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Q96E14

- RMI2_HUMAN

UniProt

Q96E14 - RMI2_HUMAN

Protein

RecQ-mediated genome instability protein 2

Gene

RMI2

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

    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.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi44 – 11471OBAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. DNA replication Source: UniProtKB-KW

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RecQ-mediated genome instability protein 2
    Short name:
    hRMI2
    Alternative name(s):
    BLM-associated protein of 18 kDa
    Short name:
    BLAP18
    Gene namesi
    Name:RMI2
    Synonyms:C16orf75
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:28349. RMI2.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Colocalizes with BLM at nuclear DNA repair foci.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi24 – 241K → A: Abolishes interaction with RMI1, TOP3A and BLM. 1 Publication
    Mutagenesisi59 – 591W → A: According to PubMed:18923083, abolishes interaction with RMI1, TOP3A and BLM. According to PubMed:18923082, does not affects interaction with RMI1 and TOP3A. 1 Publication
    Mutagenesisi100 – 1001K → A: Does not affect interaction with RMI1, TOP3A and BLM. 1 Publication
    Mutagenesisi121 – 1211K → 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. 2 Publications
    Mutagenesisi135 – 1351W → A: Abolishes interaction with RMI1, TOP3A and BLM. 1 Publication

    Organism-specific databases

    PharmGKBiPA145149635.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 147146RecQ-mediated genome instability protein 2PRO_0000297577Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei7 – 71Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated during mitosis.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96E14.
    PaxDbiQ96E14.
    PRIDEiQ96E14.

    PTM databases

    PhosphoSiteiQ96E14.

    Expressioni

    Gene expression databases

    ArrayExpressiQ96E14.
    BgeeiQ96E14.
    CleanExiHS_C16orf75.
    GenevestigatoriQ96E14.

    Organism-specific databases

    HPAiHPA040995.

    Interactioni

    Subunit structurei

    Component of the RMI complex, containing at least TOP3A, RMI1 and RMI2. The RMI complex interacts with BLM.2 Publications

    Protein-protein interaction databases

    BioGridi125466. 9 interactions.
    DIPiDIP-56480N.
    IntActiQ96E14. 6 interactions.
    MINTiMINT-8048937.
    STRINGi9606.ENSP00000310356.

    Structurei

    Secondary structure

    1
    147
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi27 – 337
    Beta strandi34 – 363
    Beta strandi40 – 434
    Turni46 – 494
    Beta strandi56 – 6813
    Beta strandi71 – 766
    Beta strandi79 – 846
    Helixi86 – 883
    Beta strandi92 – 943
    Beta strandi101 – 11010
    Beta strandi112 – 1143
    Beta strandi116 – 1249
    Helixi130 – 14314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MXNX-ray1.55B1-147[»]
    3NBHX-ray2.00B6-147[»]
    4DAYX-ray3.30B1-147[»]
    ProteinModelPortaliQ96E14.
    SMRiQ96E14. Positions 17-147.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RMI2 family.Curated
    Contains 1 OB DNA-binding domain.Curated

    Phylogenomic databases

    eggNOGiNOG27893.
    HOGENOMiHOG000154149.
    HOVERGENiHBG108410.
    InParanoidiQ96E14.
    KOiK15365.
    OMAiNTIEGEW.
    OrthoDBiEOG7M6D9F.
    PhylomeDBiQ96E14.
    TreeFamiTF332971.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96E14-1) [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

    MAAAADSFSG GPAGVRLPRS PPLKVLAEQL RRDAEGGPGA WRLSRAAAGR    50
    GPLDLAAVWM QGRVVMADRG EARLRDPSGD FSVRGLERVP RGRPCLVPGK 100
    YVMVMGVVQA CSPEPCLQAV KMTDLSDNPI HESMWELEVE DLHRNIP 147
    Length:147
    Mass (Da):15,865
    Last modified:March 1, 2004 - v2
    Checksum:iC385825F9AB4439E
    GO
    Isoform 2 (identifier: Q96E14-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-98: MAAAADSFSG...VPRGRPCLVP → MKQTQVGSLFSLGIRNPEPGPVSGTAVPRQLAWKS

    Note: No experimental confirmation available.

    Show »
    Length:84
    Mass (Da):9,262
    Checksum:iDAFD4A80EF28023B
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9898MAAAA…PCLVP → MKQTQVGSLFSLGIRNPEPG PVSGTAVPRQLAWKS in isoform 2. 1 PublicationVSP_027287Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS10548.1. [Q96E14-1]
    RefSeqiNP_689521.1. NM_152308.1. [Q96E14-1]
    UniGeneiHs.347524.

    Genome annotation databases

    EnsembliENST00000312499; ENSP00000310356; ENSG00000175643. [Q96E14-1]
    ENST00000572173; ENSP00000461206; ENSG00000175643. [Q96E14-2]
    GeneIDi116028.
    KEGGihsa:116028.
    UCSCiuc002daw.1. human. [Q96E14-1]

    Polymorphism databases

    DMDMi74731517.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS10548.1. [Q96E14-1 ]
    RefSeqi NP_689521.1. NM_152308.1. [Q96E14-1 ]
    UniGenei Hs.347524.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3MXN X-ray 1.55 B 1-147 [» ]
    3NBH X-ray 2.00 B 6-147 [» ]
    4DAY X-ray 3.30 B 1-147 [» ]
    ProteinModelPortali Q96E14.
    SMRi Q96E14. Positions 17-147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125466. 9 interactions.
    DIPi DIP-56480N.
    IntActi Q96E14. 6 interactions.
    MINTi MINT-8048937.
    STRINGi 9606.ENSP00000310356.

    PTM databases

    PhosphoSitei Q96E14.

    Polymorphism databases

    DMDMi 74731517.

    Proteomic databases

    MaxQBi Q96E14.
    PaxDbi Q96E14.
    PRIDEi Q96E14.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000312499 ; ENSP00000310356 ; ENSG00000175643 . [Q96E14-1 ]
    ENST00000572173 ; ENSP00000461206 ; ENSG00000175643 . [Q96E14-2 ]
    GeneIDi 116028.
    KEGGi hsa:116028.
    UCSCi uc002daw.1. human. [Q96E14-1 ]

    Organism-specific databases

    CTDi 116028.
    GeneCardsi GC16P011343.
    H-InvDB HIX0012817.
    HGNCi HGNC:28349. RMI2.
    HPAi HPA040995.
    MIMi 612426. gene.
    neXtProti NX_Q96E14.
    PharmGKBi PA145149635.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG27893.
    HOGENOMi HOG000154149.
    HOVERGENi HBG108410.
    InParanoidi Q96E14.
    KOi K15365.
    OMAi NTIEGEW.
    OrthoDBi EOG7M6D9F.
    PhylomeDBi Q96E14.
    TreeFami TF332971.

    Miscellaneous databases

    ChiTaRSi RMI2. human.
    GenomeRNAii 116028.
    NextBioi 79725.
    PROi Q96E14.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96E14.
    Bgeei Q96E14.
    CleanExi HS_C16orf75.
    Genevestigatori Q96E14.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRMI2_HUMAN
    AccessioniPrimary (citable) accession number: Q96E14
    Secondary accession number(s): B3KVZ6, Q49AE2, Q8TBL0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 21, 2007
    Last sequence update: March 1, 2004
    Last modified: October 1, 2014
    This is version 93 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3