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Q96E14

- RMI2_HUMAN

UniProt

Q96E14 - RMI2_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 71Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated during mitosis.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ96E14.
PaxDbiQ96E14.
PRIDEiQ96E14.

PTM databases

PhosphoSiteiQ96E14.

Expressioni

Gene expression databases

BgeeiQ96E14.
CleanExiHS_C16orf75.
ExpressionAtlasiQ96E14. baseline and differential.
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. 11 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 – 337Combined sources
Beta strandi34 – 363Combined sources
Beta strandi40 – 434Combined sources
Turni46 – 494Combined sources
Beta strandi56 – 6813Combined sources
Beta strandi71 – 766Combined sources
Beta strandi79 – 846Combined sources
Helixi86 – 883Combined sources
Beta strandi92 – 943Combined sources
Beta strandi101 – 11010Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi116 – 1249Combined sources
Helixi130 – 14314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000001653.
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

        10         20         30         40         50
MAAAADSFSG GPAGVRLPRS PPLKVLAEQL RRDAEGGPGA WRLSRAAAGR
60 70 80 90 100
GPLDLAAVWM QGRVVMADRG EARLRDPSGD FSVRGLERVP RGRPCLVPGK
110 120 130 140
YVMVMGVVQA CSPEPCLQAV KMTDLSDNPI HESMWELEVE DLHRNIP
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 11 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.
GeneTreei ENSGT00390000001653.
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

Bgeei Q96E14.
CleanExi HS_C16orf75.
ExpressionAtlasi Q96E14. baseline and differential.
Genevestigatori Q96E14.

Family and domain databases

ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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: November 26, 2014
This is version 95 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