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Protein

Choline-phosphate cytidylyltransferase B

Gene

PCYT1B

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

Functioni

Controls phosphatidylcholine synthesis.

Catalytic activityi

CTP + phosphocholine = diphosphate + CDP-choline.

Pathway:iphosphatidylcholine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes phosphatidylcholine from phosphocholine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Choline-phosphate cytidylyltransferase A (PCYT1A), Choline-phosphate cytidylyltransferase B (PCYT1B)
  2. Cholinephosphotransferase 1 (CHPT1), Choline/ethanolaminephosphotransferase 1 (CEPT1)
This subpathway is part of the pathway phosphatidylcholine biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphatidylcholine from phosphocholine, the pathway phosphatidylcholine biosynthesis and in Phospholipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei122 – 1221CTPBy similarity
Binding sitei122 – 1221SubstrateBy similarity
Binding sitei151 – 1511SubstrateBy similarity
Binding sitei173 – 1731CTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi84 – 929CTPBy similarity
Nucleotide bindingi168 – 1692CTPBy similarity
Nucleotide bindingi196 – 2005CTPBy similarity

GO - Molecular functioni

  • choline-phosphate cytidylyltransferase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiREACT_121238. Synthesis of PC.
UniPathwayiUPA00753; UER00739.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PCYT1B
Synonyms:CCTB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:8755. PCYT1B.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • endoplasmic reticulum membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33100.

Chemistry

DrugBankiDB00122. Choline.

Polymorphism and mutation databases

BioMutaiPCYT1B.
DMDMi12643330.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 369369Choline-phosphate cytidylyltransferase BPRO_0000208456Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei315 – 3151Phosphoserine1 Publication
Modified residuei319 – 3191Phosphoserine1 Publication
Modified residuei322 – 3221PhosphoserineBy similarity
Modified residuei323 – 3231PhosphoserineBy similarity
Modified residuei329 – 3291PhosphoserineBy similarity
Modified residuei331 – 3311PhosphoserineBy similarity
Modified residuei346 – 3461PhosphoserineBy similarity
Modified residuei349 – 3491PhosphoserineBy similarity
Modified residuei350 – 3501PhosphoserineBy similarity
Modified residuei355 – 3551PhosphoserineBy similarity
Modified residuei362 – 3621Phosphoserine1 Publication

Post-translational modificationi

Extensively phosphorylated. The beta-1 isoform seems to be much less phosphorylated.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y5K3.
PaxDbiQ9Y5K3.
PRIDEiQ9Y5K3.

PTM databases

PhosphoSiteiQ9Y5K3.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9Y5K3.
CleanExiHS_PCYT1B.
ExpressionAtlasiQ9Y5K3. baseline and differential.
GenevisibleiQ9Y5K3. HS.

Organism-specific databases

HPAiHPA006367.

Interactioni

Protein-protein interaction databases

BioGridi114854. 6 interactions.
MINTiMINT-5006746.
STRINGi9606.ENSP00000368439.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5K3.
SMRiQ9Y5K3. Positions 41-295.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytidylyltransferase family.Curated

Phylogenomic databases

eggNOGiCOG0615.
GeneTreeiENSGT00390000000269.
HOGENOMiHOG000230945.
HOVERGENiHBG053531.
InParanoidiQ9Y5K3.
KOiK00968.
OMAiNQVDRMK.
OrthoDBiEOG7X9G6S.
PhylomeDBiQ9Y5K3.
TreeFamiTF106336.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR004821. Cyt_trans-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: Q9Y5K3-1) [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
MPVVTTDAES ETGIPKSLSN EPPSETMEEI EHTCPQPRLT LTAPAPFADE
60 70 80 90 100
TNCQCQAPHE KLTIAQARLG TPADRPVRVY ADGIFDLFHS GHARALMQAK
110 120 130 140 150
TLFPNSYLLV GVCSDDLTHK FKGFTVMNEA ERYEALRHCR YVDEVIRDAP
160 170 180 190 200
WTLTPEFLEK HKIDFVAHDD IPYSSAGSDD VYKHIKEAGM FVPTQRTEGI
210 220 230 240 250
STSDIITRIV RDYDVYARRN LQRGYTAKEL NVSFINEKRY RFQNQVDKMK
260 270 280 290 300
EKVKNVEERS KEFVNRVEEK SHDLIQKWEE KSREFIGNFL ELFGPDGAWK
310 320 330 340 350
QMFQERSSRM LQALSPKQSP VSSPTRSRSP SRSPSPTFSW LPLKTSPPSS
360
PKAASASISS MSEGDEDEK
Length:369
Mass (Da):41,940
Last modified:November 1, 1999 - v1
Checksum:i87A00617DF690DD1
GO
Isoform 1 (identifier: Q9Y5K3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     321-369: VSSPTRSRSPSRSPSPTFSWLPLKTSPPSSPKAASASISSMSEGDEDEK → LKSWARCRDF

Show »
Length:330
Mass (Da):38,086
Checksum:iC1A16BC1B61906B2
GO
Isoform 3 (identifier: Q9Y5K3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.
     17-39: SLSNEPPSETMEEIEHTCPQPRL → MVGNQECIMEEDNRAPQLWRK

Note: No experimental confirmation available.
Show »
Length:351
Mass (Da):40,206
Checksum:i0E2BBEDD2569EAA8
GO
Isoform 4 (identifier: Q9Y5K3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: MPVVTTDAESETGIPKSLSNEPPSETMEEIEHTCPQPRL → MVGHQECIMEEDNRAPQLWRK

Note: No experimental confirmation available.
Show »
Length:351
Mass (Da):40,229
Checksum:i89BA4A3D7F09B353
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541T → S in BAG59022 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3939MPVVT…PQPRL → MVGHQECIMEEDNRAPQLWR K in isoform 4. 1 PublicationVSP_044659Add
BLAST
Alternative sequencei1 – 1616Missing in isoform 3. 1 PublicationVSP_020045Add
BLAST
Alternative sequencei17 – 3923SLSNE…PQPRL → MVGNQECIMEEDNRAPQLWR K in isoform 3. 1 PublicationVSP_020046Add
BLAST
Alternative sequencei321 – 36949VSSPT…DEDEK → LKSWARCRDF in isoform 1. 1 PublicationVSP_001226Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14213.1. [Q9Y5K3-1]
CCDS55391.1. [Q9Y5K3-2]
CCDS55392.1. [Q9Y5K3-4]
RefSeqiNP_001156736.1. NM_001163264.1. [Q9Y5K3-4]
NP_001156737.1. NM_001163265.1. [Q9Y5K3-2]
NP_004836.2. NM_004845.4. [Q9Y5K3-1]
UniGeneiHs.660708.

Genome annotation databases

EnsembliENST00000356768; ENSP00000349211; ENSG00000102230. [Q9Y5K3-2]
ENST00000379144; ENSP00000368439; ENSG00000102230.
ENST00000379145; ENSP00000368440; ENSG00000102230. [Q9Y5K3-4]
GeneIDi9468.
KEGGihsa:9468.
UCSCiuc004dbi.3. human. [Q9Y5K3-1]
uc004dbk.4. human. [Q9Y5K3-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14213.1. [Q9Y5K3-1]
CCDS55391.1. [Q9Y5K3-2]
CCDS55392.1. [Q9Y5K3-4]
RefSeqiNP_001156736.1. NM_001163264.1. [Q9Y5K3-4]
NP_001156737.1. NM_001163265.1. [Q9Y5K3-2]
NP_004836.2. NM_004845.4. [Q9Y5K3-1]
UniGeneiHs.660708.

3D structure databases

ProteinModelPortaliQ9Y5K3.
SMRiQ9Y5K3. Positions 41-295.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114854. 6 interactions.
MINTiMINT-5006746.
STRINGi9606.ENSP00000368439.

Chemistry

DrugBankiDB00122. Choline.

PTM databases

PhosphoSiteiQ9Y5K3.

Polymorphism and mutation databases

BioMutaiPCYT1B.
DMDMi12643330.

Proteomic databases

MaxQBiQ9Y5K3.
PaxDbiQ9Y5K3.
PRIDEiQ9Y5K3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356768; ENSP00000349211; ENSG00000102230. [Q9Y5K3-2]
ENST00000379144; ENSP00000368439; ENSG00000102230.
ENST00000379145; ENSP00000368440; ENSG00000102230. [Q9Y5K3-4]
GeneIDi9468.
KEGGihsa:9468.
UCSCiuc004dbi.3. human. [Q9Y5K3-1]
uc004dbk.4. human. [Q9Y5K3-2]

Organism-specific databases

CTDi9468.
GeneCardsiGC0XM024576.
HGNCiHGNC:8755. PCYT1B.
HPAiHPA006367.
MIMi300948. gene.
neXtProtiNX_Q9Y5K3.
PharmGKBiPA33100.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0615.
GeneTreeiENSGT00390000000269.
HOGENOMiHOG000230945.
HOVERGENiHBG053531.
InParanoidiQ9Y5K3.
KOiK00968.
OMAiNQVDRMK.
OrthoDBiEOG7X9G6S.
PhylomeDBiQ9Y5K3.
TreeFamiTF106336.

Enzyme and pathway databases

UniPathwayiUPA00753; UER00739.
ReactomeiREACT_121238. Synthesis of PC.

Miscellaneous databases

ChiTaRSiPCYT1B. human.
GeneWikiiPCYT1B.
GenomeRNAii9468.
NextBioi35472668.
PROiQ9Y5K3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y5K3.
CleanExiHS_PCYT1B.
ExpressionAtlasiQ9Y5K3. baseline and differential.
GenevisibleiQ9Y5K3. HS.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR004821. Cyt_trans-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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].

Entry informationi

Entry nameiPCY1B_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5K3
Secondary accession number(s): A8IX00
, B2RCX8, B4DK10, E9PD84, O60621, Q86XC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 1, 1999
Last modified: July 22, 2015
This is version 127 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.