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Q9H9A7 (RMI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RecQ-mediated genome instability protein 1
Alternative name(s):
BLM-associated protein of 75 kDa
Short name=BLAP75
FAAP75
Gene names
Name:RMI1
Synonyms:C9orf76
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length625 AA.
Sequence statusComplete.
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. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability. Ref.4 Ref.5 Ref.6

Subunit structure

Component of the RMI complex, containing at least TOP3A, RMI1 and RMI2. The RMI complex interacts with BLM. Directly interacts with RMI2 and TOP3A. May bind DHJ. Interacts (via N-terminal region) with BLM; the interaction is direct. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.11

Subcellular location

Nucleus. Note: Forms foci in response to DNA damage. Ref.4

Sequence similarities

Belongs to the RMI1 family.

Sequence caution

The sequence AAH20606.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAH32494.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAH39999.1 differs from that shown. Reason: Frameshift at position 375.

The sequence AAH39999.1 differs from that shown. Reason: Frameshift at positions 377 and 444.

The sequence AAH53549.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAH64937.1 differs from that shown. Reason: Frameshift at positions 444 and 615.

The sequence AAH64937.1 differs from that shown. Reason: Frameshift at positions 377 and 444.

The sequence CAI13575.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from direct assay. Source: HPA

   Molecular_functionprotein binding

Inferred from physical interaction Ref.11. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BLMP5413210EBI-621339,EBI-621372

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 625625RecQ-mediated genome instability protein 1
PRO_0000227546

Amino acid modifications

Modified residue11N-acetylmethionine Ref.10
Modified residue2251Phosphoserine Ref.9

Natural variations

Natural variant1001Y → H. Ref.3
Corresponds to variant rs17855932 [ dbSNP | Ensembl ].
VAR_025556
Natural variant4551N → S. Ref.1 Ref.3
Corresponds to variant rs1982151 [ dbSNP | Ensembl ].
VAR_025557

Experimental info

Sequence conflict111E → G in BAB14325. Ref.1
Sequence conflict2591A → T in BAB14325. Ref.1
Sequence conflict3181E → D in AAH20606. Ref.3
Sequence conflict4431L → F in AAH39999. Ref.3

Secondary structure

.......................................................... 625
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9H9A7 [UniParc].

Last modified February 8, 2011. Version 3.
Checksum: 2BB449363DBF76B7

FASTA62570,144
        10         20         30         40         50         60 
MNVTSIALRA ETWLLAAWHV KVPPMWLEAC INWIQEENNN VNLSQAQMNK QVFEQWLLTD 

        70         80         90        100        110        120 
LRDLEHPLLP DGILEIPKGE LNGFYALQIN SLVDVSQPAY SQIQKLRGKN TTNDLVTAEA 

       130        140        150        160        170        180 
QVTPKPWEAK PSRMLMLQLT DGIVQIQGME YQPIPILHSD LPPGTKILIY GNISFRLGVL 

       190        200        210        220        230        240 
LLKPENVKVL GGEVDALLEE YAQEKVLARL IGEPDLVVSV IPNNSNENIP RVTDVLDPAL 

       250        260        270        280        290        300 
GPSDEELLAS LDENDELTAN NDTSSERCFT TGSSSNTIPT RQSSFEPEFV ISPRPKEEPS 

       310        320        330        340        350        360 
NLSIHVMDGE LDDFSLEEAL LLEETVQKEQ METKELQPLT FNRNADRSIE RFSHNPNTTN 

       370        380        390        400        410        420 
NFSLTCKNGN NNWSEKNVSE QMTNEDKSFG CPSVRDQNRS IFSVHCNVPL AHDFTNKEKN 

       430        440        450        460        470        480 
LETDNKIKQT SSSDSHSLNN KILNREVVNY VQKRNSQISN ENDCNLQSCS LRSSENSINL 

       490        500        510        520        530        540 
SIAMDLYSPP FVYLSVLMAS KPKEVTTVKV KAFIVTLTGN LSSSGGIWSI TAKVSDGTAY 

       550        560        570        580        590        600 
LDVDFVDEIL TSLIGFSVPE MKQSKKDPLQ YQKFLEGLQK CQRDLIDLCC LMTISFNPSL 

       610        620 
SKAMVLALQD VNMEHLENLK KRLNK 

« Hide

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], VARIANT SER-455.
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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], VARIANTS HIS-100 AND SER-455.
Tissue: Brain, Skin, Testis and Uterus.
[4]"BLAP75, an essential component of Bloom's syndrome protein complexes that maintain genome integrity."
Yin J., Sobeck A., Xu C., Meetei A.R., Hoatlin M., Li L., Wang W.
EMBO J. 24:1465-1476(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN COMPLEX WITH BLM AND TOP3A, SUBCELLULAR LOCATION.
[5]"A double Holliday junction dissolvasome comprising BLM, topoisomerase III alpha, and BLAP75."
Raynard S., Bussen W., Sung P.
J. Biol. Chem. 281:13861-13864(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BLM AND TOP3A.
[6]"BLAP75/RMI1 promotes the BLM-dependent dissolution of homologous recombination intermediates."
Wu L., Bachrati C.Z., Ou J., Xu C., Yin J., Chang M., Wang W., Li L., Brown G.W., Hickson I.D.
Proc. Natl. Acad. Sci. U.S.A. 103:4068-4073(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BINDING TO DOUBLE HOLLIDAY JUNCTION, INTERACTION WITH TOP3A.
[7]"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: IDENTIFICATION IN THE RMI COMPLEX, INTERACTION WITH RMI2.
[8]"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: IDENTIFICATION IN THE RMI COMPLEX, INTERACTION WITH RMI2.
[9]"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-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase with homologous recombination repair."
Wan L., Han J., Liu T., Dong S., Xie F., Chen H., Huang J.
Proc. Natl. Acad. Sci. U.S.A. 110:10646-10651(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BLM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK022950 mRNA. Translation: BAB14325.1.
AL732446 Genomic DNA. Translation: CAI13576.1.
AL732446 Genomic DNA. Translation: CAI13575.1. Sequence problems.
BC020606 mRNA. Translation: AAH20606.1. Sequence problems.
BC032494 mRNA. Translation: AAH32494.1. Sequence problems.
BC039999 mRNA. Translation: AAH39999.1. Frameshift.
BC053549 mRNA. Translation: AAH53549.1. Sequence problems.
BC064937 mRNA. Translation: AAH64937.1. Frameshift.
CCDSCCDS6669.1.
RefSeqNP_079221.2. NM_024945.2.
XP_005252268.1. XM_005252211.1.
XP_005252270.1. XM_005252213.1.
UniGeneHs.726327.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MXNX-ray1.55A473-625[»]
3NBHX-ray2.00A475-625[»]
3NBIX-ray2.00A2-213[»]
4CGYX-ray2.85B1-219[»]
4CHTX-ray3.25B1-219[»]
4DAYX-ray3.30A473-625[»]
ProteinModelPortalQ9H9A7.
SMRQ9H9A7. Positions 2-216, 475-625.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123066. 20 interactions.
DIPDIP-33324N.
IntActQ9H9A7. 13 interactions.
MINTMINT-8048917.
STRING9606.ENSP00000317039.

PTM databases

PhosphoSiteQ9H9A7.

Polymorphism databases

DMDM322510109.

Proteomic databases

MaxQBQ9H9A7.
PaxDbQ9H9A7.
PRIDEQ9H9A7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000325875; ENSP00000317039; ENSG00000178966.
GeneID80010.
KEGGhsa:80010.
UCSCuc004anp.4. human.

Organism-specific databases

CTD80010.
GeneCardsGC09P086595.
H-InvDBHIX0008132.
HGNCHGNC:25764. RMI1.
HPACAB012247.
HPA021661.
HPA051592.
MIM610404. gene.
neXtProtNX_Q9H9A7.
PharmGKBPA134939007.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG261197.
HOVERGENHBG061190.
InParanoidQ9H9A7.
KOK10990.
OMAAMDLYSP.
OrthoDBEOG7F7W8R.
PhylomeDBQ9H9A7.
TreeFamTF316491.

Gene expression databases

BgeeQ9H9A7.
CleanExHS_RMI1.
GenevestigatorQ9H9A7.

Family and domain databases

InterProIPR013894. DUF1767.
[Graphical view]
PfamPF08585. DUF1767. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRMI1.
GenomeRNAi80010.
NextBio70103.
PROQ9H9A7.
SOURCESearch...

Entry information

Entry nameRMI1_HUMAN
AccessionPrimary (citable) accession number: Q9H9A7
Secondary accession number(s): Q05BX1 expand/collapse secondary AC list , Q05CW3, Q5SQG8, Q5SQG9, Q6P1Q4, Q6PI89, Q7Z6L6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: February 8, 2011
Last modified: July 9, 2014
This is version 102 of the entry and version 3 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM