Translation: BAD97288.1 .
AK292024 mRNA. Translation: BAF84713.1 .
CH471054 Genomic DNA. Translation: EAW97215.1 .
BC000714 mRNA. Translation: AAH00714.1 .
BC005000 mRNA. Translation: AAH05000.1 .
CCDSi CCDS8988.1. [Q16630-1 ]
PIRi S57447.
RefSeqi NP_008938.2. NM_007007.2. [Q16630-1 ]
XP_005268646.1. XM_005268589.1. [Q16630-2 ]
UniGenei Hs.369606.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3P5T X-ray 2.70 L/M/N/O/P/Q 80-161 [» ]
3P6Y X-ray 2.90 C/D/G/H/K/L/O/P 80-161 [» ]
3Q2S X-ray 2.90 C/D 13-235 [» ]
3Q2T X-ray 3.06 C/D 13-235 [» ]
4B4N X-ray 1.81 B 276-290 [» ]
ProteinModelPortali Q16630.
SMRi Q16630. Positions 80-158.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116238. 62 interactions.
DIPi DIP-34501N.
IntActi Q16630. 28 interactions.
MINTi MINT-1153789.
STRINGi 9606.ENSP00000391774.

PTM databases

PhosphoSitei Q16630.

Polymorphism databases

DMDMi 88909266.

Proteomic databases

MaxQBi Q16630.
PaxDbi Q16630.
PeptideAtlasi Q16630.
PRIDEi Q16630.

Protocols and materials databases

DNASUi 11052.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000266679 ; ENSP00000266679 ; ENSG00000111605 . [Q16630-2 ]
ENST00000435070 ; ENSP00000391774 ; ENSG00000111605 . [Q16630-1 ]
GeneIDi 11052.
KEGGi hsa:11052.
UCSCi uc001sut.4. human. [Q16630-1 ]
uc001suu.4. human. [Q16630-2 ]

Organism-specific databases

CTDi 11052.
GeneCardsi GC12P069633.
HGNCi HGNC:13871. CPSF6.
HPAi HPA039973.
MIMi 604979. gene.
neXtProti NX_Q16630.
PharmGKBi PA26846.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG313287.
HOGENOMi HOG000111137.
KOi K14398.
OMAi SAPNVVY.
OrthoDBi EOG74TX09.
PhylomeDBi Q16630.
TreeFami TF316430.

Enzyme and pathway databases

Reactomei REACT_121141. Signaling by FGFR1 fusion mutants.

Miscellaneous databases

GeneWikii CPSF6.
GenomeRNAii 11052.
NextBioi 41995.
PROi Q16630.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q16630.
Bgeei Q16630.
CleanExi HS_CPSF6.
Genevestigatori Q16630.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
SMARTi SM00360. RRM. 1 hit.
[Graphical view ]
PROSITEi PS50102. RRM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human pre-mRNA cleavage factor Im is related to spliceosomal SR proteins and can be reconstituted in vitro from recombinant subunits."
    Rueegsegger U., Blank D., Keller W.
    Mol. Cell 1:243-253(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 125-138 AND 162-168, FUNCTION, IDENTIFICATION IN THE CLEAVAGE FACTOR IM COMPLEX, SUBCELLULAR LOCATION.
    Tissue: Leukemia.
  2. Fleischhauer K.L.
    Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    Tissue: Leukemia.
  3. "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).
    Tissue: Spleen.
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Heart.
  5. 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 2 AND 3).
    Tissue: Kidney.
  7. "Purification and characterization of human cleavage factor Im involved in the 3' end processing of messenger RNA precursors."
    Rueegsegger U., Beyer K., Keller W.
    J. Biol. Chem. 271:6107-6113(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX.
  8. "A mechanism for the regulation of pre-mRNA 3' processing by human cleavage factor Im."
    Brown K.M., Gilmartin G.M.
    Mol. Cell 12:1467-1476(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization."
    Dettwiler S., Aringhieri C., Cardinale S., Keller W., Barabino S.M.
    J. Biol. Chem. 279:35788-35797(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, INTERACTION WITH NUDT21/CPSF5; SFRS3; SFRS7 AND TRA2B, RNA-BINDING, MUTAGENESIS OF GLY-86 AND ASN-87, SUBCELLULAR LOCATION.
  10. "Association of polyadenylation cleavage factor I with U1 snRNP."
    Awasthi S., Alwine J.C.
    RNA 9:1400-1409(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, INTERACTION WITH NUDT21/CPSF5 AND SNRNP70.
  11. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-404, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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 THR-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Evidence that cleavage factor Im is a heterotetrameric protein complex controlling alternative polyadenylation."
    Kim S., Yamamoto J., Chen Y., Aida M., Wada T., Handa H., Yamaguchi Y.
    Genes Cells 15:1003-1013(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Crystal structure of a human cleavage factor CFI(m)25/CFI(m)68/RNA complex provides an insight into poly(A) site recognition and RNA looping."
    Yang Q., Coseno M., Gilmartin G.M., Doublie S.
    Structure 19:368-377(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 13-235 IN COMPLEX WITH NUDT21/CPSF5 AND RNA, FUNCTION, SUBUNIT, MUTAGENESIS OF TYR-84; 90-TRP-TRP-91; ASP-94; GLU-111; PHE-126 AND LEU-128.

Entry informationi

Entry nameiCPSF6_HUMAN
AccessioniPrimary (citable) accession number: Q16630
Secondary accession number(s): A8K7K9
, Q53ES1, Q9BSJ7, Q9BW18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: February 7, 2006
Last modified: September 3, 2014
This is version 128 of the entry and version 2 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi