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Protein

Cleavage and polyadenylation specificity factor subunit 7

Gene

CPSF7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Binds to cleavage and polyadenylation RNA substrates.1 Publication

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72187. mRNA 3'-end processing.
R-HSA-77595. Processing of Intronless Pre-mRNAs.

Names & Taxonomyi

Protein namesi
Recommended name:
Cleavage and polyadenylation specificity factor subunit 7
Alternative name(s):
Cleavage and polyadenylation specificity factor 59 kDa subunit
Short name:
CFIm59
Short name:
CPSF 59 kDa subunit
Pre-mRNA cleavage factor Im 59 kDa subunit
Gene namesi
Name:CPSF7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:30098. CPSF7.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB
  • mRNA cleavage factor complex Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165543380.

Polymorphism and mutation databases

BioMutaiCPSF7.
DMDMi74759932.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 471471Cleavage and polyadenylation specificity factor subunit 7PRO_0000081527Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031PhosphothreonineCombined sources
Modified residuei205 – 2051PhosphoserineBy similarity
Modified residuei413 – 4131PhosphoserineCombined sources
Modified residuei423 – 4231PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8N684.
MaxQBiQ8N684.
PaxDbiQ8N684.
PeptideAtlasiQ8N684.
PRIDEiQ8N684.

PTM databases

iPTMnetiQ8N684.
PhosphoSiteiQ8N684.
SwissPalmiQ8N684.

Miscellaneous databases

PMAP-CutDBQ8N684.

Expressioni

Gene expression databases

BgeeiQ8N684.
ExpressionAtlasiQ8N684. baseline and differential.
GenevisibleiQ8N684. HS.

Organism-specific databases

HPAiHPA041094.

Interactioni

Subunit structurei

Component of the cleavage factor Im (CFIm) complex, composed of, at least, 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/CPSF5.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AESQ081173EBI-746909,EBI-717810
ARMC7Q9H6L43EBI-746909,EBI-742909
ATXN1P542532EBI-746909,EBI-930964
CLK2P497603EBI-746909,EBI-750020
EPM2AIP1Q7L7753EBI-746909,EBI-6255981
NCK2O436394EBI-746909,EBI-713635
NUDT21O438095EBI-746909,EBI-355720
RUNX1T1Q06455-43EBI-746909,EBI-10224192
SEC23BQ154373EBI-746909,EBI-742673
SMAD3P840223EBI-746909,EBI-347161
SNRNP25Q9BV903EBI-746909,EBI-9675976
U2AF2P263682EBI-746909,EBI-742339

Protein-protein interaction databases

BioGridi122957. 79 interactions.
IntActiQ8N684. 37 interactions.
MINTiMINT-1469392.
STRINGi9606.ENSP00000345412.

Structurei

Secondary structure

1
471
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi83 – 875Combined sources
Helixi95 – 10410Combined sources
Beta strandi110 – 1178Combined sources
Turni119 – 1213Combined sources
Beta strandi124 – 13310Combined sources
Helixi135 – 14410Combined sources
Beta strandi156 – 1594Combined sources
Helixi162 – 17615Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N9UX-ray1.92C/I50-182[»]
ProteinModelPortaliQ8N684.
SMRiQ8N684. Positions 82-177.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8N684.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini82 – 16281RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi51 – 544Poly-Pro
Compositional biasi218 – 329112Pro-richAdd
BLAST
Compositional biasi418 – 46952Arg-richAdd
BLAST

Sequence similaritiesi

Belongs to the RRM CPSF6/7 family.Curated
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4849. Eukaryota.
ENOG4111NBM. LUCA.
GeneTreeiENSGT00730000110905.
HOGENOMiHOG000111137.
HOVERGENiHBG056699.
InParanoidiQ8N684.
KOiK14398.
OMAiRRGPFEG.
OrthoDBiEOG74TX09.
PhylomeDBiQ8N684.
TreeFamiTF316430.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8N684-1) [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
MSEGVDLIDI YADEEFNQDP EFNNTDQIDL YDDVLTATSQ PSDDRSSSTE
60 70 80 90 100
PPPPVRQEPS PKPNNKTPAI LYTYSGLRNR RAAVYVGSFS WWTTDQQLIQ
110 120 130 140 150
VIRSIGVYDV VELKFAENRA NGQSKGYAEV VVASENSVHK LLELLPGKVL
160 170 180 190 200
NGEKVDVRPA TRQNLSQFEA QARKRECVRV PRGGIPPRAH SRDSSDSADG
210 220 230 240 250
RATPSENLVP SSARVDKPPS VLPYFNRPPS ALPLMGLPPP PIPPPPPLSS
260 270 280 290 300
SFGVPPPPPG IHYQHLMPPP PRLPPHLAVP PPGAIPPALH LNPAFFPPPN
310 320 330 340 350
ATVGPPPDTY MKASAPYNHH GSRDSGPPPS TVSEAEFEDI MKRNRAISSS
360 370 380 390 400
AISKAVSGAS AGDYSDAIET LLTAIAVIKQ SRVANDERCR VLISSLKDCL
410 420 430 440 450
HGIEAKSYSV GASGSSSRKR HRSRERSPSR SRESSRRHRD LLHNEDRHDD
460 470
YFQERNREHE RHRDRERDRH H
Length:471
Mass (Da):52,050
Last modified:October 1, 2002 - v1
Checksum:i69529E441D742CF9
GO
Isoform 2 (identifier: Q8N684-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     176-184: Missing.

Show »
Length:462
Mass (Da):51,096
Checksum:iA3E41F7CB8340247
GO
Isoform 3 (identifier: Q8N684-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGRPESAGGGSRGPFEGGGRARRAGGIFLTLSILRTRDLPSGAM

Show »
Length:514
Mass (Da):56,375
Checksum:i37D5BE0605F7A0FB
GO

Sequence cautioni

The sequence AAH18135.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB14118.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAD97884.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti335 – 3351A → V in CAD97884 (PubMed:17974005).Curated
Sequence conflicti353 – 3531S → F in CAD97884 (PubMed:17974005).Curated
Sequence conflicti387 – 3871E → D in BAB14118 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MGRPESAGGGSRGPFEGGGR ARRAGGIFLTLSILRTRDLP SGAM in isoform 3. CuratedVSP_038975
Alternative sequencei176 – 1849Missing in isoform 2. 1 PublicationVSP_017194

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ275970 mRNA. Translation: CAC81661.1.
AK022591 mRNA. Translation: BAB14118.1. Different initiation.
AK096343 mRNA. Translation: BAG53266.1.
AL512759 mRNA. Translation: CAC21678.1.
BX537888 mRNA. Translation: CAD97884.1. Different initiation.
AP003108 Genomic DNA. No translation available.
BC018135 mRNA. Translation: AAH18135.1. Different initiation.
CCDSiCCDS44619.1. [Q8N684-1]
CCDS44620.1. [Q8N684-2]
CCDS8006.2. [Q8N684-3]
RefSeqiNP_001129512.1. NM_001136040.2. [Q8N684-1]
NP_001136037.1. NM_001142565.1. [Q8N684-2]
NP_079087.3. NM_024811.3. [Q8N684-3]
XP_005274356.1. XM_005274299.3. [Q8N684-1]
XP_011543560.1. XM_011545258.1. [Q8N684-1]
XP_011543561.1. XM_011545259.1. [Q8N684-2]
UniGeneiHs.718984.

Genome annotation databases

EnsembliENST00000340437; ENSP00000345412; ENSG00000149532. [Q8N684-3]
ENST00000394888; ENSP00000378352; ENSG00000149532. [Q8N684-1]
ENST00000439958; ENSP00000397203; ENSG00000149532. [Q8N684-2]
ENST00000448745; ENSP00000407394; ENSG00000149532. [Q8N684-2]
GeneIDi79869.
KEGGihsa:79869.
UCSCiuc001nrp.4. human. [Q8N684-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ275970 mRNA. Translation: CAC81661.1.
AK022591 mRNA. Translation: BAB14118.1. Different initiation.
AK096343 mRNA. Translation: BAG53266.1.
AL512759 mRNA. Translation: CAC21678.1.
BX537888 mRNA. Translation: CAD97884.1. Different initiation.
AP003108 Genomic DNA. No translation available.
BC018135 mRNA. Translation: AAH18135.1. Different initiation.
CCDSiCCDS44619.1. [Q8N684-1]
CCDS44620.1. [Q8N684-2]
CCDS8006.2. [Q8N684-3]
RefSeqiNP_001129512.1. NM_001136040.2. [Q8N684-1]
NP_001136037.1. NM_001142565.1. [Q8N684-2]
NP_079087.3. NM_024811.3. [Q8N684-3]
XP_005274356.1. XM_005274299.3. [Q8N684-1]
XP_011543560.1. XM_011545258.1. [Q8N684-1]
XP_011543561.1. XM_011545259.1. [Q8N684-2]
UniGeneiHs.718984.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N9UX-ray1.92C/I50-182[»]
ProteinModelPortaliQ8N684.
SMRiQ8N684. Positions 82-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122957. 79 interactions.
IntActiQ8N684. 37 interactions.
MINTiMINT-1469392.
STRINGi9606.ENSP00000345412.

PTM databases

iPTMnetiQ8N684.
PhosphoSiteiQ8N684.
SwissPalmiQ8N684.

Polymorphism and mutation databases

BioMutaiCPSF7.
DMDMi74759932.

Proteomic databases

EPDiQ8N684.
MaxQBiQ8N684.
PaxDbiQ8N684.
PeptideAtlasiQ8N684.
PRIDEiQ8N684.

Protocols and materials databases

DNASUi79869.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340437; ENSP00000345412; ENSG00000149532. [Q8N684-3]
ENST00000394888; ENSP00000378352; ENSG00000149532. [Q8N684-1]
ENST00000439958; ENSP00000397203; ENSG00000149532. [Q8N684-2]
ENST00000448745; ENSP00000407394; ENSG00000149532. [Q8N684-2]
GeneIDi79869.
KEGGihsa:79869.
UCSCiuc001nrp.4. human. [Q8N684-1]

Organism-specific databases

CTDi79869.
GeneCardsiCPSF7.
HGNCiHGNC:30098. CPSF7.
HPAiHPA041094.
neXtProtiNX_Q8N684.
PharmGKBiPA165543380.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4849. Eukaryota.
ENOG4111NBM. LUCA.
GeneTreeiENSGT00730000110905.
HOGENOMiHOG000111137.
HOVERGENiHBG056699.
InParanoidiQ8N684.
KOiK14398.
OMAiRRGPFEG.
OrthoDBiEOG74TX09.
PhylomeDBiQ8N684.
TreeFamiTF316430.

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72187. mRNA 3'-end processing.
R-HSA-77595. Processing of Intronless Pre-mRNAs.

Miscellaneous databases

ChiTaRSiCPSF7. human.
EvolutionaryTraceiQ8N684.
GeneWikiiFLJ12529.
GenomeRNAii79869.
PMAP-CutDBQ8N684.
PROiQ8N684.

Gene expression databases

BgeeiQ8N684.
ExpressionAtlasiQ8N684. baseline and differential.
GenevisibleiQ8N684. HS.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a second SR protein related subunit of human pre-mRNA cleavage factor I."
    Rueegsegger U., Blank D., Dettwiler S., Keller W.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Cervix carcinoma.
  2. "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: Teratocarcinoma.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Bone marrow and Embryonic brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Uterus.
  6. "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, RNA-BINDING.
  7. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "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-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND SER-413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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: SUBUNIT, SUBCELLULAR LOCATION.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "Crystal structure of the complex between the 25 kDA subunit and the 59 kDA subunit (RRM domain) of human cleavage factor Im."
    Structural genomics consortium (SGC)
    Submitted (JUL-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 50-182 IN COMPLEX WITH NUDT21/CPSF5, SUBUNIT.

Entry informationi

Entry nameiCPSF7_HUMAN
AccessioniPrimary (citable) accession number: Q8N684
Secondary accession number(s): B3KU04
, C9K0Q4, Q7Z3H9, Q9H025, Q9H9V1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: October 1, 2002
Last modified: July 6, 2016
This is version 136 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, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.