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P10155 (RO60_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length538 AA.
Sequence statusComplete.
Protein existenceEvidence 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 IGF2BP1-dependent mRNP granule complex containing 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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PUF60Q9UHX11EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 53853860 kDa SS-A/Ro ribonucleoprotein
PRO_0000174169

Regions

Domain16 – 369354TROVE
Region120 – 284165RNA-binding By similarity
Region361 – 538178VWFA-like domain By similarity

Sites

Metal binding3781Divalent metal cation By similarity
Metal binding3801Divalent metal cation By similarity
Metal binding4451Divalent metal cation By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9 Ref.17
Modified residue191Phosphoserine Ref.15 Ref.16 Ref.19
Modified residue2241N6-acetyllysine Ref.18
Modified residue3591N6-acetyllysine Ref.18

Natural variations

Alternative sequence195 – 20511LAIVTKYITKG → KHKIFIGKKGG in isoform Short.
VSP_005911
Alternative sequence206 – 538333Missing in isoform Short.
VSP_005912
Alternative sequence515 – 53824GMLDM…TLDMI → DTVK in isoform 3.
VSP_045262
Alternative sequence529 – 53810VIRNFTLDMI → PCKIPY in isoform 4.
VSP_045797

Experimental info

Sequence conflict1361K → R in AAO47001. Ref.4
Sequence conflict1361K → R in AAO47002. Ref.4
Sequence conflict2391R → K in AAA35493. Ref.1
Sequence conflict515 – 53824GMLDM…TLDMI → ALQNTLLNKSF in AAB81552. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified September 27, 2004. Version 2.
Checksum: CD735B1DF2B13098

FASTA53860,671
        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 

« Hide

Isoform Short (60E2) [UniParc].

Checksum: 31CF4F9732BEB16E
Show »

FASTA20523,299
Isoform 3 [UniParc].

Checksum: D3CE550ADBB2761B
Show »

FASTA51858,483
Isoform 4 [UniParc].

Checksum: 785F949FED553344
Show »

FASTA53460,169

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, 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]"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].
[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].
+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.
PIRA31760.
RefSeqNP_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.
UniGeneHs.288178.

3D structure databases

ProteinModelPortalP10155.
SMRP10155. Positions 4-537.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112616. 26 interactions.
IntActP10155. 4 interactions.
MINTMINT-8395039.
STRING9606.ENSP00000356411.

PTM databases

PhosphoSiteP10155.

Polymorphism databases

DMDM52788235.

Proteomic databases

PaxDbP10155.
PRIDEP10155.

Protocols and materials databases

DNASU6738.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367441; ENSP00000356411; ENSG00000116747. [P10155-1]
ENST00000367443; ENSP00000356413; ENSG00000116747. [P10155-3]
ENST00000367445; ENSP00000356415; ENSG00000116747. [P10155-4]
ENST00000367446; ENSP00000356416; ENSG00000116747. [P10155-1]
ENST00000400968; ENSP00000383752; ENSG00000116747. [P10155-1]
GeneID6738.
KEGGhsa:6738.
UCSCuc001gss.3. human. [P10155-1]
uc009wyp.3. human.
uc009wyq.3. human.

Organism-specific databases

CTD6738.
GeneCardsGC01P193028.
HGNCHGNC:11313. TROVE2.
HPAHPA002835.
MIM600063. gene.
neXtProtNX_P10155.
PharmGKBPA36137.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG74865.
HOGENOMHOG000075167.
HOVERGENHBG013234.
InParanoidP10155.
KOK11089.
OMAAKQEPML.
OrthoDBEOG78D7JR.
PhylomeDBP10155.
TreeFamTF105990.

Gene expression databases

ArrayExpressP10155.
BgeeP10155.
CleanExHS_TROVE2.
GenevestigatorP10155.

Family and domain databases

InterProIPR008858. TROVE.
IPR018698. VWA-like_dom.
[Graphical view]
PfamPF09967. DUF2201. 1 hit.
PF05731. TROVE. 1 hit.
[Graphical view]
PROSITEPS50988. TROVE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTROVE2. human.
GeneWikiTROVE2.
GenomeRNAi6738.
NextBio26284.
PROP10155.
SOURCESearch...

Entry information

Entry nameRO60_HUMAN
AccessionPrimary (citable) accession number: P10155
Secondary accession number(s): B2RBB9 expand/collapse secondary AC list , Q5LJ98, Q5LJ99, Q86WL3, Q86WL4, Q92787, Q9H1W6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: September 27, 2004
Last modified: March 19, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM