Q9H9A7 (RMI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	625 AA.
Sequence status	Complete.
Protein existence	Evidence 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, BLM and TOP3A. May bind DHJ. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8
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 process	DNA replication
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BLM	P54132	7	EBI-621339,EBI-621372

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 625

625

RecQ-mediated genome instability protein 1

PRO_0000227546

Amino acid modifications

Modified residue

225

1

Phosphoserine Ref.9

Natural variations

Natural variant

100

1

Y → H. Ref.3
Corresponds to variant rs17855932 [ dbSNP | Ensembl ].

VAR_025556

Natural variant

455

1

N → S. Ref.1 Ref.3
Corresponds to variant rs1982151 [ dbSNP | Ensembl ].

VAR_025557

Experimental info

Sequence conflict

11

1

E → G in BAB14325. Ref.1

Sequence conflict

259

1

A → T in BAB14325. Ref.1

Sequence conflict

318

1

E → D in AAH20606. Ref.3

Sequence conflict

443

1

L → F in AAH39999. Ref.3

Secondary structure

1

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625

Helix Strand Turn

Details...

Helix

3 – 18

16

Helix

24 – 38

15

Helix

45 – 57

13

Helix

61 – 64

4

Turn

71 – 75

5

Beta strand

77 – 95

19

Helix

96 – 108

13

Beta strand

135 – 143

9

Beta strand

145 – 150

6

Beta strand

166 – 176

11

Beta strand

179 – 182

4

Helix

184 – 186

3

Beta strand

187 – 191

5

Helix

195 – 201

7

Helix

480 – 482

3

Helix

483 – 487

5

Helix

494 – 499

6

Beta strand

506 – 517

12

Helix

524 – 526

3

Beta strand

531 – 535

5

Beta strand

540 – 545

6

Helix

547 – 554

8

Helix

558 – 564

7

Helix

568 – 587

20

Beta strand

589 – 597

9

Turn

598 – 601

4

Beta strand

602 – 609

8

Helix

613 – 622

10

Sequences

	Sequence		Length	Mass (Da)
	Q9H9A7 [UniParc]. Last modified February 8, 2011. Version 3. Checksum: 2BB449363DBF76B7	FASTA	625	70,144
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	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.

IPI

IPI00017203.

RefSeq

NP_079221.2. NM_024945.2.

UniGene

Hs.726327.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3MXN	X-ray	1.55	A	473-625	[»]
3NBH	X-ray	2.00	A	475-625	[»]
3NBI	X-ray	2.00	A	2-213	[»]
4DAY	X-ray	3.30	A	473-625	[»]

ProteinModelPortal

Q9H9A7.

SMR

Q9H9A7. Positions 2-204, 475-625.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33324N.

IntAct

Q9H9A7. 7 interactions.

STRING

9606.ENSP00000317039.

PTM databases

PhosphoSite

Q9H9A7.

Polymorphism databases

DMDM

90111982.

Proteomic databases

PaxDb

Q9H9A7.

PRIDE

Q9H9A7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000325875; ENSP00000317039; ENSG00000178966.
ENST00000445877; ENSP00000402433; ENSG00000178966.

GeneID

80010.

KEGG

hsa:80010.

UCSC

uc004anp.4. human.

Organism-specific databases

CTD

80010.

GeneCards

GC09P086595.

H-InvDB

HIX0008132.

HGNC

HGNC:25764. RMI1.

HPA

CAB012247.
HPA021661.
HPA051592.

MIM

610404. gene.

neXtProt

NX_Q9H9A7.

PharmGKB

PA134939007.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG261197.

HOVERGEN

HBG061190.

InParanoid

Q9H9A7.

KO

K10990.

OMA

TPKPWEA.

OrthoDB

EOG4XKV7M.

PhylomeDB

Q9H9A7.

Gene expression databases

Bgee

Q9H9A7.

CleanEx

HS_RMI1.

Genevestigator

Q9H9A7.

GermOnline

ENSG00000178966. Homo sapiens.

Family and domain databases

InterPro

IPR013894. DUF1767.
[Graphical view]

Pfam

PF08585. DUF1767. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

80010.

NextBio

70103.

SOURCE

Search...

Entry information

Entry name

RMI1_HUMAN

Accession

Primary (citable) accession number: Q9H9A7
Secondary accession number(s): Q05BX1 , Q05CW3, Q5SQG8, Q5SQG9, Q6P1Q4, Q6PI89, Q7Z6L6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	February 8, 2011
Last modified:	May 1, 2013
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.