CPLM-017722

Genbank Nucleotide ID

Protein Synonyms/Alias

ALL1-fused gene from chromosome 15q14 protein; AF15q14; Bub-linking kinetochore protein; Blinkin; Cancer susceptibility candidate gene 5 protein; Cancer/testis antigen 29; CT29; Kinetochore-null protein 1; Protein D40/AF15q14

Homo sapiens (Human)

Position	Peptide	Type	References
124	LLLIQNKKLEDNYCE	ubiquitination	[1, 2]
150	IHTQMQQKEFSIIEH	ubiquitination	[1]
199	LDNPISEKSTKIDTT	ubiquitination	[1, 2, 3, 4]
202	PISEKSTKIDTTSFL	ubiquitination	[1, 2, 3, 4]
213	TSFLANLKLHTEDSR	ubiquitination	[1, 2, 3, 4, 5]
223	TEDSRMKKEVNFSVD	ubiquitination	[2]
238	QNTSSENKIDFNDFI	ubiquitination	[1, 2]
246	IDFNDFIKRLKTGKC	ubiquitination	[1, 2]
252	IKRLKTGKCSAFPDV	ubiquitination	[1, 2]
262	AFPDVPDKENFEIPI	ubiquitination	[1, 2, 3]
288	HQMHVSLKEDENNSN	ubiquitination	[2, 3]
303	ITRLFREKDDGMNFT	ubiquitination	[1, 2]
393	NKTVFKSKQNTAFQD	ubiquitination	[1, 2, 3, 6]
408	LSINSADKIHITRSH	ubiquitination	[1]
467	NDAMEMTKCLSNMRE	ubiquitination	[1, 2]
476	LSNMREEKNLLKHDS	ubiquitination	[1]
480	REEKNLLKHDSNYAK	ubiquitination	[1]
487	KHDSNYAKMYCNPDA	ubiquitination	[1, 2]
501	AMSSLTEKTIYSGEE	ubiquitination	[1, 2]
514	EENMDITKSHTVAID	ubiquitination	[2]
526	AIDNQIFKQDQSNVQ	ubiquitination	[2]
570	NSVPHVSKERIQQSL	ubiquitination	[1, 2]
643	DECEEITKSRNEPFQ	ubiquitination	[1, 2, 4]
657	QRSDIIAKNSLTDTW	ubiquitination	[1, 2, 3, 6]
666	SLTDTWNKDKDWVLK	ubiquitination	[1, 2, 3]
668	TDTWNKDKDWVLKIL	ubiquitination	[1, 2]
673	KDKDWVLKILPYLDK	ubiquitination	[3]
680	KILPYLDKDSPQSAD	ubiquitination	[1, 2]
707	YCGGVLDKQITNRNT	ubiquitination	[1, 2]
726	QSLFSTTKPLFSSGQ	ubiquitination	[1, 2]
749	AISSHTVKSVLGQNS	ubiquitination	[1, 2]
757	SVLGQNSKLAEPLRK	ubiquitination	[1, 2]
764	KLAEPLRKSLSNPTP	ubiquitination	[1, 2, 4]
777	TPDYCHDKMIICSEE	ubiquitination	[1, 2]
810	SELQELGKTNLEHTT	ubiquitination	[1, 2]
830	MNRQIAVKVEKCGKS	acetylation	[2, 7]
841	CGKSPIEKSGVLKSN	ubiquitination	[1, 2]
846	IEKSGVLKSNCIMDV	ubiquitination	[1, 2]
861	LEDESVQKPKFPKEK	ubiquitination	[1, 2]
863	DESVQKPKFPKEKQN	ubiquitination	[1, 2]
872	PKEKQNVKIWGRKSV	ubiquitination	[1]
883	RKSVGGPKIDKTIVF	ubiquitination	[1, 2]
886	VGGPKIDKTIVFSED	ubiquitination	[1, 2]
895	IVFSEDDKNDMDITK	ubiquitination	[1, 2]
916	NHRPLLEKRDCHLVP	ubiquitination	[1, 2]
953	HTTALECKTVSPDEI	ubiquitination	[1, 2, 5]
1007	NFELSQRKSLGTPTV	ubiquitination	[1]
1064	ADNMELSKSATCKNI	ubiquitination	[1]
1069	LSKSATCKNIKDVQS	ubiquitination	[1]
1072	SATCKNIKDVQSPGF	ubiquitination	[1]
1087	LNEPLSSKSQRRKSL	ubiquitination	[1, 3]
1165	HTTALECKTLLPNEI	ubiquitination	[1]
1214	KILEENPKFGIGKGK	ubiquitination	[1, 3]
1219	NPKFGIGKGKNLGVS	ubiquitination	[1]
1221	KFGIGKGKNLGVSFP	ubiquitination	[1]
1229	NLGVSFPKDNSCVQE	ubiquitination	[1]
1240	CVQEIAEKQALAVGN	ubiquitination	[1, 4]
1256	IVLHTEQKQQLFAAT	ubiquitination	[1]
1272	RTTNEIIKFHSAAMD	ubiquitination	[1]
1281	HSAAMDEKVIGKVVD	ubiquitination	[1]
1285	MDEKVIGKVVDQACT	ubiquitination	[1]
1295	DQACTLEKAQVESCQ	ubiquitination	[1]
1393	APCPLLEKEEVIQTS	ubiquitination	[3]
1413	DCVITLHKDQDLIKD	ubiquitination	[1]
1419	HKDQDLIKDPRNLLA	ubiquitination	[1]
1441	QDLGEMTKLNSKRVS	ubiquitination	[1, 3]
1457	KLPKDQMKVYVDDIY	ubiquitination	[1]
1481	DQPPLPKKGQSSINK	ubiquitination	[1]
1488	KGQSSINKEEVILSK	ubiquitination	[1]
1495	KEEVILSKAGNKSLN	ubiquitination	[3]
1515	SAPICENKPKILNSE	ubiquitination	[1]
1517	PICENKPKILNSEEW	ubiquitination	[1]
1531	WFAAACKKELKENIQ	ubiquitination	[1]
1534	AACKKELKENIQTTN	ubiquitination	[1]
1584	VPCFHSIKPNLNNLN	ubiquitination	[1]
1718	ETQPVSSKDSGIGSV	ubiquitination	[1]
1770	ALIETYQKEISPYEN	ubiquitination	[1]
1830	HTEEDIDKSANSVLI	ubiquitination	[1]
1855	SSSLDSIKADGTSLD	ubiquitination	[1]
1976	KLLVDINKNLWEKMR	ubiquitination	[1]
1981	INKNLWEKMRHCSDK	ubiquitination	[1]
2083	SEMRAAEKELEQLKT	ubiquitination	[1]
2118	AQIDFMQKQRNRTEE	ubiquitination	[1]
2247	GEEIEYLKRWGPNYN	ubiquitination	[1, 3]

[1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[5] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[7] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]

Functional Description

Performs two crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Required for attachment of the kinetochores to the spindle microtubules. Directly links BUB1 and BUB1B to kinetochores. Part of the MIS12 complex, which may be fundamental for kinetochore formation and proper chromosome segregation during mitosis. Acts in coordination with CENPK to recruit the NDC80 complex to the outer kinetochore.

REPEAT 885 989 1.
REPEAT 1099 1201 2.
REGION 1 728 Interaction with BUB1 and BUB1B.
REGION 855 1201 2 X 104 AA approximate repeats.
REGION 1834 2316 Necessary for kinetochore localization
MOTIF 1789 1803 Nuclear localization signal (Potential).
MOD_RES 32 32 Phosphoserine.
MOD_RES 60 60 Phosphoserine.
MOD_RES 539 539 Phosphothreonine.
MOD_RES 956 956 Phosphoserine.
MOD_RES 1076 1076 Phosphoserine.
MOD_RES 1773 1773 Phosphoserine.
MOD_RES 1831 1831 Phosphoserine.
MOD_RES 1845 1845 Phosphoserine.

3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere; Chromosomal rearrangement; Chromosome; Chromosome partition; Coiled coil; Complete proteome; Disease mutation; Kinetochore; Mental retardation; Mitosis; Nucleus; Phosphoprotein; Polymorphism; Primary microcephaly; Reference proteome; Repeat.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO:0005829; C:cytosol; TAS:Reactome.
GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0001675; P:acrosome assembly; NAS:UniProtKB.
GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:UniProtKB.
GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO:0034080; P:CENP-A containing nucleosome assembly at centromere; TAS:Reactome.
GO:0007067; P:mitosis; IEA:UniProtKB-KW.
GO:0000278; P:mitotic cell cycle; TAS:Reactome.
GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
GO:0034501; P:protein localization to kinetochore; IDA:MGI.
GO:0071173; P:spindle assembly checkpoint; IDA:UniProtKB.