P10155 (RO60_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
60 kDa SS-A/Ro ribonucleoprotein
Short name=60 kDa Ro protein
Short name=60 kDa ribonucleoprotein Ro
Short name=RoRNP

Alternative name(s):
Ro 60 kDa autoantigen
Sjoegren syndrome antigen A2
Sjoegren syndrome type A antigen
Short name=SS-A
TROVE domain family member 2

Gene names

Name:	TROVE2
Synonyms:	RO60, SSA2

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

General annotation (Comments)

Function	RNA-binding protein that binds to misfolded non-coding RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y RNAs. May stabilize some of these RNAs and protect them from degradation. Ref.12 May play roles in cilia formation and/or maintenance By similarity. Ref.12
Subunit structure	Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Found in a complex with PUF60 and Y5 RNA. Interacts with RIP11. Ref.10 Ref.11 Ref.13
Subcellular location	Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.13
Domain	The horseshoe-shaped TROVE domain is built with 7 helical HEAT-like repeats, and is closed by the VWFA-like domain giving rise to a ring-shaped monomer. Single-stranded RNA is bound in the positively charged central cavity By similarity. The MIDAS-like motif in the VWFA-like domain binds divalent metal cations By similarity.
Miscellaneous	Antibodies against normal cellular SSA2 protein are found in sera from patients with systemic lupus erythematosus (SLE).
Sequence similarities	Belongs to the Ro 60 kDa family. Contains 1 TROVE domain.

Ontologies

Keywords
Biological process	Cilium biogenesis/degradation
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Metal-binding RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cilium morphogenesis Inferred from electronic annotation. Source: Compara transcription from RNA polymerase III promoter Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA ribonucleoprotein complex Inferred from direct assay Ref.13. Source: UniProtKB
Molecular_function	RNA binding Traceable author statement Ref.1. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PUF60	Q9UHX1	1	EBI-1049168,EBI-1053259

Alternative products

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

Isoform Long (identifier: P10155-1)

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 Short (identifier: P10155-2)

Also known as: 60E2;

The sequence of this isoform differs from the canonical sequence as follows:
     195-205: LAIVTKYITKG → KHKIFIGKKGG
     206-538: Missing.

Isoform 3 (identifier: P10155-3)

The sequence of this isoform differs from the canonical sequence as follows:
     515-538: GMLDMCGFDTGALDVIRNFTLDMI → DTVK

Isoform 4 (identifier: P10155-4)

The sequence of this isoform differs from the canonical sequence as follows:
     529-538: VIRNFTLDMI → PCKIPY

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 538	538	60 kDa SS-A/Ro ribonucleoprotein		PRO_0000174169
Regions
	Domain	16 – 369	354	TROVE
	Region	120 – 284	165	RNA-binding By similarity
	Region	361 – 538	178	VWFA-like domain By similarity
Sites
	Metal binding	378	1	Divalent metal cation By similarity
	Metal binding	380	1	Divalent metal cation By similarity
	Metal binding	445	1	Divalent metal cation By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.9
	Modified residue	19	1	Phosphoserine Ref.15 Ref.16 Ref.18
	Modified residue	224	1	N6-acetyllysine Ref.17
	Modified residue	359	1	N6-acetyllysine Ref.17
Natural variations
	Alternative sequence	195 – 205	11	LAIVTKYITKG → KHKIFIGKKGG in isoform Short.		VSP_005911
	Alternative sequence	206 – 538	333	Missing in isoform Short.		VSP_005912
	Alternative sequence	515 – 538	24	GMLDM…TLDMI → DTVK in isoform 3.		VSP_045262
	Alternative sequence	529 – 538	10	VIRNFTLDMI → PCKIPY in isoform 4.		VSP_045797
Experimental info
	Sequence conflict	136	1	K → R in AAO47001. Ref.4
	Sequence conflict	136	1	K → R in AAO47002. Ref.4
	Sequence conflict	239	1	R → K in AAA35493. Ref.1
	Sequence conflict	515 – 538	24	GMLDM…TLDMI → ALQNTLLNKSF in AAB81552. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified September 27, 2004. Version 2. Checksum: CD735B1DF2B13098	FASTA	538	60,671
	10 20 30 40 50 60 MEESVNQMQP LNEKQIANSQ DGYVWQVTDM NRLHRFLCFG SEGGTYYIKE QKLGLENAEA 70 80 90 100 110 120 LIRLIEDGRG CEVIQEIKSF SQEGRTTKQE PMLFALAICS QCSDISTKQA AFKAVSEVCR 130 140 150 160 170 180 IPTHLFTFIQ FKKDLKESMK CGMWGRALRK AIADWYNEKG GMALALAVTK YKQRNGWSHK 190 200 210 220 230 240 DLLRLSHLKP SSEGLAIVTK YITKGWKEVH ELYKEKALSV ETEKLLKYLE AVEKVKRTRD 250 260 270 280 290 300 ELEVIHLIEE HRLVREHLLT NHLKSKEVWK ALLQEMPLTA LLRNLGKMTA NSVLEPGNSE 310 320 330 340 350 360 VSLVCEKLCN EKLLKKARIH PFHILIALET YKTGHGLRGK LKWRPDEEIL KALDAAFYKT 370 380 390 400 410 420 FKTVEPTGKR FLLAVDVSAS MNQRVLGSIL NASTVAAAMC MVVTRTEKDS YVVAFSDEMV 430 440 450 460 470 480 PCPVTTDMTL QQVLMAMSQI PAGGTDCSLP MIWAQKTNTP ADVFIVFTDN ETFAGGVHPA 490 500 510 520 530 IALREYRKKM DIPAKLIVCG MTSNGFTIAD PDDRGMLDMC GFDTGALDVI RNFTLDMI
	Isoform Short (60E2) [UniParc]. Checksum: 31CF4F9732BEB16E	FASTA	205	23,299
	10 20 30 40 50 60 MEESVNQMQP LNEKQIANSQ DGYVWQVTDM NRLHRFLCFG SEGGTYYIKE QKLGLENAEA 70 80 90 100 110 120 LIRLIEDGRG CEVIQEIKSF SQEGRTTKQE PMLFALAICS QCSDISTKQA AFKAVSEVCR 130 140 150 160 170 180 IPTHLFTFIQ FKKDLKESMK CGMWGRALRK AIADWYNEKG GMALALAVTK YKQRNGWSHK 190 200 DLLRLSHLKP SSEGKHKIFI GKKGG
	Isoform 3 [UniParc]. Checksum: D3CE550ADBB2761B	FASTA	518	58,483
	10 20 30 40 50 60 MEESVNQMQP LNEKQIANSQ DGYVWQVTDM NRLHRFLCFG SEGGTYYIKE QKLGLENAEA 70 80 90 100 110 120 LIRLIEDGRG CEVIQEIKSF SQEGRTTKQE PMLFALAICS QCSDISTKQA AFKAVSEVCR 130 140 150 160 170 180 IPTHLFTFIQ FKKDLKESMK CGMWGRALRK AIADWYNEKG GMALALAVTK YKQRNGWSHK 190 200 210 220 230 240 DLLRLSHLKP SSEGLAIVTK YITKGWKEVH ELYKEKALSV ETEKLLKYLE AVEKVKRTRD 250 260 270 280 290 300 ELEVIHLIEE HRLVREHLLT NHLKSKEVWK ALLQEMPLTA LLRNLGKMTA NSVLEPGNSE 310 320 330 340 350 360 VSLVCEKLCN EKLLKKARIH PFHILIALET YKTGHGLRGK LKWRPDEEIL KALDAAFYKT 370 380 390 400 410 420 FKTVEPTGKR FLLAVDVSAS MNQRVLGSIL NASTVAAAMC MVVTRTEKDS YVVAFSDEMV 430 440 450 460 470 480 PCPVTTDMTL QQVLMAMSQI PAGGTDCSLP MIWAQKTNTP ADVFIVFTDN ETFAGGVHPA 490 500 510 IALREYRKKM DIPAKLIVCG MTSNGFTIAD PDDRDTVK
	Isoform 4 [UniParc]. Checksum: 785F949FED553344	FASTA	534	60,169
	10 20 30 40 50 60 MEESVNQMQP LNEKQIANSQ DGYVWQVTDM NRLHRFLCFG SEGGTYYIKE QKLGLENAEA 70 80 90 100 110 120 LIRLIEDGRG CEVIQEIKSF SQEGRTTKQE PMLFALAICS QCSDISTKQA AFKAVSEVCR 130 140 150 160 170 180 IPTHLFTFIQ FKKDLKESMK CGMWGRALRK AIADWYNEKG GMALALAVTK YKQRNGWSHK 190 200 210 220 230 240 DLLRLSHLKP SSEGLAIVTK YITKGWKEVH ELYKEKALSV ETEKLLKYLE AVEKVKRTRD 250 260 270 280 290 300 ELEVIHLIEE HRLVREHLLT NHLKSKEVWK ALLQEMPLTA LLRNLGKMTA NSVLEPGNSE 310 320 330 340 350 360 VSLVCEKLCN EKLLKKARIH PFHILIALET YKTGHGLRGK LKWRPDEEIL KALDAAFYKT 370 380 390 400 410 420 FKTVEPTGKR FLLAVDVSAS MNQRVLGSIL NASTVAAAMC MVVTRTEKDS YVVAFSDEMV 430 440 450 460 470 480 PCPVTTDMTL QQVLMAMSQI PAGGTDCSLP MIWAQKTNTP ADVFIVFTDN ETFAGGVHPA 490 500 510 520 530 IALREYRKKM DIPAKLIVCG MTSNGFTIAD PDDRGMLDMC GFDTGALDPC KIPY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular analysis of the 60-kDa human Ro ribonucleoprotein." Deutscher S.L., Harley J.B., Keene J.D. Proc. Natl. Acad. Sci. U.S.A. 85:9479-9483(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
[2]	"Isolation and characterization of a cDNA clone encoding the 60-kD component of the human SS-A/Ro ribonucleoprotein autoantigen." Ben-Chetrit E., Gandy B.J., Tan E.M., Sulivan K.F. J. Clin. Invest. 83:1284-1292(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
[3]	"Identification and characterization of an alternative mRNA transcript of the 60-kD SS-A/Ro ribonucleoprotein encoding the N-terminal RNA binding domain alone." Buyon J.P., DiDonato F., Tseng C.E., Rashbaum W., Morris A., Hamel J.C., Chan E.K.L. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SHORT).
[4]	"A variant of the 60-kD component of the human SS-A/Ro ribonucleoprotein autoantigen involved in multidrug resistance of gastric cancer cells." Han Q., Wang X., Shi Y., Ding J., Fan D. Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
[5]	"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 LONG). Tissue: Thalamus.
[6]	"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].
[7]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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 LONG). Tissue: Testis.
[9]	Bienvenut W.V., Sumpton D.P., Lilla S., Ozanne B.W. Submitted (FEB-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-14; 271-283 AND 352-359, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: Pre-B cell.
[10]	"Defining a novel 75-kDa phosphoprotein associated with SS-A/Ro and identification of distinct human autoantibodies." Wang D., Buyon J.P., Zhu W., Chan E.K.L. J. Clin. Invest. 104:1265-1275(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RIP11. Tissue: Keratinocyte.
[11]	"Interaction cloning and characterization of RoBPI, a novel protein binding to human Ro ribonucleoproteins." Bouffard P., Barbar E., Briere F., Boire G. RNA 6:66-78(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH PUF60 AND Y5 RNA.
[12]	"Human Y5 RNA specializes a Ro ribonucleoprotein for 5S ribosomal RNA quality control." Hogg J.R., Collins K. Genes Dev. 21:3067-3072(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Molecular composition of IMP1 ribonucleoprotein granules." Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C. Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, SUBCELLULAR LOCATION.
[14]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[15]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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-19, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-224 AND LYS-359, MASS SPECTROMETRY.
[18]	"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-19, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04137 mRNA. Translation: AAA35493.1. M25077 mRNA. Translation: AAA35532.1. U44388 Genomic DNA. Translation: AAB81552.1. Different termination. U44388 Genomic DNA. Translation: AAB81553.1. AY205314 mRNA. Translation: AAO47001.1. AY205315 mRNA. Translation: AAO47002.1. AK314594 mRNA. Translation: BAG37166.1. AL136370 Genomic DNA. Translation: CAC17589.1. AL136370 Genomic DNA. Translation: CAI10823.1. AL136370 Genomic DNA. Translation: CAI10824.1. CH471067 Genomic DNA. Translation: EAW91240.1. CH471067 Genomic DNA. Translation: EAW91243.1. CH471067 Genomic DNA. Translation: EAW91245.1. BC036658 mRNA. Translation: AAH36658.1.
IPI	IPI00019450. IPI00219287. IPI00642416. IPI00646322.
PIR	A31760.
RefSeq	NP_001035828.1. NM_001042369.2. NP_001035829.2. NM_001042370.2. NP_001166995.1. NM_001173524.1. NP_001166996.1. NM_001173525.1. NP_004591.2. NM_004600.5.
UniGene	Hs.288178.
3D structure databases
ProteinModelPortal	P10155.
ModBase	Search...
Protein-protein interaction databases
IntAct	P10155. 3 interactions.
MINT	MINT-8395039.
STRING	9606.ENSP00000356411.
PTM databases
PhosphoSite	P10155.
Polymorphism databases
DMDM	52788235.
Proteomic databases
PaxDb	P10155.
PRIDE	P10155.
Protocols and materials databases
DNASU	6738.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000367441; ENSP00000356411; ENSG00000116747. ENST00000367443; ENSP00000356413; ENSG00000116747. ENST00000367445; ENSP00000356415; ENSG00000116747. ENST00000367446; ENSP00000356416; ENSG00000116747. ENST00000400968; ENSP00000383752; ENSG00000116747.
GeneID	6738.
KEGG	hsa:6738.
UCSC	uc001gss.3. human. uc009wyp.3. human. uc009wyq.3. human.
Organism-specific databases
CTD	6738.
GeneCards	GC01P193028.
HGNC	HGNC:11313. TROVE2.
HPA	HPA002835.
MIM	600063. gene.
neXtProt	NX_P10155.
PharmGKB	PA36137.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG74865.
HOGENOM	HOG000075167.
HOVERGEN	HBG013234.
InParanoid	P10155.
KO	K11089.
OMA	AKQEPML.
OrthoDB	EOG4NZTT5.
PhylomeDB	P10155.
Gene expression databases
ArrayExpress	P10155.
Bgee	P10155.
CleanEx	HS_TROVE2.
Genevestigator	P10155.
GermOnline	ENSG00000116747. Homo sapiens.
Family and domain databases
InterPro	IPR008858. TROVE. IPR018698. VWA-like_dom. [Graphical view]
Pfam	PF09967. DUF2201. 1 hit. PF05731. TROVE. 1 hit. [Graphical view]
PROSITE	PS50988. TROVE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TROVE2. human.
GenomeRNAi	6738.
NextBio	26284.
SOURCE	Search...

Entry information

Entry name

RO60_HUMAN

Accession

Primary (citable) accession number: P10155
Secondary accession number(s): B2RBB9 , Q5LJ98, Q5LJ99, Q86WL3, Q86WL4, Q92787, Q9H1W6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	September 27, 2004
Last modified:	May 29, 2013
This is version 133 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.