Q9BQ52 (RNZ2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zinc phosphodiesterase ELAC protein 2
EC=3.1.26.11

Alternative name(s):
ElaC homolog protein 2
Heredity prostate cancer protein 2
Ribonuclease Z 2
Short name=RNase Z 2
tRNA 3 endonuclease 2
tRNase Z 2

Gene names

Name:	ELAC2
Synonyms:	HPC2

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

General annotation (Comments)

Function	Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Catalytic activity	Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule. Ref.6
Cofactor	Zinc Probable.
Subunit structure	Homodimer By similarity. Interacts with PTCD1. Ref.9
Subcellular location	Nucleus Probable.
Tissue specificity	Widely expressed. Highly expressed in heart, placenta, liver, skeletal muscle, kidney, pancreas, testis and ovary. Weakly expressed in brain, lung, spleen, thymus, prostate, small intestine, colon and leukocytes. Ref.1
Involvement in disease	Prostate cancer, hereditary, 2 (HPC2) [MIM:614731]: A condition associated with familial predisposition to cancer of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.3 Ref.5 Ref.6 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17
Sequence similarities	Belongs to the RNase Z family.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Proto-oncogene
Ligand	Metal-binding Zinc
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC tRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrion Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	endonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PUF60	Q9UHX1	1	EBI-718223,EBI-1053259

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BQ52-1)

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: Q9BQ52-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: Missing.
     554-595: GLPSILLQRE...AWLQQYHNQC → VSVGLDHKAG...CPELLLLISG
     596-826: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9BQ52-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-372: Missing.
     373-406: NCASVHNLRSHKIQTQLNLIHPDIFPLLTSFRCK → MRTVPQFTTFAATRFKPSSTSSTRTSSPCSPVSA

Note: No experimental confirmation available.

Isoform 4 (identifier: Q9BQ52-4)

The sequence of this isoform differs from the canonical sequence as follows:
     188-227: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 826	826	Zinc phosphodiesterase ELAC protein 2		PRO_0000155828
Amino acid modifications
	Modified residue	199	1	Phosphoserine Ref.7
	Modified residue	208	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 372	372	Missing in isoform 3.		VSP_009168
	Alternative sequence	1 – 94	94	Missing in isoform 2.		VSP_009169
	Alternative sequence	188 – 227	40	Missing in isoform 4.		VSP_043449
	Alternative sequence	373 – 406	34	NCASV…SFRCK → MRTVPQFTTFAATRFKPSST SSTRTSSPCSPVSA in isoform 3.		VSP_009170
	Alternative sequence	554 – 595	42	GLPSI…YHNQC → VSVGLDHKAGAWRRHCHVEL ALWLRLFLRFQTCPELLLLI SG in isoform 2.		VSP_009171
	Alternative sequence	596 – 826	231	Missing in isoform 2.		VSP_009172
	Natural variant	52	1	S → F. Corresponds to variant rs9895963 [ dbSNP | Ensembl ].		VAR_038210
	Natural variant	211	1	R → Q in HPC2. Ref.13		VAR_017425
	Natural variant	217	1	S → L in HPC2; does not affect the enzymatic activity. Ref.1 Ref.3 Ref.5 Ref.6 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Corresponds to variant rs4792311 [ dbSNP | Ensembl ].		VAR_017426
	Natural variant	436	1	D → N. Corresponds to variant rs3760317 [ dbSNP | Ensembl ].		VAR_038211
	Natural variant	487	1	G → R in HPC2. Ref.13		VAR_017427
	Natural variant	541	1	A → T in HPC2; does not affect the enzymatic activity. Ref.1 Ref.6 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Corresponds to variant rs34152967 [ dbSNP | Ensembl ].		VAR_017428
	Natural variant	622	1	E → V in HPC2; higher frequency in prostate cancer cases. Ref.12		VAR_017429
	Natural variant	627	1	S → L. Ref.16		VAR_017430
	Natural variant	781	1	R → H in HPC2; does not affect the enzymatic activity. Ref.1 Ref.6		VAR_017431
	Natural variant	806	1	G → R in HPC2. Ref.13		VAR_017432
Experimental info
	Sequence conflict	165	1	V → M in AK001392. Ref.2
	Sequence conflict	406	1	Missing in AK001392. Ref.2
	Sequence conflict	592	1	H → Y in AK001392. Ref.2
	Sequence conflict	754	1	F → L in AK001392. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 16, 2004. Version 2. Checksum: 4AE701C755EC7339	FASTA	826	92,219
	10 20 30 40 50 60 MWALCSLLRS AAGRTMSQGR TISQAPARRE RPRKDPLRHL RTREKRGPSG CSGGPNTVYL 70 80 90 100 110 120 QVVAAGSRDS GAALYVFSEF NRYLFNCGEG VQRLMQEHKL KVARLDNIFL TRMHWSNVGG 130 140 150 160 170 180 LSGMILTLKE TGLPKCVLSG PPQLEKYLEA IKIFSGPLKG IELAVRPHSA PEYEDETMTV 190 200 210 220 230 240 YQIPIHSEQR RGKHQPWQSP ERPLSRLSPE RSSDSESNEN EPHLPHGVSQ RRGVRDSSLV 250 260 270 280 290 300 VAFICKLHLK RGNFLVLKAK EMGLPVGTAA IAPIIAAVKD GKSITHEGRE ILAEELCTPP 310 320 330 340 350 360 DPGAAFVVVE CPDESFIQPI CENATFQRYQ GKADAPVALV VHMAPASVLV DSRYQQWMER 370 380 390 400 410 420 FGPDTQHLVL NENCASVHNL RSHKIQTQLN LIHPDIFPLL TSFRCKKEGP TLSVPMVQGE 430 440 450 460 470 480 CLLKYQLRPR REWQRDAIIT CNPEEFIVEA LQLPNFQQSV QEYRRSAQDG PAPAEKRSQY 490 500 510 520 530 540 PEIIFLGTGS AIPMKIRNVS ATLVNISPDT SLLLDCGEGT FGQLCRHYGD QVDRVLGTLA 550 560 570 580 590 600 AVFVSHLHAD HHTGLPSILL QRERALASLG KPLHPLLVVA PNQLKAWLQQ YHNQCQEVLH 610 620 630 640 650 660 HISMIPAKCL QEGAEISSPA VERLISSLLR TCDLEEFQTC LVRHCKHAFG CALVHTSGWK 670 680 690 700 710 720 VVYSGDTMPC EALVRMGKDA TLLIHEATLE DGLEEEAVEK THSTTSQAIS VGMRMNAEFI 730 740 750 760 770 780 MLNHFSQRYA KVPLFSPNFS EKVGVAFDHM KVCFGDFPTM PKLIPPLKAL FAGDIEEMEE 790 800 810 820 RREKRELRQV RAALLSRELA GGLEDGEPQQ KRAHTEEPQA KKVRAQ
	Isoform 2 [UniParc]. Checksum: C1C61F066EE55707	FASTA	501	56,095
	10 20 30 40 50 60 MQEHKLKVAR LDNIFLTRMH WSNVGGLSGM ILTLKETGLP KCVLSGPPQL EKYLEAIKIF 70 80 90 100 110 120 SGPLKGIELA VRPHSAPEYE DETMTVYQIP IHSEQRRGKH QPWQSPERPL SRLSPERSSD 130 140 150 160 170 180 SESNENEPHL PHGVSQRRGV RDSSLVVAFI CKLHLKRGNF LVLKAKEMGL PVGTAAIAPI 190 200 210 220 230 240 IAAVKDGKSI THEGREILAE ELCTPPDPGA AFVVVECPDE SFIQPICENA TFQRYQGKAD 250 260 270 280 290 300 APVALVVHMA PASVLVDSRY QQWMERFGPD TQHLVLNENC ASVHNLRSHK IQTQLNLIHP 310 320 330 340 350 360 DIFPLLTSFR CKKEGPTLSV PMVQGECLLK YQLRPRREWQ RDAIITCNPE EFIVEALQLP 370 380 390 400 410 420 NFQQSVQEYR RSAQDGPAPA EKRSQYPEII FLGTGSAIPM KIRNVSATLV NISPDTSLLL 430 440 450 460 470 480 DCGEGTFGQL CRHYGDQVDR VLGTLAAVFV SHLHADHHTV SVGLDHKAGA WRRHCHVELA 490 500 LWLRLFLRFQ TCPELLLLIS G
	Isoform 3 [UniParc]. Checksum: 8A85498B4B0BFDED	FASTA	454	50,615
	10 20 30 40 50 60 MRTVPQFTTF AATRFKPSST SSTRTSSPCS PVSAKEGPTL SVPMVQGECL LKYQLRPRRE 70 80 90 100 110 120 WQRDAIITCN PEEFIVEALQ LPNFQQSVQE YRRSAQDGPA PAEKRSQYPE IIFLGTGSAI 130 140 150 160 170 180 PMKIRNVSAT LVNISPDTSL LLDCGEGTFG QLCRHYGDQV DRVLGTLAAV FVSHLHADHH 190 200 210 220 230 240 TGLPSILLQR ERALASLGKP LHPLLVVAPN QLKAWLQQYH NQCQEVLHHI SMIPAKCLQE 250 260 270 280 290 300 GAEISSPAVE RLISSLLRTC DLEEFQTCLV RHCKHAFGCA LVHTSGWKVV YSGDTMPCEA 310 320 330 340 350 360 LVRMGKDATL LIHEATLEDG LEEEAVEKTH STTSQAISVG MRMNAEFIML NHFSQRYAKV 370 380 390 400 410 420 PLFSPNFSEK VGVAFDHMKV CFGDFPTMPK LIPPLKALFA GDIEEMEERR EKRELRQVRA 430 440 450 ALLSRELAGG LEDGEPQQKR AHTEEPQAKK VRAQ
	Isoform 4 [UniParc]. Checksum: 783F20F15CB91BAC	FASTA	786	87,564
	10 20 30 40 50 60 MWALCSLLRS AAGRTMSQGR TISQAPARRE RPRKDPLRHL RTREKRGPSG CSGGPNTVYL 70 80 90 100 110 120 QVVAAGSRDS GAALYVFSEF NRYLFNCGEG VQRLMQEHKL KVARLDNIFL TRMHWSNVGG 130 140 150 160 170 180 LSGMILTLKE TGLPKCVLSG PPQLEKYLEA IKIFSGPLKG IELAVRPHSA PEYEDETMTV 190 200 210 220 230 240 YQIPIHSVSQ RRGVRDSSLV VAFICKLHLK RGNFLVLKAK EMGLPVGTAA IAPIIAAVKD 250 260 270 280 290 300 GKSITHEGRE ILAEELCTPP DPGAAFVVVE CPDESFIQPI CENATFQRYQ GKADAPVALV 310 320 330 340 350 360 VHMAPASVLV DSRYQQWMER FGPDTQHLVL NENCASVHNL RSHKIQTQLN LIHPDIFPLL 370 380 390 400 410 420 TSFRCKKEGP TLSVPMVQGE CLLKYQLRPR REWQRDAIIT CNPEEFIVEA LQLPNFQQSV 430 440 450 460 470 480 QEYRRSAQDG PAPAEKRSQY PEIIFLGTGS AIPMKIRNVS ATLVNISPDT SLLLDCGEGT 490 500 510 520 530 540 FGQLCRHYGD QVDRVLGTLA AVFVSHLHAD HHTGLPSILL QRERALASLG KPLHPLLVVA 550 560 570 580 590 600 PNQLKAWLQQ YHNQCQEVLH HISMIPAKCL QEGAEISSPA VERLISSLLR TCDLEEFQTC 610 620 630 640 650 660 LVRHCKHAFG CALVHTSGWK VVYSGDTMPC EALVRMGKDA TLLIHEATLE DGLEEEAVEK 670 680 690 700 710 720 THSTTSQAIS VGMRMNAEFI MLNHFSQRYA KVPLFSPNFS EKVGVAFDHM KVCFGDFPTM 730 740 750 760 770 780 PKLIPPLKAL FAGDIEEMEE RREKRELRQV RAALLSRELA GGLEDGEPQQ KRAHTEEPQA KKVRAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A candidate prostate cancer susceptibility gene at chromosome 17p." Tavtigian S.V., Simard J., Teng D.H.F., Abtin V., Baumgard M., Beck A., Camp N.J., Carillo A.R., Chen Y., Dayananth P., Desrochers M., Dumont M., Farnham J.M., Frank D., Frye C., Ghaffari S., Gupte J.S., Hu R. , Iliev D., Janecki T., Kort E.N., Laity K.E., Leavitt A., Leblanc G., McArthur-Morrison J., Pederson A., Penn B., Peterson K.T., Reid J.E., Richards S., Schroeder M., Smith R., Snyder S.C., Swedlund B., Swensen J., Thomas A., Tranchant M., Woodland A.-M., Labrie F., Skolnick M.H., Neuhausen S., Rommens J., Cannon-Albright L.A. Nat. Genet. 27:172-180(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS HPC2 LEU-217; THR-541 AND HIS-781.
[2]	"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 1; 2; 3 AND 4). Tissue: Hippocampus, Liver, Teratocarcinoma and Thalamus.
[3]	"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 1), VARIANT HPC2 LEU-217.
[4]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(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] (ISOFORM 1), VARIANT HPC2 LEU-217. Tissue: Lung.
[6]	"A candidate prostate cancer susceptibility gene encodes tRNA 3' processing endoribonuclease." Takaku H., Minagawa A., Takagi M., Nashimoto M. Nucleic Acids Res. 31:2272-2278(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME ACTIVITY, CHARACTERIZATION OF VARIANTS HPC2 LEU-217; THR-541 AND HIS-781.
[7]	"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-199, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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].
[9]	"RNA processing in human mitochondria." Sanchez M.I., Mercer T.R., Davies S.M., Shearwood A.M., Nygard K.K., Richman T.R., Mattick J.S., Rackham O., Filipovska A. Cell Cycle 10:2904-2916(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTCD1.
[10]	"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].
[11]	"Association of HPC2/ELAC2 genotypes and prostate cancer." Rebbeck T.R., Walker A.H., Zeigler-Johnson C., Weisburg S., Martin A.-M., Nathanson K.L., Wein A.J., Malkowicz S.B. Am. J. Hum. Genet. 67:1014-1019(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HPC2 LEU-217 AND THR-541.
[12]	"ELAC2/HPC2 involvement in hereditary and sporadic prostate cancer." Roekman A., Ikonen T., Mononen N., Autio V., Matikainen M.P., Koivisto P.A., Tammela T.L.J., Kallioniemi O.-P., Schleutker J. Cancer Res. 61:6038-6041(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HPC2 VAL-622.
[13]	"Role of HPC2/ELAC2 in hereditary prostate cancer." Wang L., McDonnell S.K., Elkins D.A., Slager S.L., Christensen E., Marks A.F., Cunningham J.M., Peterson B.J., Jacobsen S.J., Cerhan J.R., Blute M.L., Schaid D.J., Thibodeau S.N. Cancer Res. 61:6494-6499(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HPC2 GLN-211; LEU-217; ARG-487; THR-541 AND ARG-806.
[14]	"Association of common missense changes in ELAC2 (HPC2) with prostate cancer in a Japanese case-control series." Fujiwara H., Emi M., Nagai H., Nishimura T., Konishi N., Kubota Y., Ichikawa T., Takahashi S., Shuin T., Habuchi T., Ogawa O., Inoue K., Skolnick M.H., Swensen J., Camp N.J., Tavtigian S.V. J. Hum. Genet. 47:641-648(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HPC2 LEU-217 AND THR-541.
[15]	"Meta-analysis of associations of the Ser217Leu and Ala541Thr variants in ELAC2 (HPC2) and prostate cancer." Camp N.J., Tavtigian S.V. Am. J. Hum. Genet. 71:1475-1478(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HPC2 LEU-217 AND THR-541.
[16]	"Ser217Leu polymorphism of the HPC2/ELAC2 gene associated with prostatic cancer risk in Japanese men." Takahashi H., Lu W., Watanabe M., Katoh T., Furusato M., Tsukino H., Nakao H., Sudo A., Suzuki H., Akakura K., Ikemoto I., Asano K., Ito T., Wakui S., Muto T., Hano H. Int. J. Cancer 107:224-228(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LEU-627.
[17]	"ELAC2/HPC2 polymorphisms, prostate-specific antigen levels, and prostate cancer." Severi G., Giles G.G., Southey M.C., Tesoriero A., Tilley W., Neufing P., Morris H., English D.R., McCredie M.R., Boyle P., Hopper J.L. J. Natl. Cancer Inst. 95:818-824(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HPC2 LEU-217 AND THR-541.
[18]	"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome." Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K. Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] HPC2 LEU-217.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF304369 Genomic DNA. Translation: AAG24440.1. AF304370 mRNA. Translation: AAG24441.1. AK001392 mRNA. No translation available. AK124838 mRNA. Translation: BAC85964.1. AK125030 mRNA. Translation: BAC86026.1. AK298397 mRNA. Translation: BAG60631.1. CR457261 mRNA. Translation: CAG33542.1. AC005277 Genomic DNA. No translation available. BC001939 mRNA. Translation: AAH01939.1. BC004158 mRNA. Translation: AAH04158.1.
IPI	IPI00396627. IPI00398822. IPI00398823. IPI00789842.
RefSeq	NP_001159434.1. NM_001165962.1. NP_060597.4. NM_018127.6. NP_776065.1. NM_173717.1.
UniGene	Hs.434232.
3D structure databases
ProteinModelPortal	Q9BQ52.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BQ52. 4 interactions.
MINT	MINT-1401619.
STRING	9606.ENSP00000337445.
PTM databases
PhosphoSite	Q9BQ52.
Polymorphism databases
DMDM	41017788.
Proteomic databases
PaxDb	Q9BQ52.
PRIDE	Q9BQ52.
Protocols and materials databases
DNASU	60528.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000338034; ENSP00000337445; ENSG00000006744. ENST00000426905; ENSP00000405223; ENSG00000006744.
GeneID	60528.
KEGG	hsa:60528.
UCSC	uc002gnv.4. human. uc002gnz.4. human.
Organism-specific databases
CTD	60528.
GeneCards	GC17M012836.
HGNC	HGNC:14198. ELAC2.
HPA	HPA019535.
MIM	176807. phenotype. 605367. gene. 614731. phenotype.
neXtProt	NX_Q9BQ52.
Orphanet	1331. Familial prostate cancer.
PharmGKB	PA27739.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1234.
HOGENOM	HOG000007499.
HOVERGEN	HBG050042.
InParanoid	Q9BQ52.
KO	K00784.
OMA	RAHTEEP.
OrthoDB	EOG4FTW05.
Enzyme and pathway databases
BRENDA	3.1.26.11. 2681.
Gene expression databases
ArrayExpress	Q9BQ52.
Bgee	Q9BQ52.
CleanEx	HS_ELAC2.
Genevestigator	Q9BQ52.
GermOnline	ENSG00000006744. Homo sapiens.
Family and domain databases
InterPro	IPR001279. Beta-lactamas-like. [Graphical view]
SMART	SM00849. Lactamase_B. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ELAC2. human.
GenomeRNAi	60528.
NextBio	65429.
SOURCE	Search...

Entry information

Entry name

RNZ2_HUMAN

Accession

Primary (citable) accession number: Q9BQ52
Secondary accession number(s): B4DPL9 , Q6IA94, Q9HAS8, Q9HAS9, Q9NVT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	January 16, 2004
Last modified:	May 1, 2013
This is version 109 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.