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Protein

60 kDa SS-A/Ro ribonucleoprotein

Gene

TROVE2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication
May play roles in cilia formation and/or maintenance.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi378 – 3781Divalent metal cationBy similarity
Metal bindingi380 – 3801Divalent metal cationBy similarity
Metal bindingi445 – 4451Divalent metal cationBy similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • RNA binding Source: ProtInc
  • U2 snRNA binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

Cilium biogenesis/degradation

Keywords - Ligandi

Metal-binding, RNA-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:TROVE2
Synonyms:RO60, SSA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:11313. TROVE2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nucleoplasm Source: HPA
  • ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36137.

Polymorphism and mutation databases

BioMutaiTROVE2.
DMDMi52788235.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 53853860 kDa SS-A/Ro ribonucleoproteinPRO_0000174169Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei19 – 191Phosphoserine3 Publications
Modified residuei224 – 2241N6-acetyllysine1 Publication
Modified residuei359 – 3591N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP10155.
PaxDbiP10155.
PRIDEiP10155.

PTM databases

PhosphoSiteiP10155.

Expressioni

Gene expression databases

BgeeiP10155.
CleanExiHS_TROVE2.
ExpressionAtlasiP10155. baseline and differential.
GenevisibleiP10155. HS.

Organism-specific databases

HPAiHPA002835.

Interactioni

Subunit structurei

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Found in a complex with PUF60 and Y5 RNA. Interacts with RIP11.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PUF60Q9UHX11EBI-1049168,EBI-1053259

Protein-protein interaction databases

BioGridi112616. 25 interactions.
IntActiP10155. 6 interactions.
MINTiMINT-8395039.
STRINGi9606.ENSP00000356411.

Structurei

3D structure databases

ProteinModelPortaliP10155.
SMRiP10155. Positions 4-537.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 369354TROVEPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni120 – 284165RNA-bindingBy similarityAdd
BLAST
Regioni361 – 538178VWFA-like domainBy similarityAdd
BLAST

Domaini

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).By similarity
The MIDAS-like motif in the VWFA-like domain binds divalent metal cations.By similarity

Sequence similaritiesi

Belongs to the Ro 60 kDa family.Curated
Contains 1 TROVE domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG74865.
GeneTreeiENSGT00390000006200.
HOGENOMiHOG000075167.
HOVERGENiHBG013234.
InParanoidiP10155.
KOiK11089.
OMAiAKQEPML.
OrthoDBiEOG78D7JR.
PhylomeDBiP10155.
TreeFamiTF105990.

Family and domain databases

InterProiIPR008858. TROVE.
IPR018698. VWA-like_dom.
IPR002035. VWF_A.
[Graphical view]
PfamiPF09967. DUF2201. 1 hit.
PF05731. TROVE. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
PROSITEiPS50988. TROVE. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P10155-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MEESVNQMQP LNEKQIANSQ DGYVWQVTDM NRLHRFLCFG SEGGTYYIKE
60 70 80 90 100
QKLGLENAEA LIRLIEDGRG CEVIQEIKSF SQEGRTTKQE PMLFALAICS
110 120 130 140 150
QCSDISTKQA AFKAVSEVCR IPTHLFTFIQ FKKDLKESMK CGMWGRALRK
160 170 180 190 200
AIADWYNEKG GMALALAVTK YKQRNGWSHK DLLRLSHLKP SSEGLAIVTK
210 220 230 240 250
YITKGWKEVH ELYKEKALSV ETEKLLKYLE AVEKVKRTRD ELEVIHLIEE
260 270 280 290 300
HRLVREHLLT NHLKSKEVWK ALLQEMPLTA LLRNLGKMTA NSVLEPGNSE
310 320 330 340 350
VSLVCEKLCN EKLLKKARIH PFHILIALET YKTGHGLRGK LKWRPDEEIL
360 370 380 390 400
KALDAAFYKT FKTVEPTGKR FLLAVDVSAS MNQRVLGSIL NASTVAAAMC
410 420 430 440 450
MVVTRTEKDS YVVAFSDEMV PCPVTTDMTL QQVLMAMSQI PAGGTDCSLP
460 470 480 490 500
MIWAQKTNTP ADVFIVFTDN ETFAGGVHPA IALREYRKKM DIPAKLIVCG
510 520 530
MTSNGFTIAD PDDRGMLDMC GFDTGALDVI RNFTLDMI
Length:538
Mass (Da):60,671
Last modified:September 27, 2004 - v2
Checksum:iCD735B1DF2B13098
GO
Isoform Short (identifier: P10155-2) [UniParc]FASTAAdd to basket

Also known as: 60E2

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

Show »
Length:205
Mass (Da):23,299
Checksum:i31CF4F9732BEB16E
GO
Isoform 3 (identifier: P10155-3) [UniParc]FASTAAdd to basket

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

Show »
Length:518
Mass (Da):58,483
Checksum:iD3CE550ADBB2761B
GO
Isoform 4 (identifier: P10155-4) [UniParc]FASTAAdd to basket

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

Show »
Length:534
Mass (Da):60,169
Checksum:i785F949FED553344
GO
Isoform 5 (identifier: P10155-5) [UniParc]FASTAAdd to basket

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

Show »
Length:525
Mass (Da):59,270
Checksum:i9240B125E1038544
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361K → R in AAO47001 (Ref. 4) Curated
Sequence conflicti136 – 1361K → R in AAO47002 (Ref. 4) Curated
Sequence conflicti239 – 2391R → K in AAA35493 (PubMed:3200833).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei195 – 20511LAIVTKYITKG → KHKIFIGKKGG in isoform Short. CuratedVSP_005911Add
BLAST
Alternative sequencei206 – 538333Missing in isoform Short. CuratedVSP_005912Add
BLAST
Alternative sequencei515 – 53824GMLDM…TLDMI → DTVK in isoform 3. 1 PublicationVSP_045262Add
BLAST
Alternative sequencei515 – 53824GMLDM…TLDMI → ALQNTLLNKSF in isoform 5. 1 PublicationVSP_054041Add
BLAST
Alternative sequencei529 – 53810VIRNFTLDMI → PCKIPY in isoform 4. 1 PublicationVSP_045797

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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. No translation available.
CH471067 Genomic DNA. Translation: EAW91240.1.
CH471067 Genomic DNA. Translation: EAW91243.1.
CH471067 Genomic DNA. Translation: EAW91245.1.
CH471067 Genomic DNA. Translation: EAW91247.1.
BC036658 mRNA. Translation: AAH36658.1.
CCDSiCCDS1379.1. [P10155-1]
CCDS41449.1. [P10155-5]
CCDS41450.2. [P10155-4]
CCDS53451.1. [P10155-3]
PIRiA31760.
RefSeqiNP_001035828.1. NM_001042369.2. [P10155-5]
NP_001035829.2. NM_001042370.2. [P10155-4]
NP_001166995.1. NM_001173524.1. [P10155-1]
NP_001166996.1. NM_001173525.1. [P10155-3]
NP_004591.2. NM_004600.5. [P10155-1]
XP_006711560.1. XM_006711497.2. [P10155-1]
UniGeneiHs.288178.

Genome annotation databases

EnsembliENST00000367441; ENSP00000356411; ENSG00000116747.
ENST00000367443; ENSP00000356413; ENSG00000116747. [P10155-3]
ENST00000367444; ENSP00000356414; ENSG00000116747. [P10155-5]
ENST00000367445; ENSP00000356415; ENSG00000116747. [P10155-4]
ENST00000367446; ENSP00000356416; ENSG00000116747.
ENST00000400968; ENSP00000383752; ENSG00000116747.
GeneIDi6738.
KEGGihsa:6738.
UCSCiuc001gss.3. human. [P10155-1]
uc001gsw.3. human.
uc009wyp.3. human.
uc009wyq.3. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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. No translation available.
CH471067 Genomic DNA. Translation: EAW91240.1.
CH471067 Genomic DNA. Translation: EAW91243.1.
CH471067 Genomic DNA. Translation: EAW91245.1.
CH471067 Genomic DNA. Translation: EAW91247.1.
BC036658 mRNA. Translation: AAH36658.1.
CCDSiCCDS1379.1. [P10155-1]
CCDS41449.1. [P10155-5]
CCDS41450.2. [P10155-4]
CCDS53451.1. [P10155-3]
PIRiA31760.
RefSeqiNP_001035828.1. NM_001042369.2. [P10155-5]
NP_001035829.2. NM_001042370.2. [P10155-4]
NP_001166995.1. NM_001173524.1. [P10155-1]
NP_001166996.1. NM_001173525.1. [P10155-3]
NP_004591.2. NM_004600.5. [P10155-1]
XP_006711560.1. XM_006711497.2. [P10155-1]
UniGeneiHs.288178.

3D structure databases

ProteinModelPortaliP10155.
SMRiP10155. Positions 4-537.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112616. 25 interactions.
IntActiP10155. 6 interactions.
MINTiMINT-8395039.
STRINGi9606.ENSP00000356411.

PTM databases

PhosphoSiteiP10155.

Polymorphism and mutation databases

BioMutaiTROVE2.
DMDMi52788235.

Proteomic databases

MaxQBiP10155.
PaxDbiP10155.
PRIDEiP10155.

Protocols and materials databases

DNASUi6738.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367441; ENSP00000356411; ENSG00000116747.
ENST00000367443; ENSP00000356413; ENSG00000116747. [P10155-3]
ENST00000367444; ENSP00000356414; ENSG00000116747. [P10155-5]
ENST00000367445; ENSP00000356415; ENSG00000116747. [P10155-4]
ENST00000367446; ENSP00000356416; ENSG00000116747.
ENST00000400968; ENSP00000383752; ENSG00000116747.
GeneIDi6738.
KEGGihsa:6738.
UCSCiuc001gss.3. human. [P10155-1]
uc001gsw.3. human.
uc009wyp.3. human.
uc009wyq.3. human.

Organism-specific databases

CTDi6738.
GeneCardsiGC01P193028.
HGNCiHGNC:11313. TROVE2.
HPAiHPA002835.
MIMi600063. gene.
neXtProtiNX_P10155.
PharmGKBiPA36137.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG74865.
GeneTreeiENSGT00390000006200.
HOGENOMiHOG000075167.
HOVERGENiHBG013234.
InParanoidiP10155.
KOiK11089.
OMAiAKQEPML.
OrthoDBiEOG78D7JR.
PhylomeDBiP10155.
TreeFamiTF105990.

Miscellaneous databases

ChiTaRSiTROVE2. human.
GeneWikiiTROVE2.
GenomeRNAii6738.
NextBioi26284.
PROiP10155.
SOURCEiSearch...

Gene expression databases

BgeeiP10155.
CleanExiHS_TROVE2.
ExpressionAtlasiP10155. baseline and differential.
GenevisibleiP10155. HS.

Family and domain databases

InterProiIPR008858. TROVE.
IPR018698. VWA-like_dom.
IPR002035. VWF_A.
[Graphical view]
PfamiPF09967. DUF2201. 1 hit.
PF05731. TROVE. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
PROSITEiPS50988. TROVE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 5).
  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. 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, IDENTIFICATION BY 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. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, SUBCELLULAR LOCATION.
  14. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRO60_HUMAN
AccessioniPrimary (citable) accession number: P10155
Secondary accession number(s): B2RBB9
, Q5LJ98, Q5LJ99, Q5LJA0, Q86WL3, Q86WL4, Q92787, Q9H1W6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: September 27, 2004
Last modified: July 22, 2015
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Miscellaneous

Antibodies against normal cellular SSA2 protein are found in sera from patients with systemic lupus erythematosus (SLE).

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.