P33240 (CSTF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cleavage stimulation factor subunit 2

Alternative name(s):
CF-1 64 kDa subunit
Cleavage stimulation factor 64 kDa subunit
Short name=CSTF 64 kDa subunit
Short name=CstF-64

Gene names

Name:

CSTF2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	577 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. This subunit is directly involved in the binding to pre-mRNAs By similarity. Ref.5
Subunit structure	The CSTF complex is composed of CSTF1 (50 kDa subunit), CSTF2 (64 kDa subunit) and CSTF3 (77 kDa subunit). CSTF2 directly interacts with CSTF3, SYMPK and RPO2TC1. Interacts with HSF1 in heat-stressed cells. Interacts with CPSF2, CPSF3 and FIP1L1. Interacts with DDX1. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.16
Subcellular location	Nucleus. Note: Localized with DDX1 in cleavage bodies. Ref.9
Induction	Up-regulated during the G0 to S phase transition. Ref.6
Sequence similarities	Contains 1 RRM (RNA recognition motif) domain.
Sequence caution	The sequence CAI42681.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA cleavage Traceable author statement Ref.1. Source: ProtInc mRNA polyadenylation Traceable author statement Ref.1. Source: ProtInc mRNA splicing, via spliceosome Traceable author statement. Source: Reactome termination of RNA polymerase II transcription Traceable author statement. Source: Reactome
Cellular_component	cleavage body Inferred from direct assay Ref.9. Source: UniProtKB mRNA cleavage and polyadenylation specificity factor complex Inferred from direct assay PubMed 18305108Ref.16. Source: UniProtKB
Molecular_function	RNA binding Traceable author statement Ref.1. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BARD1	Q99728	5	EBI-711360,EBI-473181
SUB1	P53999	3	EBI-711374,EBI-998260

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P33240-1)

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.

Isoform 2 (identifier: P33240-2)

The sequence of this isoform differs from the canonical sequence as follows:
     235-251: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 577

577

Cleavage stimulation factor subunit 2

PRO_0000081531

Regions

Domain

16 – 94

79

RRM

Repeat

410 – 414

5

1; approximate

Repeat

415 – 419

5

2

Repeat

420 – 424

5

3

Repeat

425 – 429

5

4; approximate

Repeat

430 – 434

5

5; approximate

Repeat

435 – 439

5

6

Repeat

440 – 444

5

7

Repeat

445 – 449

5

8

Repeat

450 – 454

5

9

Repeat

455 – 459

5

10; approximate

Repeat

460 – 464

5

11

Repeat

465 – 469

5

12; approximate

Region

108 – 248

141

Interactions with CSTF3 and SYMPK

Region

410 – 469

60

12 X 5 AA tandem repeats of M-E-A-R-[AG]

Region

514 – 577

64

Interaction with RPO2TC1

Compositional bias

198 – 409

212

Gly/Pro-rich

Compositional bias

470 – 526

57

Gly/Pro-rich

Amino acid modifications

Modified residue

518

1

Phosphoserine Ref.12

Modified residue

524

1

Phosphoserine Ref.14 Ref.15

Natural variations

Alternative sequence

235 – 251

17

Missing in isoform 2.

VSP_014841

Secondary structure

1

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577

Helix Strand Turn

Details...

Helix

12 – 15

4

Beta strand

18 – 22

5

Helix

29 – 37

9

Beta strand

43 – 50

8

Turn

51 – 54

4

Beta strand

55 – 63

9

Helix

67 – 76

10

Beta strand

77 – 81

5

Beta strand

83 – 85

3

Beta strand

87 – 91

5

Helix

97 – 104

8

Helix

532 – 535

4

Helix

537 – 545

9

Helix

549 – 553

5

Helix

557 – 560

4

Helix

562 – 571

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: B76595E9BF8FABBD	FASTA	577	60,959
	10 20 30 40 50 60 MAGLTVRDPA VDRSLRSVFV GNIPYEATEE QLKDIFSEVG PVVSFRLVYD RETGKPKGYG 70 80 90 100 110 120 FCEYQDQETA LSAMRNLNGR EFSGRALRVD NAASEKNKEE LKSLGTGAPV IESPYGETIS 130 140 150 160 170 180 PEDAPESISK AVASLPPEQM FELMKQMKLC VQNSPQEARN MLLQNPQLAY ALLQAQVVMR 190 200 210 220 230 240 IVDPEIALKI LHRQTNIPTL IAGNPQPVHG AGPGSGSNVS MNQQNPQAPQ AQSLGGMHVN 250 260 270 280 290 300 GAPPLMQASM QGGVPAPGQM PAAVTGPGPG SLAPGGGMQA QVGMPGSGPV SMERGQVPMQ 310 320 330 340 350 360 DPRAAMQRGS LPANVPTPRG LLGDAPNDPR GGTLLSVTGE VEPRGYLGPP HQGPPMHHVP 370 380 390 400 410 420 GHESRGPPPH ELRGGPLPEP RPLMAEPRGP MLDQRGPPLD GRGGRDPRGI DARGMEARAM 430 440 450 460 470 480 EARGLDARGL EARAMEARAM EARAMEARAM EARAMEVRGM EARGMDTRGP VPGPRGPIPS 490 500 510 520 530 540 GMQGPSPINM GAVVPQGSRQ VPVMQGTGMQ GASIQGGSQP GGFSPGQNQV TPQDHEKAAL 550 560 570 IMQVLQLTAD QIAMLPPEQR QSILILKEQI QKSTGAP
	Isoform 2 [UniParc]. Checksum: D76823A0FF6363B8	FASTA	560	59,251
	10 20 30 40 50 60 MAGLTVRDPA VDRSLRSVFV GNIPYEATEE QLKDIFSEVG PVVSFRLVYD RETGKPKGYG 70 80 90 100 110 120 FCEYQDQETA LSAMRNLNGR EFSGRALRVD NAASEKNKEE LKSLGTGAPV IESPYGETIS 130 140 150 160 170 180 PEDAPESISK AVASLPPEQM FELMKQMKLC VQNSPQEARN MLLQNPQLAY ALLQAQVVMR 190 200 210 220 230 240 IVDPEIALKI LHRQTNIPTL IAGNPQPVHG AGPGSGSNVS MNQQNPQAPQ AQSLGGVPAP 250 260 270 280 290 300 GQMPAAVTGP GPGSLAPGGG MQAQVGMPGS GPVSMERGQV PMQDPRAAMQ RGSLPANVPT 310 320 330 340 350 360 PRGLLGDAPN DPRGGTLLSV TGEVEPRGYL GPPHQGPPMH HVPGHESRGP PPHELRGGPL 370 380 390 400 410 420 PEPRPLMAEP RGPMLDQRGP PLDGRGGRDP RGIDARGMEA RAMEARGLDA RGLEARAMEA 430 440 450 460 470 480 RAMEARAMEA RAMEARAMEV RGMEARGMDT RGPVPGPRGP IPSGMQGPSP INMGAVVPQG 490 500 510 520 530 540 SRQVPVMQGT GMQGASIQGG SQPGGFSPGQ NQVTPQDHEK AALIMQVLQL TADQIAMLPP 550 560 EQRQSILILK EQIQKSTGAP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human 64-kDa polyadenylylation factor contains a ribonucleoprotein-type RNA binding domain and unusual auxiliary motifs." Takagaki Y., Macdonald C.C., Shenk T., Manley J.L. Proc. Natl. Acad. Sci. U.S.A. 89:1403-1407(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION, RNA-BINDING.
[2]	"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 (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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 2). Tissue: Kidney and Ovary.
[5]	"RNA recognition by the human polyadenylation factor CstF." Takagaki Y., Manley J.L. Mol. Cell. Biol. 17:3907-3914(1997) [PubMed] [Europe PMC] [Abstract] Cited for: RNA-BINDING, FUNCTION.
[6]	"Increase in the 64-kDa subunit of the polyadenylation/cleavage stimulatory factor during the G0 to S phase transition." Martincic K., Campbell R., Edwalds-Gilbert G., Souan L., Lotze M.T., Milcarek C. Proc. Natl. Acad. Sci. U.S.A. 95:11095-11100(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[7]	"Complex protein interactions within the human polyadenylation machinery identify a novel component." Takagaki Y., Manley J.L. Mol. Cell. Biol. 20:1515-1525(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CSTF3 AND SYMPK.
[8]	"Evolutionarily conserved interaction between CstF-64 and PC4 links transcription, polyadenylation, and termination." Calvo O., Manley J.L. Mol. Cell 7:1013-1023(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RPO2TC1.
[9]	"Association of human DEAD box protein DDX1 with a cleavage stimulation factor involved in 3'-end processing of pre-MRNA." Bleoo S., Sun X., Hendzel M.J., Rowe J.M., Packer M., Godbout R. Mol. Biol. Cell 12:3046-3059(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DDX1, SUBCELLULAR LOCATION.
[10]	"Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and stimulates poly(A) polymerase." Kaufmann I., Martin G., Friedlein A., Langen H., Keller W. EMBO J. 23:616-626(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FIP1L1.
[11]	"HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with symplekin." Xing H., Mayhew C.N., Cullen K.E., Park-Sarge O.-K., Sarge K.D. J. Biol. Chem. 279:10551-10555(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HSF1.
[12]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3'-end maturation." Kolev N.G., Yario T.A., Benson E., Steitz J.A. EMBO Rep. 9:1013-1018(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CPSF2 AND CPSF3.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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-524, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF interaction and specificity toward the pre-mRNA." Laishram R.S., Anderson R.A. EMBO J. 29:4132-4145(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE CPSF COMPLEX.
[17]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]	"Recognition of GU-rich polyadenylation regulatory elements by human CstF-64 protein." Perez Canadillas J.M., Varani G. EMBO J. 22:2821-2830(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 8-111.
[21]	"The C-terminal domains of vertebrate CstF-64 and its yeast orthologue Rna15 form a new structure critical for mRNA 3'-end processing." Qu X., Perez-Canadillas J.M., Agrawal S., De Baecke J., Cheng H., Varani G., Moore C. J. Biol. Chem. 282:2101-2115(2007) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 531-577.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M85085 mRNA. Translation: AAA35724.1.
BT009778 mRNA. Translation: AAP88780.1.
Z83819, Z95327 Genomic DNA. Translation: CAB06072.2.
Z95327, Z83819 Genomic DNA. Translation: CAI42680.1.
Z95327 Genomic DNA. Translation: CAI42681.1. Sequence problems.
BC017712 mRNA. Translation: AAH17712.1.
BC033135 mRNA. Translation: AAH33135.1.

IPI

IPI00013256.
IPI00607841.

PIR

A40220.

RefSeq

NP_001316.1. NM_001325.2.

UniGene

Hs.132370.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P1T	NMR	-	A	8-111	[»]
2J8P	NMR	-	A	531-577	[»]

ProteinModelPortal

P33240.

SMR

P33240. Positions 8-164, 529-577.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36129N.

IntAct

P33240. 15 interactions.

MINT

MINT-1375144.

STRING

9606.ENSP00000362063.

PTM databases

PhosphoSite

P33240.

Polymorphism databases

DMDM

461847.

Proteomic databases

PaxDb

P33240.

PRIDE

P33240.

Protocols and materials databases

DNASU

1478.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000372972; ENSP00000362063; ENSG00000101811.
ENST00000413437; ENSP00000415705; ENSG00000101811.

GeneID

1478.

KEGG

hsa:1478.

UCSC

uc004egh.3. human.
uc004egi.3. human.

Organism-specific databases

CTD

1478.

GeneCards

GC0XP100075.

HGNC

HGNC:2484. CSTF2.

HPA

CAB004680.
HPA000427.

MIM

600368. gene.

neXtProt

NX_P33240.

PharmGKB

PA26986.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0724.

HOGENOM

HOG000214373.

HOVERGEN

HBG051145.

InParanoid

P33240.

KO

K14407.

OrthoDB

EOG4640BW.

PhylomeDB

P33240.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpress

P33240.

Bgee

P33240.

CleanEx

HS_CSTF2.

Genevestigator

P33240.

GermOnline

ENSG00000101811. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 1 hit.

InterPro

IPR025742. CSTF2_hinge.
IPR026896. CSTF_C.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF14327. CSTF2_hinge. 1 hit.
PF14304. CSTF_C. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 1 hit.
[Graphical view]

PROSITE

PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P33240.

GenomeRNAi

1478.

NextBio

6073.

SOURCE

Search...

Entry information

Entry name

CSTF2_HUMAN

Accession

Primary (citable) accession number: P33240
Secondary accession number(s): Q5H951, Q6LA74, Q8N502

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	April 3, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.