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Q9Y5K3 (PCY1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Choline-phosphate cytidylyltransferase B

EC=2.7.7.15
Alternative name(s):
CCT-beta
CTP:phosphocholine cytidylyltransferase B
Short name=CCT B
Short name=CT B
Phosphorylcholine transferase B
Gene names
Name:PCYT1B
Synonyms:CCTB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Controls phosphatidylcholine synthesis.

Catalytic activity

CTP + phosphocholine = diphosphate + CDP-choline.

Pathway

Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 1/2.

Subcellular location

Endoplasmic reticulum.

Tissue specificity

Highly expressed in testis, placenta, brain, ovary and fetus.

Post-translational modification

Extensively phosphorylated. The beta-1 isoform seemsto be much less phosphorylated.

Sequence similarities

Belongs to the cytidylyltransferase family.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: Q9Y5K3-1)

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 1 (identifier: Q9Y5K3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     321-369: VSSPTRSRSPSRSPSPTFSWLPLKTSPPSSPKAASASISSMSEGDEDEK → LKSWARCRDF
Isoform 3 (identifier: Q9Y5K3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.
     17-39: SLSNEPPSETMEEIEHTCPQPRL → MVGNQECIMEEDNRAPQLWRK
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9Y5K3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: MPVVTTDAESETGIPKSLSNEPPSETMEEIEHTCPQPRL → MVGHQECIMEEDNRAPQLWRK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369Choline-phosphate cytidylyltransferase B
PRO_0000208456

Regions

Nucleotide binding84 – 929CTP By similarity
Nucleotide binding168 – 1692CTP By similarity
Nucleotide binding196 – 2005CTP By similarity

Sites

Binding site1221CTP By similarity
Binding site1221Substrate By similarity
Binding site1511Substrate By similarity
Binding site1731CTP By similarity

Amino acid modifications

Modified residue3151Phosphoserine Ref.8
Modified residue3191Phosphoserine Ref.8
Modified residue3621Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 3939MPVVT…PQPRL → MVGHQECIMEEDNRAPQLWR K in isoform 4.
VSP_044659
Alternative sequence1 – 1616Missing in isoform 3.
VSP_020045
Alternative sequence17 – 3923SLSNE…PQPRL → MVGNQECIMEEDNRAPQLWR K in isoform 3.
VSP_020046
Alternative sequence321 – 36949VSSPT…DEDEK → LKSWARCRDF in isoform 1.
VSP_001226

Experimental info

Sequence conflict1541T → S in BAG59022. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 87A00617DF690DD1

FASTA36941,940
        10         20         30         40         50         60 
MPVVTTDAES ETGIPKSLSN EPPSETMEEI EHTCPQPRLT LTAPAPFADE TNCQCQAPHE 

        70         80         90        100        110        120 
KLTIAQARLG TPADRPVRVY ADGIFDLFHS GHARALMQAK TLFPNSYLLV GVCSDDLTHK 

       130        140        150        160        170        180 
FKGFTVMNEA ERYEALRHCR YVDEVIRDAP WTLTPEFLEK HKIDFVAHDD IPYSSAGSDD 

       190        200        210        220        230        240 
VYKHIKEAGM FVPTQRTEGI STSDIITRIV RDYDVYARRN LQRGYTAKEL NVSFINEKRY 

       250        260        270        280        290        300 
RFQNQVDKMK EKVKNVEERS KEFVNRVEEK SHDLIQKWEE KSREFIGNFL ELFGPDGAWK 

       310        320        330        340        350        360 
QMFQERSSRM LQALSPKQSP VSSPTRSRSP SRSPSPTFSW LPLKTSPPSS PKAASASISS 


MSEGDEDEK 

« Hide

Isoform 1 [UniParc].

Checksum: C1A16BC1B61906B2
Show »

FASTA33038,086
Isoform 3 [UniParc].

Checksum: 0E2BBEDD2569EAA8
Show »

FASTA35140,206
Isoform 4 [UniParc].

Checksum: 89BA4A3D7F09B353
Show »

FASTA35140,229

References

« Hide 'large scale' references
[1]"Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase."
Lykidis A., Murti K.G., Jackowski S.
J. Biol. Chem. 273:14022-14029(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTbeta splice variant."
Lykidis A., Baburina I., Jackowski S.
J. Biol. Chem. 274:26992-27001(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHARACTERIZATION.
[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. expand/collapse author list , 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] (ISOFORMS 2 AND 4).
Tissue: Hippocampus and Thalamus.
[4]SeattleSNPs variation discovery resource
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"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. expand/collapse author list , 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].
[6]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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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 3).
Tissue: Brain.
[8]"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-315; SER-319 AND SER-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF052510 mRNA. Translation: AAC39754.1.
AF148464 mRNA. Translation: AAD35088.1.
AK296333 mRNA. Translation: BAG59022.1.
AK315323 mRNA. Translation: BAG37725.1.
EU181262 Genomic DNA. Translation: ABW03924.1.
AC079168 Genomic DNA. No translation available.
CH471074 Genomic DNA. Translation: EAW99021.1.
BC045634 mRNA. Translation: AAH45634.2.
CCDSCCDS14213.1. [Q9Y5K3-1]
CCDS55391.1. [Q9Y5K3-2]
CCDS55392.1. [Q9Y5K3-4]
RefSeqNP_001156736.1. NM_001163264.1. [Q9Y5K3-4]
NP_001156737.1. NM_001163265.1. [Q9Y5K3-2]
NP_004836.2. NM_004845.4. [Q9Y5K3-1]
UniGeneHs.660708.

3D structure databases

ProteinModelPortalQ9Y5K3.
SMRQ9Y5K3. Positions 41-295.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114854. 7 interactions.
MINTMINT-5006746.
STRING9606.ENSP00000368439.

Chemistry

DrugBankDB00122. Choline.

PTM databases

PhosphoSiteQ9Y5K3.

Polymorphism databases

DMDM12643330.

Proteomic databases

MaxQBQ9Y5K3.
PaxDbQ9Y5K3.
PRIDEQ9Y5K3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356768; ENSP00000349211; ENSG00000102230. [Q9Y5K3-2]
ENST00000379144; ENSP00000368439; ENSG00000102230. [Q9Y5K3-1]
ENST00000379145; ENSP00000368440; ENSG00000102230. [Q9Y5K3-4]
GeneID9468.
KEGGhsa:9468.
UCSCuc004dbi.3. human. [Q9Y5K3-1]
uc004dbk.4. human. [Q9Y5K3-2]

Organism-specific databases

CTD9468.
GeneCardsGC0XM024576.
HGNCHGNC:8755. PCYT1B.
HPAHPA006367.
MIM604926. gene.
neXtProtNX_Q9Y5K3.
PharmGKBPA33100.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0615.
HOGENOMHOG000230945.
HOVERGENHBG053531.
InParanoidQ9Y5K3.
KOK00968.
OMALEHTCPH.
OrthoDBEOG7X9G6S.
PhylomeDBQ9Y5K3.
TreeFamTF106336.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00753; UER00739.

Gene expression databases

ArrayExpressQ9Y5K3.
BgeeQ9Y5K3.
CleanExHS_PCYT1B.
GenevestigatorQ9Y5K3.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
InterProIPR004821. Cyt_trans-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00125. cyt_tran_rel. 1 hit.
ProtoNetSearch...

Other

GeneWikiPCYT1B.
GenomeRNAi9468.
NextBio35472668.
PROQ9Y5K3.
SOURCESearch...

Entry information

Entry namePCY1B_HUMAN
AccessionPrimary (citable) accession number: Q9Y5K3
Secondary accession number(s): A8IX00 expand/collapse secondary AC list , B2RCX8, B4DK10, E9PD84, O60621, Q86XC9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM