Q71F23 (CENPU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Centromere protein U
Short name=CENP-U

Alternative name(s):
Interphase centromere complex protein 24
KSHV latent nuclear antigen-interacting protein 1
MLF1-interacting protein
Polo-box-interacting protein 1
centromere protein of 50 kDa
Short name=CENP-50

Gene names

Name:	MLF1IP
Synonyms:	CENPU, ICEN24, KLIP1, PBIP1

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

General annotation (Comments)

Function	Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Plays an important role in the correct PLK1 localization to the mitotic kinetochores. A scaffold protein responsible for the initial recruitment and maintenance of the kinetochore PLK1 population until its degradation. Involved in transcriptional repression. Ref.1 Ref.8 Ref.11
Subunit structure	Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and MLF1IP/CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Interacts with the N-terminal domain of Kaposi's sarcoma-associated herpesvirus latent nuclear antigen (LNA). Interacts with MLF1. Interacts with PLK1. Ref.1 Ref.2 Ref.9 Ref.10 Ref.11
Subcellular location	Cytoplasm. Nucleus. Chromosome › centromere › kinetochore. Note: Localizes in the kinetochore domain of centromeres. Colocalizes with PLK1 at the interzone between the inner and the outer kinetochore plates. Ref.1 Ref.2 Ref.7 Ref.8 Ref.11
Tissue specificity	Expressed at high levels in the testis, fetal liver, thymus, bone marrow and at lower levels in the lymph nodes, placenta, colon and spleen. Present in all cell lines examined, including B-cells, T-cells, epithelial cells and fibroblast cells. Expressed at high levels in glioblastoma cell lines. Ref.1 Ref.2 Ref.7
Post-translational modification	Phosphorylated by PLK1 at Thr-78, creating a self-tethering site that specifically interacts with the polo-box domain of PLK1. Ref.11

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Centromere Chromosome Cytoplasm Kinetochore Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	CENP-A containing nucleosome assembly at centromere Traceable author statement. Source: Reactome mitotic prometaphase Traceable author statement. Source: Reactome regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	centrosome Inferred from direct assay. Source: HPA condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q71F23-1)

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 2 (identifier: Q71F23-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-242: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 418	418	Centromere protein U		PRO_0000247672
Regions
	Coiled coil	297 – 356	60	Potential
	Coiled coil	397 – 417	21	Potential
	Motif	6 – 23	18	Nuclear localization signal Potential
	Motif	303 – 320	18	Nuclear localization signal Potential
Amino acid modifications
	Modified residue	78	1	Phosphothreonine; by PLK1 Ref.11
	Modified residue	110	1	Phosphothreonine Ref.12
	Modified residue	111	1	Phosphoserine Ref.12 Ref.13
	Modified residue	136	1	Phosphoserine Ref.12
	Modified residue	139	1	Phosphoserine Ref.12
	Modified residue	141	1	Phosphoserine Ref.12
	Modified residue	194	1	Phosphoserine Ref.14
Natural variations
	Alternative sequence	1 – 242	242	Missing in isoform 2.		VSP_020030
	Natural variant	16	1	G → R. Corresponds to variant rs902174 [ dbSNP | Ensembl ].		VAR_048692
	Natural variant	16	1	G → S. Corresponds to variant rs902174 [ dbSNP | Ensembl ].		VAR_027144
	Natural variant	157	1	I → T. Corresponds to variant rs6552804 [ dbSNP | Ensembl ].		VAR_027145
	Natural variant	214	1	I → M. Corresponds to variant rs4616798 [ dbSNP | Ensembl ].		VAR_027146
	Natural variant	279	1	A → T. Corresponds to variant rs34007339 [ dbSNP | Ensembl ].		VAR_048693
Experimental info
	Mutagenesis	77	1	S → A: Insensitive to PLK1-induced degradation. Ref.11
	Mutagenesis	78	1	T → A: Insensitive to PLK1-induced degradation. Ref.11
	Mutagenesis	78	1	T → D: Failed to enhance the PLK1-dependent degradation. Ref.11
	Mutagenesis	78	1	T → E: Failed to enhance the PLK1-dependent degradation. Ref.11
	Sequence conflict	163	1	E → G in AAI07745. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: A99BC012EF7188F9	FASTA	418	47,522
	10 20 30 40 50 60 MAPRGRRRPR PHRSEGARRS KNTLERTHSM KDKAGQKCKP IDVFDFPDNS DVSSIGRLGE 70 80 90 100 110 120 NEKDEETYET FDPPLHSTAI YADEEEFSKH CGLSLSSTPP GKEAKRSSDT SGNEASEIES 130 140 150 160 170 180 VKISAKKPGR KLRPISDDSE SIEESDTRRK VKSAEKISTQ RHEVIRTTAS SELSEKPAES 190 200 210 220 230 240 VTSKKTGPLS AQPSVEKENL AIESQSKTQK KGKISHDKRK KSRSKAIGSD TSDIVHIWCP 250 260 270 280 290 300 EGMKTSDIKE LNIVLPEFEK THLEHQQRIE SKVCKAAIAT FYVNVKEQFI KMLKESQMLT 310 320 330 340 350 360 NLKRKNAKMI SDIEKKRQRM IEVQDELLRL EPQLKQLQTK YDELKERKSS LRNAAYFLSN 370 380 390 400 410 LKQLYQDYSD VQAQEPNVKE TYDSSSLPAL LFKARTLLGA ESHLRNINHQ LEKLLDQG
	Isoform 2 [UniParc]. Checksum: C5731EE5F7ADCE1D	FASTA	176	20,710
	10 20 30 40 50 60 MKTSDIKELN IVLPEFEKTH LEHQQRIESK VCKAAIATFY VNVKEQFIKM LKESQMLTNL 70 80 90 100 110 120 KRKNAKMISD IEKKRQRMIE VQDELLRLEP QLKQLQTKYD ELKERKSSLR NAAYFLSNLK 130 140 150 160 170 QLYQDYSDVQ AQEPNVKETY DSSSLPALLF KARTLLGAES HLRNINHQLE KLLDQG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a novel cellular transcriptional repressor interacting with the latent nuclear antigen of Kaposi's sarcoma-associated herpesvirus." Pan H.-Y., Zhang Y.-J., Wang X.-P., Deng J.-H., Zhou F.-C., Gao S.-J. J. Virol. 77:9758-9768(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS LATENT NUCLEAR ANTIGEN.
[2]	"cDNA cloning and characterization of a novel gene encoding the MLF1-interacting protein MLF1IP." Hanissian S.H., Akbar U., Teng B., Janjetovic Z., Hoffmann A., Hitzler J.K., Iscove N., Hamre K., Du X., Tong Y., Mukatira S., Robertson J.H., Morris S.W. Oncogene 23:3700-3707(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH MLF1.
[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] (ISOFORM 2). Tissue: Small intestine.
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORMS 1 AND 2). Tissue: Adrenal cortex and Testis.
[7]	"Regulation of myeloid leukemia factor-1 interacting protein (MLF1IP) expression in glioblastoma." Hanissian S.H., Teng B., Akbar U., Janjetovic Z., Zhou Q., Duntsch C., Robertson J.H. Brain Res. 1047:56-64(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]	"Comprehensive analysis of the ICEN (Interphase Centromere Complex) components enriched in the CENP-A chromatin of human cells." Izuta H., Ikeno M., Suzuki N., Tomonaga T., Nozaki N., Obuse C., Kisu Y., Goshima N., Nomura F., Nomura N., Yoda K. Genes Cells 11:673-684(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]	"The CENP-H-I complex is required for the efficient incorporation of newly synthesized CENP-A into centromeres." Okada M., Cheeseman I.M., Hori T., Okawa K., McLeod I.X., Yates J.R. III, Desai A., Fukagawa T. Nat. Cell Biol. 8:446-457(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH CENPH; CENPI; CENPK; CENPN; CENPO; CENPP; CENPQ AND CENPR.
[10]	"The human CENP-A centromeric nucleosome-associated complex." Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III, Cleveland D.W. Nat. Cell Biol. 8:458-469(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE CENPA-NAC COMPLEX WITH CENPA; CENPC; CENPH; CENPM; CENPN AND CENPT.
[11]	"Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1 interaction is critical for proper chromosome segregation." Kang Y.H., Park J.-E., Yu L.-R., Soung N.-K., Yun S.-M., Bang J.K., Seong Y.-S., Yu H., Garfield S., Veenstra T.D., Lee K.S. Mol. Cell 24:409-422(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PLK1, PHOSPHORYLATION AT THR-78, MUTAGENESIS OF SER-77 AND THR-78.
[12]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110; SER-111; SER-136; SER-139 AND SER-141, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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-194, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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].
[16]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF469667 mRNA. Translation: AAQ05290.1. AF516710 mRNA. Translation: AAQ08228.1. AK027121 mRNA. Translation: BAB15665.1. CR457376 mRNA. Translation: CAG33657.1. CH471056 Genomic DNA. Translation: EAX04666.1. BC107744 mRNA. Translation: AAI07745.1. BC031520 mRNA. Translation: AAH31520.1. BC131556 mRNA. Translation: AAI31557.1.
IPI	IPI00002828. IPI00783686.
RefSeq	NP_078905.2. NM_024629.3.
UniGene	Hs.575032.
3D structure databases
ProteinModelPortal	Q71F23.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48539N.
IntAct	Q71F23. 2 interactions.
STRING	9606.ENSP00000281453.
PTM databases
PhosphoSite	Q71F23.
Polymorphism databases
DMDM	74712714.
Proteomic databases
PaxDb	Q71F23.
PRIDE	Q71F23.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000281453; ENSP00000281453; ENSG00000151725.
GeneID	79682.
KEGG	hsa:79682.
UCSC	uc003iwq.3. human.
Organism-specific databases
CTD	79682.
GeneCards	GC04M185615.
HGNC	HGNC:21348. MLF1IP.
HPA	HPA022048.
MIM	611511. gene.
neXtProt	NX_Q71F23.
PharmGKB	PA134893791.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG45595.
HOGENOM	HOG000236255.
HOVERGEN	HBG081090.
InParanoid	Q71F23.
KO	K11513.
OMA	TFDPPLH.
OrthoDB	EOG49W2FJ.
PhylomeDB	Q71F23.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases.
Gene expression databases
ArrayExpress	Q71F23.
Bgee	Q71F23.
CleanEx	HS_MLF1IP.
Genevestigator	Q71F23.
GermOnline	ENSG00000151725. Homo sapiens.
Family and domain databases
InterPro	IPR025214. NAC_CENP-U. [Graphical view]
Pfam	PF13097. CENP-U. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	79682.
NextBio	68934.
SOURCE	Search...

Entry information

Entry name

CENPU_HUMAN

Accession

Primary (citable) accession number: Q71F23
Secondary accession number(s): A2RRD9, Q32Q71, Q9H5G1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 78 of the entry and version 1 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.