LipidDB-9606-00901

Lipid Modification Database

Tag

Content

LipidDB ID

LipidDB-9606-00901

Entry Name

CCNY_HUMAN

UniProt Accession

Q8ND76; B7ZKX9; D3DRY9; Q2M3V4; Q2TU96; Q6NT86; Q7Z4U7; Q8TEX2; Q8TEX3; Q96M99; Q96P45;

Theoretical PI

6.76

Molecular Weight

39336.65

Genbank Protein ID

AAS79427.1; AAP97301.1; AAL07802.1; AAL78998.1; AAL78999.1; BAB71409.1; CAD39020.2; CAH70072.1; CAH70072.1; CAH70072.1; CAH70073.1; CAH70073.1; CAH70073.1; CAH70073.1; CAH71567.1; CAH71567.1; CAH71567.1; CAH71568.1; CAH71568.1; CAH71568.1; CAH71568.1; CAH72501.1; CAH72501.1; CAH72501.1; CAH72501.1; CAH73707.1; CAH73707.1; CAH73707.1; CAH73709.1; CAH73709.1; CAH73709.1; CAH73709.1; EAW85912.1; EAW85913.1; EAW85914.1; AAH69224.1; AAH94815.1; AAI04774.1; AAI04802.1; AAI43451.1; AAI43456.1;

Genbank Nucleotide ID

AY504868; AF429969; AF413522; AF465728; AF465729; AK057280; AL834355; AL592445; AL121749; AL603824; AL592445; AL121749; AL603824; AL117336; AL603824; AL121749; AL592445; AL603824; AL121749; AL592445; AL117336; AL117336; AL121749; AL603824; AL592445; AL121749; AL603824; AL592445; AL121749; AL603824; AL592445; AL117336; CH471072; CH471072; CH471072; BC069224; BC094815; BC104773; BC104801; BC143450; BC143455;

Protein Name

Cyclin-Y

Protein Synonyms/Alias

Cyc-Y; Cyclin box protein 1; Cyclin fold protein 1; cyclin-X;

Gene Name

CCNY

Gene Synonyms/Alias

C10orf9; CBCP1; CFP1;

Created Date

02-AUG-2005

Lipid Modification Sites
Position	Sequence Form	Peptide	References	Modification Type
2	Canonical	******MGNTTSCCV	[2][3]	N-Myristoylation
7	Canonical	*MGNTTSCCVSSSPK	[1]	S-Palmitoylation
8	Canonical	MGNTTSCCVSSSPKL	[1]	S-Palmitoylation

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Reference

[1] Predicted from GPS-Lipid
[2] Davidson G, Shen J, Huang YL, Su Y, Karaulanov E, Bartscherer K, Hassler C,Stannek P, Boutros M, Niehrs C. Cell cycle control of wnt receptor activation.Dev Cell. 2009 Dec;17(6):788-99. doi: 10.1016/j.devcel.2009.11.006.[PMID:20059949]
[3] Jiang M, Gao Y, Yang T, Zhu X, Chen J. Cyclin Y, a novel membrane-associatedcyclin, interacts with PFTK1. FEBS Lett. 2009 Jul 7;583(13):2171-8. doi:10.1016/j.febslet.2009.06.010. Epub 2009 Jun 12.[PMID:19524571]

Functional Description

Positive regulatory subunit of the cyclin-dependent kinases CDK14/PFTK1 and CDK16. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by recruiting CDK14/PFTK1 to the plasma membrane and promoting phosphorylation of LRP6, leading to the activation of the Wnt signaling pathway. Recruits CDK16 to the plasma membrane. Isoform 3 might play a role in the activation of MYC-mediated transcription.

Sequence Annotation

Domain: 143 265 Cyclin N-terminal.
Modified residue: 25 25 Phosphoserine.
Modified residue: 30 30 Phosphothreonine.
Modified residue: 33 33 Phosphoserine.
Modified residue: 37 37 Phosphothreonine.
Modified residue: 67 67 Phosphothreonine; by CDK14.
Modified residue: 71 71 Phosphoserine; by CDK14.
Modified residue: 73 73 Phosphoserine; by CDK14.
Modified residue: 75 75 Phosphothreonine.
Modified residue: 83 83 Phosphoserine; by CDK14.
Modified residue: 99 99 Phosphoserine.
Modified residue: 100 100 Phosphoserine.
Modified residue: 102 102 Phosphoserine.
Modified residue: 288 288 Phosphoserine; by CDK14.
Modified residue: 295 295 Phosphoserine; by CDK14.
Modified residue: 324 324 Phosphoserine.
Modified residue: 326 326 Phosphoserine.

Protein Length

341 AA.

Protein Sequence
(Canonical)

MGNTTSCCVS SSPKLRRNAH SRLESYRPDT DLSREDTGCN LQHISDRENI DDLNMEFNPS  60
DHPRASTIFL SKSQTDVREK RKSLFINHHP PGQIARKYSS CSTIFLDDST VSQPNLKYTI  120
KCVALAIYYH IKNRDPDGRM LLDIFDENLH PLSKSEVPPD YDKHNPEQKQ IYRFVRTLFS  180
AAQLTAECAI VTLVYLERLL TYAEIDICPA NWKRIVLGAI LLASKVWDDQ AVWNVDYCQI  240
LKDITVEDMN ELERQFLELL QFNINVPSSV YAKYYFDLRS LAEANNLSFP LEPLSRERAH  300
KLEAISRLCE DKYKDLRRSA RKRSASADNL TLPRWSPAII S                      341
MGNTTSCCVS SSPKLRRNAH SRLESYRPDT DLSREDTGCN LQHISDRENI DDLNMEFNPS  60
DHPRASTIFL SKSQTDVREK RKSLFINHHP PGQIARKYSS CSTIFLDDST VSQPNLKYTI  120
KCVALAIYYH IKNRDPDGRM LLDIFDENLH PLSKSEVPPD YDKHNPEQKQ IYRFVRTLFS  180
AAQLTAECAI VTLVYLERLL TYAEIDICPA NWKRIVLGAI LLASKVWDDQ AVWNVDYCQI  240
LKDITVEDMN ELERQFLELL QFNINVPSSV YAKYYFDLRS LAEANNLSFP LEPLSRERAH  300
KLEAISRLCE DKYKDLRRSA RKRSASADNL TLPRWSPAII S                      341

FASTA
(Canonical)

>LipidDB-9606-00901|Q8ND76
MGNTTSCCVSSSPKLRRNAHSRLESYRPDTDLSREDTGCNLQHISDRENIDDLNMEFNPS
DHPRASTIFLSKSQTDVREKRKSLFINHHPPGQIARKYSSCSTIFLDDSTVSQPNLKYTI
KCVALAIYYHIKNRDPDGRMLLDIFDENLHPLSKSEVPPDYDKHNPEQKQIYRFVRTLFS
AAQLTAECAIVTLVYLERLLTYAEIDICPANWKRIVLGAILLASKVWDDQAVWNVDYCQI
LKDITVEDMNELERQFLELLQFNINVPSSVYAKYYFDLRSLAEANNLSFPLEPLSRERAH
KLEAISRLCEDKYKDLRRSARKRSASADNLTLPRWSPAIIS
MGNTTSCCVSSSPKLRRNAHSRLESYRPDTDLSREDTGCNLQHISDRENIDDLNMEFNPS
DHPRASTIFLSKSQTDVREKRKSLFINHHPPGQIARKYSSCSTIFLDDSTVSQPNLKYTI
KCVALAIYYHIKNRDPDGRMLLDIFDENLHPLSKSEVPPDYDKHNPEQKQIYRFVRTLFS
AAQLTAECAIVTLVYLERLLTYAEIDICPANWKRIVLGAILLASKVWDDQAVWNVDYCQI
LKDITVEDMNELERQFLELLQFNINVPSSVYAKYYFDLRSLAEANNLSFPLEPLSRERAH
KLEAISRLCEDKYKDLRRSARKRSASADNLTLPRWSPAIIS

Gene Ontology

GO:0000308; C:cytoplasmic cyclin-dependent protein kinase holoenzyme complex; IDA:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005634; C:nucleus; IDA:LIFEdb
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:UniProtKB
GO:0051301; P:cell division; IEA:UniProtKB-KW
GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB
GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB
GO:0060828; P:regulation of canonical Wnt signaling pathway; IDA:UniProtKB
GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW

Interpro

InterPro; IPR013763; Cyclin-like
InterPro; IPR006671; Cyclin_N
InterPro; IPR012399; Cyclin_Y

Pfam

Pfam; PF00134; Cyclin_N;

SMART

SMART; SM00385; CYCLIN;

PROSITE

PRINTS