Q13352 (CENPR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Beta-3-endonexin
Integrin beta-3-binding protein
Nuclear receptor-interacting factor 3

Gene names

Name:	ITGB3BP
Synonyms:	CENPR, NRIF3

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

General annotation (Comments)

Function	Transcription coregulator that can have both coactivator and corepressor functions. Isoform 1, but not other isoforms, is involved in the coactivation of nuclear receptors for retinoid X (RXRs) and thyroid hormone (TRs) in a ligand-dependent fashion. In contrast, it does not coactivate nuclear receptors for retinoic acid, vitamin D, progesterone receptor, nor glucocorticoid. Acts as a coactivator for estrogen receptor alpha. Acts as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit, possibly by interfering with the transactivation domain of NFKB1. Induces apoptosis in breast cancer cells, but not in other cancer cells, via a caspase-2 mediated pathway that involves mitochondrial membrane permeabilization but does not require other caspases. May also act as an inhibitor of cyclin A-associated kinase. Also acts a component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Ref.2 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Subunit structure	Homodimer; mediated by the coiled coil domain. Isoform 3, but not other isoforms, interacts with the cytoplasmic tail of integrin ITGB3. The relevance of the interaction with ITGB3 is however uncertain, since isoform 3 is mainly nuclear. Interacts with CCNA2 and MTA1. Interacts with NFKB1 NF-kappa-B subunit. Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex interacts with the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and MLF1IP/CENPU. Ref.1 Ref.2 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14
Subcellular location	Isoform 1: Nucleus Ref.2 Ref.6 Ref.7 Ref.9 Ref.10 Ref.13. Chromosome › centromere. Chromosome › centromere › kinetochore Ref.2 Ref.6 Ref.7 Ref.9 Ref.10 Ref.13. Isoform 2: Nucleus Ref.2 Ref.6 Ref.7 Ref.9 Ref.10 Ref.13. Isoform 3: Nucleus Ref.2 Ref.6 Ref.7 Ref.9 Ref.10 Ref.13. Cytoplasm Ref.2 Ref.6 Ref.7 Ref.9 Ref.10 Ref.13. Note: Isoform 3 is predominantly nuclear and weakly cytoplasmic. Ref.2 Ref.6 Ref.7 Ref.9 Ref.10 Ref.13 Isoform 4: Cytoplasm Ref.2 Ref.6 Ref.7 Ref.9 Ref.10 Ref.13.
Tissue specificity	Widely expressed. Expressed in spleen, thymus, prostate, ovary, small intestine and white blood cells. Highly expressed in testis and colon. Isoform 4 is expressed in platelets, lymphocytes and granulocytes. Ref.1 Ref.6
Induction	By estrogen. Ref.12
Domain	The DD1 domain (also called RepD1 domain) mediates the corepressor function and is essential in the triggering of apoptosis. Ref.11 Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, a motif known to be important for the association with nuclear receptors. Such motif, which is required for an efficient association with nuclear receptors, is however not essential. Ref.11 Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, which is essential for the association with nuclear receptors. Ref.11
Sequence caution	The sequence AAH14385.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle Cell division Mitosis Transcription Transcription regulation
Cellular component	Centromere Chromosome Cytoplasm Kinetochore Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Molecular function	Activator 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 apoptotic process Traceable author statement. Source: Reactome cell adhesion Traceable author statement Ref.1. Source: ProtInc cell division Inferred from electronic annotation. Source: UniProtKB-KW mitotic prometaphase Traceable author statement. Source: Reactome nerve growth factor receptor signaling pathway 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
Cellular_component	condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome membrane Traceable author statement Ref.1. Source: ProtInc nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	protein C-terminus binding Traceable author statement Ref.2. Source: ProtInc signal transducer activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13352-1)

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: Q13352-2)

Also known as: Long; EnL; En-L;

The sequence of this isoform differs from the canonical sequence as follows:
     162-177: ASRHLDSYEFLKAILN → GQPQMSQPL

Isoform 3 (identifier: Q13352-3)

Also known as: Short; EnS; En-S;

The sequence of this isoform differs from the canonical sequence as follows:
     112-177: Missing.

Isoform 4 (identifier: Q13352-4)

The sequence of this isoform differs from the canonical sequence as follows:
     63-177: Missing.

Isoform 5 (identifier: Q13352-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MP → MPFAPVAQAGVQWHDFRSLQHLLPAFKRFSCLSLGSSWDYS

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 177	177	Centromere protein R		PRO_0000057949
Regions
	Region	20 – 50	31	DD1
	Coiled coil	83 – 113	31	Potential
	Motif	9 – 13	5	LXXLL motif
	Motif	63 – 66	4	Nuclear localization signal
	Motif	172 – 176	5	LXXIL motif
Amino acid modifications
	Modified residue	17	1	Phosphoserine Ref.15 Ref.16
	Modified residue	28	1	Phosphoserine Probable
	Modified residue	71	1	Phosphoserine Ref.16
Natural variations
	Alternative sequence	1 – 2	2	MP → MPFAPVAQAGVQWHDFRSLQ HLLPAFKRFSCLSLGSSWDY S in isoform 5.		VSP_010831
	Alternative sequence	63 – 177	115	Missing in isoform 4.		VSP_010832
	Alternative sequence	112 – 177	66	Missing in isoform 3.		VSP_010833
	Alternative sequence	162 – 177	16	ASRHL…KAILN → GQPQMSQPL in isoform 2.		VSP_010834
	Natural variant	30	1	I → V. Corresponds to variant rs1058057 [ dbSNP | Ensembl ].		VAR_048691
Experimental info
	Mutagenesis	9	1	L → A: Decreased interaction with nuclear receptors. Ref.2
	Mutagenesis	28	1	S → A: Loss of repressor function. Ref.9 Ref.11
	Mutagenesis	63 – 66	4	Missing: Abolishes localization to nucleus. Ref.10
	Mutagenesis	63 – 65	3	KRK → AAA: Abolishes localization to nucleus. Ref.6
	Mutagenesis	89	1	L → R: Abolishes dimerization, but not interactions with nuclear receptors; when associated with R-96. Ref.9
	Mutagenesis	96	1	L → R: Abolishes dimerization, but not interactions with nuclear receptors; when associated with R-89. Ref.9
	Mutagenesis	172 – 176	5	LKAIL → AKAAA: Abolishes interaction with nuclear receptors. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 19, 2004. Version 2. Checksum: C0A6FD5A56E98D43	FASTA	177	20,194
	10 20 30 40 50 60 MPVKRSLKLD GLLEENSFDP SKITRKKSVI TYSPTTGTCQ MSLFASPTSS EEQKHRNGLS 70 80 90 100 110 120 NEKRKKLNHP SLTESKESTT KDNDEFMMLL SKVEKLSEEI MEIMQNLSSI QALEGSRELE 130 140 150 160 170 NLIGISCASH FLKREMQKTK ELMTKVNKQK LFEKSTGLPH KASRHLDSYE FLKAILN
	Isoform 2 (Long) (EnL) (En-L) [UniParc]. Checksum: 227EE95365D0AB5C	FASTA	170	19,302
	10 20 30 40 50 60 MPVKRSLKLD GLLEENSFDP SKITRKKSVI TYSPTTGTCQ MSLFASPTSS EEQKHRNGLS 70 80 90 100 110 120 NEKRKKLNHP SLTESKESTT KDNDEFMMLL SKVEKLSEEI MEIMQNLSSI QALEGSRELE 130 140 150 160 170 NLIGISCASH FLKREMQKTK ELMTKVNKQK LFEKSTGLPH KGQPQMSQPL
	Isoform 3 (Short) (EnS) (En-S) [UniParc]. Checksum: 790E4D07D5CC09AF	FASTA	111	12,624
	10 20 30 40 50 60 MPVKRSLKLD GLLEENSFDP SKITRKKSVI TYSPTTGTCQ MSLFASPTSS EEQKHRNGLS 70 80 90 100 110 NEKRKKLNHP SLTESKESTT KDNDEFMMLL SKVEKLSEEI MEIMQNLSSI Q
	Isoform 4 [UniParc]. Checksum: DB8074B62E359160	FASTA	62	6,902
	10 20 30 40 50 60 MPVKRSLKLD GLLEENSFDP SKITRKKSVI TYSPTTGTCQ MSLFASPTSS EEQKHRNGLS NE
	Isoform 5 [UniParc]. Checksum: E6E7B64BF3FBD654	FASTA	216	24,630
	10 20 30 40 50 60 MPFAPVAQAG VQWHDFRSLQ HLLPAFKRFS CLSLGSSWDY SVKRSLKLDG LLEENSFDPS 70 80 90 100 110 120 KITRKKSVIT YSPTTGTCQM SLFASPTSSE EQKHRNGLSN EKRKKLNHPS LTESKESTTK 130 140 150 160 170 180 DNDEFMMLLS KVEKLSEEIM EIMQNLSSIQ ALEGSRELEN LIGISCASHF LKREMQKTKE 190 200 210 LMTKVNKQKL FEKSTGLPHK ASRHLDSYEF LKAILN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Beta 3-endonexin, a novel polypeptide that interacts specifically with the cytoplasmic tail of the integrin beta 3 subunit." Shattil S.J., O'Toole T.E., Eigenthaler M.J., Thon V., Williams M.J., Babior B.M., Ginsberg M.H. J. Cell Biol. 131:807-816(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY, INTERACTION WITH ITGB3. Tissue: B-cell.
[2]	"NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors." Li D., Desai-Yajnik V., Lo E., Schapira M., Abagyan R., Samuels H.H. Mol. Cell. Biol. 19:7191-7202(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), COACTIVATOR FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RXRA AND THRA, MUTAGENESIS OF LEU-9 AND 172-LEU--LEU-176. Tissue: Cervix carcinoma.
[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 1). Tissue: Testis.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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 5). Tissue: Bone marrow and Placenta.
[6]	"Novel alternatively spliced form of beta(3)-endonexin." Fujimoto T.-T., Katsutani S., Shimomura T., Fujimura K. Thromb. Res. 105:63-70(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORM 4), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF 63-LYS--LYS-65.
[7]	"Affinity modulation of platelet integrin alphaIIbbeta3 by beta3-endonexin, a selective binding partner of the beta3 integrin cytoplasmic tail." Kashiwagi H., Schwartz M.A., Eigenthaler M., Davis K.A., Ginsberg M.H., Shattil S.J. J. Cell Biol. 137:1433-1443(1997) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[8]	"Beta3-endonexin as a novel inhibitor of cyclin A-associated kinase." Ohtoshi A., Maeda T., Higashi H., Ashizawa S., Yamada M., Hatakeyama M. Biochem. Biophys. Res. Commun. 267:947-952(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CCNA2.
[9]	"Domain structure of the NRIF3 family of coregulators suggests potential dual roles in transcriptional regulation." Li D., Wang F., Samuels H.H. Mol. Cell. Biol. 21:8371-8384(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A COREPRESSOR, SUBCELLULAR LOCATION, HOMODIMERIZATION, PHOSPHORYLATION, MUTAGENESIS OF SER-28; LEU-89 AND LEU-96.
[10]	"Role of beta(3)-endonexin in the regulation of NF-kappaB-dependent expression of urokinase-type plasminogen activator receptor." Besta F., Massberg S., Brand K., Mueller E., Page S., Gruener S., Lorenz M., Sadoul K., Kolanus W., Lengyel E., Gawaz M. J. Cell Sci. 115:3879-3888(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A COREPRESSOR, SUBCELLULAR LOCATION, INTERACTION WITH NFKB1, MUTAGENESIS OF 63-LYS--LYS-66.
[11]	"The NRIF3 family of transcriptional coregulators induces rapid and profound apoptosis in breast cancer cells." Li D., Das S., Yamada T., Samuels H.H. Mol. Cell. Biol. 24:3838-3848(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DOMAIN, MUTAGENESIS OF SER-28.
[12]	"Metastasis-associated protein 1 interacts with NRIF3, an estrogen-inducible nuclear receptor coregulator." Talukder A.H., Gururaj A., Mishra S.K., Vadlamudi R.K., Kumar R. Mol. Cell. Biol. 24:6581-6591(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION, INTERACTION WITH MTA1.
[13]	"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 BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH CENPH; CENPI; CENPK; CENPN; CENPO; CENPP; CENPQ AND CENPU, FUNCTION, SUBCELLULAR LOCATION.
[14]	"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 BY MASS SPECTROMETRY, IDENTIFICATION IN THE CENPA-CAD COMPLEX WITH CENPI; CENPK; CENPL; CENPO; CENPP; CENPQ AND CENPS.
[15]	"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 SER-17, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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-17 AND SER-71, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U37139 mRNA. Translation: AAC50295.1. U37139 mRNA. Translation: AAC50294.1. AF175306 mRNA. Translation: AAF00239.1. AK312944 mRNA. Translation: BAG35785.1. BX004807, AL592218 Genomic DNA. Translation: CAI15771.1. BX004807, AL592218 Genomic DNA. Translation: CAI15772.1. AL592218, BX004807 Genomic DNA. Translation: CAI18958.1. AL592218, BX004807 Genomic DNA. Translation: CAI18959.1. BC009929 mRNA. Translation: AAH09929.1. BC014385 mRNA. Translation: AAH14385.1. Different initiation.
IPI	IPI00439184. IPI00439185. IPI00439186. IPI00439187. IPI00555934.
PIR	A57277.
RefSeq	NP_001193668.1. NM_001206739.1. NP_055103.3. NM_014288.4.
UniGene	Hs.166539.
3D structure databases
ProteinModelPortal	Q13352.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13352. 28 interactions.
MINT	MINT-1378371.
PTM databases
PhosphoSite	Q13352.
Polymorphism databases
DMDM	50400855.
Proteomic databases
PaxDb	Q13352.
PRIDE	Q13352.
Protocols and materials databases
DNASU	23421.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000271002; ENSP00000271002; ENSG00000142856. ENST00000283568; ENSP00000283568; ENSG00000142856. ENST00000371092; ENSP00000360133; ENSG00000142856. ENST00000489099; ENSP00000432904; ENSG00000142856.
GeneID	23421.
KEGG	hsa:23421.
UCSC	uc001dba.2. human. uc001dbb.2. human. uc009wak.1. human.
Organism-specific databases
CTD	23421.
GeneCards	GC01M063906.
H-InvDB	HIX0019635.
HGNC	HGNC:6157. ITGB3BP.
HPA	HPA028463.
MIM	605494. gene.
neXtProt	NX_Q13352.
PharmGKB	PA29956.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG80433.
HOVERGEN	HBG080553.
KO	K11510.
OrthoDB	EOG4Z36G0.
PhylomeDB	Q13352.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases.
Gene expression databases
ArrayExpress	Q13352.
Bgee	Q13352.
Genevestigator	Q13352.
GermOnline	ENSG00000142856. Homo sapiens.
Family and domain databases
InterPro	IPR009601. NRIF3_coact_rcpt. [Graphical view]
PANTHER	PTHR15581. PTHR15581. 1 hit.
Pfam	PF06729. NRIF3. 1 hit. [Graphical view]
PIRSF	PIRSF011860. NRIF3_coact_rcpt. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	ITGB3BP. human.
GenomeRNAi	23421.
NextBio	45639.
SOURCE	Search...

Entry information

Entry name

CENPR_HUMAN

Accession

Primary (citable) accession number: Q13352
Secondary accession number(s): B2R7D8 , Q13353, Q5RJ42, Q5RJ44, Q5RJ45, Q7KYX2, Q96CD5, Q9UKB6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 19, 2004
Last modified:	April 3, 2013
This is version 98 of the entry and version 2 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.