Q96E14 (RMI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. 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 process	DNA replication
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
PTM	Acetylation 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	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular_function	DNA 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 147

146

RecQ-mediated genome instability protein 2

PRO_0000297577

Regions

DNA binding

44 – 114

71

OB

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.7

Modified residue

7

1

Phosphoserine Ref.7

Natural variations

Alternative sequence

1 – 98

98

MAAAA…PCLVP → MKQTQVGSLFSLGIRNPEPG PVSGTAVPRQLAWKS in isoform 2.

VSP_027287

Experimental info

Mutagenesis

24

1

K → A: Abolishes interaction with RMI1, TOP3A and BLM. Ref.6

Mutagenesis

59

1

W → 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

Mutagenesis

100

1

K → A: Does not affect interaction with RMI1, TOP3A and BLM. Ref.6

Mutagenesis

121

1

K → 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

Mutagenesis

135

1

W → A: Abolishes interaction with RMI1, TOP3A and BLM. Ref.6

Secondary structure

1

.

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147

Helix Strand Turn

Details...

Helix

27 – 33

7

Beta strand

34 – 36

3

Beta strand

40 – 43

4

Turn

46 – 49

4

Beta strand

56 – 68

13

Beta strand

71 – 76

6

Beta strand

79 – 84

6

Helix

86 – 88

3

Beta strand

92 – 94

3

Beta strand

101 – 110

10

Beta strand

112 – 114

3

Beta strand

116 – 124

9

Helix

130 – 143

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2004. Version 2. Checksum: C385825F9AB4439E	FASTA	147	15,865
	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
	Isoform 2 [UniParc]. Checksum: DAFD4A80EF28023B	FASTA	84	9,262
	10 20 30 40 50 60 MKQTQVGSLF SLGIRNPEPG PVSGTAVPRQ LAWKSGKYVM VMGVVQACSP EPCLQAVKMT 70 80 DLSDNPIHES MWELEVEDLH RNIP

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] (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]	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. , 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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma.
+	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.

IPI

IPI00061111.
IPI00647591.

RefSeq

NP_689521.1. NM_152308.1.

UniGene

Hs.347524.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q96E14.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-56480N.

IntAct

Q96E14. 3 interactions.

STRING

9606.ENSP00000310356.

PTM databases

PhosphoSite

Q96E14.

Polymorphism databases

DMDM

74731517.

Proteomic databases

PaxDb

Q96E14.

PRIDE

Q96E14.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000312499; ENSP00000310356; ENSG00000175643.
ENST00000381820; ENSP00000371241; ENSG00000175643.
ENST00000572173; ENSP00000461206; ENSG00000175643.

GeneID

116028.

KEGG

hsa:116028.

UCSC

uc002daw.1. human.

Organism-specific databases

CTD

116028.

GeneCards

GC16P011343.

H-InvDB

HIX0012817.

HGNC

HGNC:28349. RMI2.

HPA

HPA040995.

MIM

612426. gene.

neXtProt

NX_Q96E14.

PharmGKB

PA145149635.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG27893.

HOGENOM

HOG000154149.

HOVERGEN

HBG108410.

InParanoid

Q96E14.

KO

K15365.

OMA

AAVWMQG.

OrthoDB

EOG44XJJ2.

PhylomeDB

Q96E14.

Gene expression databases

ArrayExpress

Q96E14.

Bgee

Q96E14.

CleanEx

HS_C16orf75.

Genevestigator

Q96E14.

Family and domain databases

ProtoNet

Search...

Other

ChiTaRS

RMI2. human.

GenomeRNAi

116028.

NextBio

79725.

SOURCE

Search...

Entry information

Entry name

RMI2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 82 of the entry and version 2 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.