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Q96E14 (RMI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RecQ-mediated genome instability protein 2

Short name=hRMI2
Alternative name(s):
BLM-associated protein of 18 kDa
Short name=BLAP18
Gene names
Name:RMI2
Synonyms:C16orf75
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. The complex is therefore essential for the stability, localization, and function of complexes containing BLM. In the RMI complex, it is required to target BLM to chromatin and stress-induced nuclear foci and mitotic phosphorylation of BLM. Ref.5 Ref.6

Subunit structure

Component of the RMI complex, containing at least TOP3A, RMI1 and RMI2. The RMI complex interacts with BLM. Ref.5 Ref.6

Subcellular location

Nucleus. Note: Colocalizes with BLM at nuclear DNA repair foci. Ref.5

Post-translational modification

Phosphorylated during mitosis. Ref.6

Sequence similarities

Belongs to the RMI2 family.

Contains 1 OB DNA-binding domain.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96E14-1)

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: Q96E14-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-98: MAAAADSFSG...VPRGRPCLVP → MKQTQVGSLFSLGIRNPEPGPVSGTAVPRQLAWKS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 147146RecQ-mediated genome instability protein 2
PRO_0000297577

Regions

DNA binding44 – 11471OB

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.8
Modified residue71Phosphoserine Ref.7

Natural variations

Alternative sequence1 – 9898MAAAA…PCLVP → MKQTQVGSLFSLGIRNPEPG PVSGTAVPRQLAWKS in isoform 2.
VSP_027287

Experimental info

Mutagenesis241K → A: Abolishes interaction with RMI1, TOP3A and BLM. Ref.6
Mutagenesis591W → A: According to PubMed:18923083, abolishes interaction with RMI1, TOP3A and BLM. According to PubMed:18923082, does not affects interaction with RMI1 and TOP3A. Ref.6
Mutagenesis1001K → A: Does not affect interaction with RMI1, TOP3A and BLM. Ref.6
Mutagenesis1211K → A: According to PubMed:18923083, does not affect interaction with RMI1, TOP3A and BLM. According to PubMed:18923082, affects interaction with BLM and the BMI complex. Ref.5 Ref.6
Mutagenesis1351W → A: Abolishes interaction with RMI1, TOP3A and BLM. Ref.6

Secondary structure

.......................... 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: C385825F9AB4439E

FASTA14715,865
        10         20         30         40         50         60 
MAAAADSFSG GPAGVRLPRS PPLKVLAEQL RRDAEGGPGA WRLSRAAAGR GPLDLAAVWM 

        70         80         90        100        110        120 
QGRVVMADRG EARLRDPSGD FSVRGLERVP RGRPCLVPGK YVMVMGVVQA CSPEPCLQAV 

       130        140 
KMTDLSDNPI HESMWELEVE DLHRNIP 

« Hide

Isoform 2 [UniParc].

Checksum: DAFD4A80EF28023B
Show »

FASTA849,262

References

« Hide 'large scale' references
[1]"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 1).
[2]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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 2).
Tissue: Lung, Lymph, Skin and Testis.
[5]"RMI, a new OB-fold complex essential for Bloom syndrome protein to maintain genome stability."
Xu D., Guo R., Sobeck A., Bachrati C.Z., Yang J., Enomoto T., Brown G.W., Hoatlin M.E., Hickson I.D., Wang W.
Genes Dev. 22:2843-2855(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE RMI COMPLEX, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-121.
[6]"BLAP18/RMI2, a novel OB-fold-containing protein, is an essential component of the Bloom helicase-double Holliday junction dissolvasome."
Singh T.R., Ali A.M., Busygina V., Raynard S., Fan Q., Du C.-H., Andreassen P.R., Sung P., Meetei A.R.
Genes Dev. 22:2856-2868(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE RMI COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION, MUTAGENESIS OF LYS-24; TRP-59; LYS-100; LYS-121 AND TRP-135.
[7]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK123764 mRNA. Translation: BAG53958.1.
AC009121 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85155.1.
BC013040 mRNA. Translation: AAH13040.2.
BC022427 mRNA. Translation: AAH22427.1.
BC031016 mRNA. Translation: AAH31016.1.
BC039361 mRNA. Translation: AAH39361.1.
CCDSCCDS10548.1. [Q96E14-1]
RefSeqNP_689521.1. NM_152308.1. [Q96E14-1]
UniGeneHs.347524.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MXNX-ray1.55B1-147[»]
3NBHX-ray2.00B6-147[»]
4DAYX-ray3.30B1-147[»]
ProteinModelPortalQ96E14.
SMRQ96E14. Positions 17-147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125466. 9 interactions.
DIPDIP-56480N.
IntActQ96E14. 6 interactions.
MINTMINT-8048937.
STRING9606.ENSP00000310356.

PTM databases

PhosphoSiteQ96E14.

Polymorphism databases

DMDM74731517.

Proteomic databases

MaxQBQ96E14.
PaxDbQ96E14.
PRIDEQ96E14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312499; ENSP00000310356; ENSG00000175643. [Q96E14-1]
ENST00000381820; ENSP00000371241; ENSG00000175643. [Q96E14-2]
ENST00000572173; ENSP00000461206; ENSG00000175643. [Q96E14-2]
GeneID116028.
KEGGhsa:116028.
UCSCuc002daw.1. human. [Q96E14-1]

Organism-specific databases

CTD116028.
GeneCardsGC16P011343.
H-InvDBHIX0012817.
HGNCHGNC:28349. RMI2.
HPAHPA040995.
MIM612426. gene.
neXtProtNX_Q96E14.
PharmGKBPA145149635.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG27893.
HOGENOMHOG000154149.
HOVERGENHBG108410.
InParanoidQ96E14.
KOK15365.
OMANTIEGEW.
OrthoDBEOG7M6D9F.
PhylomeDBQ96E14.
TreeFamTF332971.

Gene expression databases

ArrayExpressQ96E14.
BgeeQ96E14.
CleanExHS_C16orf75.
GenevestigatorQ96E14.

Family and domain databases

ProtoNetSearch...

Other

ChiTaRSRMI2. human.
GenomeRNAi116028.
NextBio79725.
PROQ96E14.
SOURCESearch...

Entry information

Entry nameRMI2_HUMAN
AccessionPrimary (citable) accession number: Q96E14
Secondary accession number(s): B3KVZ6, Q49AE2, Q8TBL0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: March 1, 2004
Last modified: July 9, 2014
This is version 92 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM