Q9Y5B0 (CTDP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RNA polymerase II subunit A C-terminal domain phosphatase
EC=3.1.3.16

Alternative name(s):
TFIIF-associating CTD phosphatase

Gene names

Name:	CTDP1
Synonyms:	FCP1

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	961 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. This promotes the activity of RNA polymerase II. Plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation. Ref.14
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Subunit structure	Homodimer. Interacts with GTF2F1. Interacts with WDR77, SNRPB and SNRNP70. Ref.1 Ref.6
Subcellular location	Nucleus. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle. Cytoplasm › cytoskeleton › spindle pole. Midbody. Note: Found at centrosomes in prometaphase, at spindle and spindle poles in metaphase and at spindle midzone and midbody in anaphase and telophase-G1 respectively. Ref.14
Tissue specificity	Ubiquitously expressed. Isoform 3 is expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and placenta. Ref.1
Post-translational modification	Phosphorylated. In the presence of TFIIF, the phosphorylated form has an increased CTD phosphatase activity. The phosphorylation is required for the physical interaction with GTF2F1. Ref.7
Involvement in disease	Congenital cataracts, facial dysmorphism, and neuropathy (CCFDN) [MIM:604168]: An autosomal recessive developmental disorder characterized by a complex clinical phenotype with seemingly unrelated features involving multiple organs and systems. Developmental abnormalities include congenital cataracts and microcorneae, hypomyelination of the peripheral nervous system, impaired physical growth, delayed early motor and intellectual development, facial dysmorphism and hypogonadism. Central nervous system involvement, with cerebral and spinal cord atrophy, may be the result of disrupted development with superimposed degenerative changes. Affected individuals are prone to severe rhabdomyolysis after viral infections and to serious complications related to general anesthesia (such as pulmonary edema and epileptic seizures). Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16
Sequence similarities	Contains 1 BRCT domain. Contains 1 FCP1 homology domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Cataract
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW exit from mitosis Inferred from mutant phenotype Ref.14. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of viral transcription Traceable author statement. Source: Reactome protein dephosphorylation Inferred from direct assay Ref.14. Source: UniProtKB transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular_component	actin cytoskeleton Inferred from direct assay. Source: HPA centrosome Inferred from direct assay Ref.14. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW midbody Inferred from direct assay Ref.14. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome spindle midzone Inferred from direct assay Ref.14. Source: UniProtKB spindle pole Inferred from direct assay Ref.14. Source: UniProtKB
Molecular_function	CTD phosphatase activity Inferred from direct assay PubMed 12721286. Source: UniProtKB DNA-directed RNA polymerase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y5B0-1)

Also known as: Fcp1;

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: Q9Y5B0-2)

Also known as: Fcp1a;

The sequence of this isoform differs from the canonical sequence as follows:
     1-119: Missing.
     807-961: AVPPPQPQMF...ALEAELNDLM → WTTSLEKAAT...AGGPEATRGS

Isoform 3 (identifier: Q9Y5B0-3)

Also known as: Fcp1b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-119: Missing.

Isoform 4 (identifier: Q9Y5B0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     807-961: AVPPPQPQMF...ALEAELNDLM → WTTSLEKAAT...AGGPEATRGS

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 961

961

RNA polymerase II subunit A C-terminal domain phosphatase

PRO_0000212564

Regions

Domain

178 – 344

167

FCP1 homology

Domain

629 – 728

100

BRCT

Compositional bias

455 – 478

24

Ser-rich

Compositional bias

577 – 582

6

Poly-Glu

Amino acid modifications

Modified residue

674

1

Phosphoserine Ref.11

Modified residue

780

1

N6-acetyllysine Ref.10

Modified residue

869

1

Phosphoserine Ref.8 Ref.11

Modified residue

872

1

Phosphoserine Ref.11 Ref.13

Natural variations

Alternative sequence

1 – 119

119

Missing in isoform 2 and isoform 3.

VSP_009864

Alternative sequence

807 – 961

155

AVPPP…LNDLM → WTTSLEKAATTATARRGGLR SRRRSPSPGSQGPAGSGRSG HLRPARGARQGAGGPEATRG S in isoform 2 and isoform 4.

VSP_009865

Natural variant

282

1

S → F.
Corresponds to variant rs4799078 [ dbSNP | Ensembl ].

VAR_060440

Natural variant

340

1

T → M.
Corresponds to variant rs2279103 [ dbSNP | Ensembl ].

VAR_018264

Natural variant

519

1

P → H.
Corresponds to variant rs557503 [ dbSNP | Ensembl ].

VAR_060441

Natural variant

755

1

L → S.
Corresponds to variant rs34967023 [ dbSNP | Ensembl ].

VAR_032763

Experimental info

Sequence conflict

61

1

S → A in AAD42088. Ref.2

Sequence conflict

61

1

S → A in AAH63447. Ref.5

Sequence conflict

157

1

P → A in AAC64549. Ref.1

Sequence conflict

281

1

F → I in AAH52576. Ref.5

Sequence conflict

305

1

E → K in AAD42088. Ref.2

Sequence conflict

390

1

A → P in AAC64549. Ref.1

Sequence conflict

478

1

S → T in AAC64549. Ref.1

Sequence conflict

486 – 487

2

KP → NA in AAC64549. Ref.1

Sequence conflict

504 – 505

2

EP → DA in AAC64549. Ref.1

Sequence conflict

513

1

L → V in AAC64549. Ref.1

Sequence conflict

656 – 657

2

EH → DD in AAC64549. Ref.1

Sequence conflict

896 – 900

5

ERTLG → GADAR in AAD42088. Ref.2

Secondary structure

1

.

.

.

.

.

.

961

Helix Strand Turn

Details...

Helix

586 – 598

13

Helix

945 – 956

12

Turn

957 – 959

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Fcp1) [UniParc]. Last modified April 5, 2011. Version 3. Checksum: 62B88FFD9CE4B157	FASTA	961	104,399
	10 20 30 40 50 60 MEVPAAGRVP AEGAPTAAVA EVRCPGPAPL RLLEWRVAAG AAVRIGSVLA VFEAAASAQS 70 80 90 100 110 120 SGASQSRVAS GGCVRPARPE RRLRSERAGV VRELCAQPGQ VVAPGAVLVR LEGCSHPVVM 130 140 150 160 170 180 KGLCAECGQD LTQLQSKNGK QQVPLSTATV SMVHSVPELM VSSEQAEQLG REDQQRLHRN 190 200 210 220 230 240 RKLVLMVDLD QTLIHTTEQH CQQMSNKGIF HFQLGRGEPM LHTRLRPHCK DFLEKIAKLY 250 260 270 280 290 300 ELHVFTFGSR LYAHTIAGFL DPEKKLFSHR ILSRDECIDP FSKTGNLRNL FPCGDSMVCI 310 320 330 340 350 360 IDDREDVWKF APNLITVKKY VYFQGTGDMN APPGSRESQT RKKVNHSRGT EVSEPSPPVR 370 380 390 400 410 420 DPEGVTQAPG VEPSNGLEKP ARELNGSEAA TPRDSPRPGK PDERDIWPPA QAPTSSQELA 430 440 450 460 470 480 GAPEPQGSCA QGGRVAPGQR PAQGATGTDL DFDLSSDSES SSESEGTKSS SSASDGESEG 490 500 510 520 530 540 KRGRQKPKAA PEGAGALAQG SSLEPGRPAA PSLPGEAEPG AHAPDKEPEL GGQEEGERDG 550 560 570 580 590 600 LCGLGNGCAD RKEAETESQN SELSGVTAGE SLDQSMEEEE EEDTDEDDHL IYLEEILVRV 610 620 630 640 650 660 HTDYYAKYDR YLNKEIEEAP DIRKIVPELK SKVLADVAII FSGLHPTNFP IEKTREHYHA 670 680 690 700 710 720 TALGAKILTR LVLSPDAPDR ATHLIAARAG TEKVLQAQEC GHLHVVNPDW LWSCLERWDK 730 740 750 760 770 780 VEEQLFPLRD DHTKAQRENS PAAFPDREGV PPTALFHPMP VLPKAQPGPE VRIYDSNTGK 790 800 810 820 830 840 LIRTGARGPP APSSSLPIRQ EPSSFRAVPP PQPQMFGEEL PDAQDGEQPG PSRRKRQPSM 850 860 870 880 890 900 SETMPLYTLC KEDLESMDKE VDDILGEGSD DSDSEKRRPE EQEEEPQPRK PGTRRERTLG 910 920 930 940 950 960 APASSERSAA GGRGPRGHKR KLNEEDAASE SSRESSNEDE GSSSEADEMA KALEAELNDL M
	Isoform 2 (Fcp1a) [UniParc]. Checksum: 8F32D19DF9F825B8	FASTA	748	81,463
	10 20 30 40 50 60 MKGLCAECGQ DLTQLQSKNG KQQVPLSTAT VSMVHSVPEL MVSSEQAEQL GREDQQRLHR 70 80 90 100 110 120 NRKLVLMVDL DQTLIHTTEQ HCQQMSNKGI FHFQLGRGEP MLHTRLRPHC KDFLEKIAKL 130 140 150 160 170 180 YELHVFTFGS RLYAHTIAGF LDPEKKLFSH RILSRDECID PFSKTGNLRN LFPCGDSMVC 190 200 210 220 230 240 IIDDREDVWK FAPNLITVKK YVYFQGTGDM NAPPGSRESQ TRKKVNHSRG TEVSEPSPPV 250 260 270 280 290 300 RDPEGVTQAP GVEPSNGLEK PARELNGSEA ATPRDSPRPG KPDERDIWPP AQAPTSSQEL 310 320 330 340 350 360 AGAPEPQGSC AQGGRVAPGQ RPAQGATGTD LDFDLSSDSE SSSESEGTKS SSSASDGESE 370 380 390 400 410 420 GKRGRQKPKA APEGAGALAQ GSSLEPGRPA APSLPGEAEP GAHAPDKEPE LGGQEEGERD 430 440 450 460 470 480 GLCGLGNGCA DRKEAETESQ NSELSGVTAG ESLDQSMEEE EEEDTDEDDH LIYLEEILVR 490 500 510 520 530 540 VHTDYYAKYD RYLNKEIEEA PDIRKIVPEL KSKVLADVAI IFSGLHPTNF PIEKTREHYH 550 560 570 580 590 600 ATALGAKILT RLVLSPDAPD RATHLIAARA GTEKVLQAQE CGHLHVVNPD WLWSCLERWD 610 620 630 640 650 660 KVEEQLFPLR DDHTKAQREN SPAAFPDREG VPPTALFHPM PVLPKAQPGP EVRIYDSNTG 670 680 690 700 710 720 KLIRTGARGP PAPSSSLPIR QEPSSFRWTT SLEKAATTAT ARRGGLRSRR RSPSPGSQGP 730 740 AGSGRSGHLR PARGARQGAG GPEATRGS
	Isoform 3 (Fcp1b) [UniParc]. Checksum: 3B01D7909C790957	FASTA	842	92,377
	10 20 30 40 50 60 MKGLCAECGQ DLTQLQSKNG KQQVPLSTAT VSMVHSVPEL MVSSEQAEQL GREDQQRLHR 70 80 90 100 110 120 NRKLVLMVDL DQTLIHTTEQ HCQQMSNKGI FHFQLGRGEP MLHTRLRPHC KDFLEKIAKL 130 140 150 160 170 180 YELHVFTFGS RLYAHTIAGF LDPEKKLFSH RILSRDECID PFSKTGNLRN LFPCGDSMVC 190 200 210 220 230 240 IIDDREDVWK FAPNLITVKK YVYFQGTGDM NAPPGSRESQ TRKKVNHSRG TEVSEPSPPV 250 260 270 280 290 300 RDPEGVTQAP GVEPSNGLEK PARELNGSEA ATPRDSPRPG KPDERDIWPP AQAPTSSQEL 310 320 330 340 350 360 AGAPEPQGSC AQGGRVAPGQ RPAQGATGTD LDFDLSSDSE SSSESEGTKS SSSASDGESE 370 380 390 400 410 420 GKRGRQKPKA APEGAGALAQ GSSLEPGRPA APSLPGEAEP GAHAPDKEPE LGGQEEGERD 430 440 450 460 470 480 GLCGLGNGCA DRKEAETESQ NSELSGVTAG ESLDQSMEEE EEEDTDEDDH LIYLEEILVR 490 500 510 520 530 540 VHTDYYAKYD RYLNKEIEEA PDIRKIVPEL KSKVLADVAI IFSGLHPTNF PIEKTREHYH 550 560 570 580 590 600 ATALGAKILT RLVLSPDAPD RATHLIAARA GTEKVLQAQE CGHLHVVNPD WLWSCLERWD 610 620 630 640 650 660 KVEEQLFPLR DDHTKAQREN SPAAFPDREG VPPTALFHPM PVLPKAQPGP EVRIYDSNTG 670 680 690 700 710 720 KLIRTGARGP PAPSSSLPIR QEPSSFRAVP PPQPQMFGEE LPDAQDGEQP GPSRRKRQPS 730 740 750 760 770 780 MSETMPLYTL CKEDLESMDK EVDDILGEGS DDSDSEKRRP EEQEEEPQPR KPGTRRERTL 790 800 810 820 830 840 GAPASSERSA AGGRGPRGHK RKLNEEDAAS ESSRESSNED EGSSSEADEM AKALEAELND LM
	Isoform 4 [UniParc]. Checksum: 8B4B87B24644BA6E	FASTA	867	93,485
	10 20 30 40 50 60 MEVPAAGRVP AEGAPTAAVA EVRCPGPAPL RLLEWRVAAG AAVRIGSVLA VFEAAASAQS 70 80 90 100 110 120 SGASQSRVAS GGCVRPARPE RRLRSERAGV VRELCAQPGQ VVAPGAVLVR LEGCSHPVVM 130 140 150 160 170 180 KGLCAECGQD LTQLQSKNGK QQVPLSTATV SMVHSVPELM VSSEQAEQLG REDQQRLHRN 190 200 210 220 230 240 RKLVLMVDLD QTLIHTTEQH CQQMSNKGIF HFQLGRGEPM LHTRLRPHCK DFLEKIAKLY 250 260 270 280 290 300 ELHVFTFGSR LYAHTIAGFL DPEKKLFSHR ILSRDECIDP FSKTGNLRNL FPCGDSMVCI 310 320 330 340 350 360 IDDREDVWKF APNLITVKKY VYFQGTGDMN APPGSRESQT RKKVNHSRGT EVSEPSPPVR 370 380 390 400 410 420 DPEGVTQAPG VEPSNGLEKP ARELNGSEAA TPRDSPRPGK PDERDIWPPA QAPTSSQELA 430 440 450 460 470 480 GAPEPQGSCA QGGRVAPGQR PAQGATGTDL DFDLSSDSES SSESEGTKSS SSASDGESEG 490 500 510 520 530 540 KRGRQKPKAA PEGAGALAQG SSLEPGRPAA PSLPGEAEPG AHAPDKEPEL GGQEEGERDG 550 560 570 580 590 600 LCGLGNGCAD RKEAETESQN SELSGVTAGE SLDQSMEEEE EEDTDEDDHL IYLEEILVRV 610 620 630 640 650 660 HTDYYAKYDR YLNKEIEEAP DIRKIVPELK SKVLADVAII FSGLHPTNFP IEKTREHYHA 670 680 690 700 710 720 TALGAKILTR LVLSPDAPDR ATHLIAARAG TEKVLQAQEC GHLHVVNPDW LWSCLERWDK 730 740 750 760 770 780 VEEQLFPLRD DHTKAQRENS PAAFPDREGV PPTALFHPMP VLPKAQPGPE VRIYDSNTGK 790 800 810 820 830 840 LIRTGARGPP APSSSLPIRQ EPSSFRWTTS LEKAATTATA RRGGLRSRRR SPSPGSQGPA 850 860 GSGRSGHLRP ARGARQGAGG PEATRGS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO." Archambault J., Pan G., Dahmus G.K., Cartier M., Marshall N., Zhang S., Dahmus M.E., Greenblatt J. J. Biol. Chem. 273:27593-27601(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY, INTERACTION WITH GTF2F1. Tissue: Placenta.
[2]	"A protein phosphatase functions to recycle RNA polymerase II." Cho H., Kim T.-K., Mancebo H., Lane W.S., Flores O., Reinberg D. Genes Dev. 13:1540-1552(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Cervix carcinoma.
[3]	"DNA sequence and analysis of human chromosome 18." Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S. Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases 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: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 88-961 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 303-961 (ISOFORM 3/4). Tissue: Colon, Lymph and Ovary.
[6]	"The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNP." Licciardo P., Amente S., Ruggiero L., Monti M., Pucci P., Lania L., Majello B. Nucleic Acids Res. 31:999-1005(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WDR77; SNRPB AND SNRNP70.
[7]	"The C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylation." Friedl E.M., Lane W.S., Erdjument-Bromage H., Tempst P., Reinberg D. Proc. Natl. Acad. Sci. U.S.A. 100:2328-2333(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[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-869, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-780, MASS SPECTROMETRY.
[11]	"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-674; SER-869 AND SER-872, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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].
[13]	"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-872, MASS SPECTROMETRY.
[14]	"Fcp1-dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit." Visconti R., Palazzo L., Della Monica R., Grieco D. Nat. Commun. 3:894-894(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]	"Molecular mechanism of recruitment of TFIIF-associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF." Kamada K., Roeder R.G., Burley S.K. Proc. Natl. Acad. Sci. U.S.A. 100:2296-2299(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 944-961 IN COMPLEX WITH GTF2F1.
[16]	"Partial deficiency of the C-terminal-domain phosphatase of RNA polymerase II is associated with congenital cataracts facial dysmorphism neuropathy syndrome." Varon R., Gooding R., Steglich C., Marns L., Tang H., Angelicheva D., Yong K.K., Ambrugger P., Reinhold A., Morar B., Baas F., Kwa M., Tournev I., Guerguelcheva V., Kremensky I., Lochmueller H., Muellner-Eidenboeck A., Merlini L. , Neumann L., Buerger J., Walter M., Swoboda K., Thomas P.K., von Moers A., Risch N., Kalaydjieva L. Nat. Genet. 35:185-189(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CCFDN.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF081287 mRNA. Translation: AAC64549.1.
AF154115 mRNA. Translation: AAD42088.1.
AC021594 Genomic DNA. No translation available.
AC068473 Genomic DNA. No translation available.
CH471117 Genomic DNA. Translation: EAW66631.1.
BC015010 mRNA. Translation: AAH15010.1.
BC052576 mRNA. Translation: AAH52576.1.
BC063447 mRNA. Translation: AAH63447.1.

IPI

IPI00410256.
IPI00410257.
IPI00410258.
IPI01008810.

RefSeq

NP_001189433.1. NM_001202504.1.
NP_004706.3. NM_004715.4.
NP_430255.2. NM_048368.3.

UniGene

Hs.465490.
Hs.734021.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J2X	X-ray	2.00	B	944-961	[»]
1ONV	NMR	-	B	879-961	[»]
2K7L	NMR	-	B	582-600	[»]

DisProt

DP00177.

ProteinModelPortal

Q9Y5B0.

SMR

Q9Y5B0. Positions 168-344, 585-728.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41788N.

IntAct

Q9Y5B0. 2 interactions.

MINT

MINT-275991.

STRING

9606.ENSP00000299543.

PTM databases

PhosphoSite

Q9Y5B0.

Polymorphism databases

DMDM

46396052.

Proteomic databases

PaxDb

Q9Y5B0.

PRIDE

Q9Y5B0.

Protocols and materials databases

DNASU

9150.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000075430; ENSP00000075430; ENSG00000060069.
ENST00000299543; ENSP00000299543; ENSG00000060069.

GeneID

9150.

KEGG

hsa:9150.

UCSC

uc002lnh.2. human.
uc002lni.2. human.

Organism-specific databases

CTD

9150.

GeneCards

GC18P077494.

HGNC

HGNC:2498. CTDP1.

HPA

CAB032641.
HPA040394.

MIM

604168. phenotype.
604927. gene.

neXtProt

NX_Q9Y5B0.

Orphanet

48431. Congenital cataracts - facial dysmorphism - neuropathy.

PharmGKB

PA27001.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5190.

HOGENOM

HOG000112039.

HOVERGEN

HBG051213.

InParanoid

Q9Y5B0.

KO

K15732.

OMA

EAPDIRK.

OrthoDB

EOG4HMJ8T.

PhylomeDB

Q9Y5B0.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_71. Gene Expression.

Gene expression databases

Bgee

Q9Y5B0.

CleanEx

HS_CTDP1.

Genevestigator

Q9Y5B0.

GermOnline

ENSG00000060069. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.1000. 2 hits.

InterPro

IPR001357. BRCT_dom.
IPR015388. FCP1_C.
IPR011947. FCP1_euk.
IPR023214. HAD-like_dom.
IPR004274. NIF.
[Graphical view]

Pfam

PF09309. FCP1_C. 1 hit.
PF03031. NIF. 1 hit.
[Graphical view]

SMART

SM00292. BRCT. 1 hit.
SM00577. CPDc. 1 hit.
[Graphical view]

SUPFAM

SSF52113. BRCT. 1 hit.
SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR02250. FCP1_euk. 1 hit.

PROSITE

PS50172. BRCT. 1 hit.
PS50969. FCP1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CTDP1. human.

EvolutionaryTrace

Q9Y5B0.

GenomeRNAi

9150.

NextBio

34327.

SOURCE

Search...

Entry information

Entry name

CTDP1_HUMAN

Accession

Primary (citable) accession number: Q9Y5B0
Secondary accession number(s): A8MY97 , Q7Z644, Q96BZ1, Q9Y6F5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	April 5, 2011
Last modified:	May 1, 2013
This is version 123 of the entry and version 3 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.