Q9NRK6 (ABCBA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-binding cassette sub-family B member 10, mitochondrial

Alternative name(s):
ATP-binding cassette transporter 10
Short name=ABC transporter 10 protein
Mitochondrial ATP-binding cassette 2
Short name=M-ABC2

Gene names

Name:

ABCB10

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	738 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	May mediate critical mitochondrial transport functions related to heme biosynthesis By similarity.
Subunit structure	Homodimer or homooligomer. Ref.7
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein.
Tissue specificity	Ubiquitous. Highly expressed in bone marrow, expressed at intermediate to high levels in skeletal muscle, small intestine, thyroid, heart, brain, placenta, liver, pancreas, prostate, testis, ovary, leukocyte, stomach, spinal cord, lymph node, trachea and adrenal gland, and low levels are found in lung, kidney, spleen, thymus and colon.
Sequence similarities	Belongs to the ABC transporter superfamily. ABCB family. Mitochondrial peptide exporter (TC 3.A.1.212) subfamily. [View classification] Contains 1 ABC transmembrane type-1 domain. Contains 1 ABC transporter domain.

Ontologies

Keywords
Biological process	Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Polymorphism
Domain	Transit peptide Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	integral to mitochondrial membrane Inferred from direct assay Ref.1. Source: UniProtKB mitochondrial inner membrane Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW oligopeptide-transporting ATPase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 105

105

Mitochondrion

Chain

106 – 738

633

ATP-binding cassette sub-family B member 10, mitochondrial

PRO_0000000255

Regions

Topological domain

? – 170

Mitochondrial intermembrane Potential

Transmembrane

171 – 191

21

Helical; Potential

Topological domain

192 – 215

24

Mitochondrial matrix Potential

Transmembrane

216 – 236

21

Helical; Potential

Topological domain

237 – 312

76

Mitochondrial intermembrane Potential

Transmembrane

313 – 333

21

Helical; Potential

Topological domain

334 – 407

74

Mitochondrial matrix Potential

Transmembrane

408 – 428

21

Helical; Potential

Topological domain

429 – 430

2

Mitochondrial intermembrane Potential

Transmembrane

431 – 451

21

Helical; Potential

Topological domain

452 – 738

287

Mitochondrial matrix Potential

Domain

171 – 457

287

ABC transmembrane type-1

Domain

492 – 731

240

ABC transporter

Nucleotide binding

527 – 534

8

ATP Potential

Amino acid modifications

Modified residue

265

1

N6-acetyllysine Ref.8

Natural variations

Natural variant

150

1

A → S. Ref.10
Corresponds to variant rs4148756 [ dbSNP | Ensembl ].

VAR_013702

Natural variant

242

1

R → G.
Corresponds to variant rs17584642 [ dbSNP | Ensembl ].

VAR_048133

Natural variant

471

1

R → T in a breast cancer sample; somatic mutation. Ref.11

VAR_035735

Natural variant

545

1

D → N. Ref.1
Corresponds to variant rs35698797 [ dbSNP | Ensembl ].

VAR_031435

Experimental info

Sequence conflict

393

1

F → V in AAF78198. Ref.1

Sequence conflict

511

1

Q → K in AAA84438. Ref.6

Sequence conflict

558 – 563

6

IRQLNP → NPSAKPS in AAA84438. Ref.6

Sequence conflict

606 – 611

6

VAEVAN → GLKGQ in BAB20265. Ref.2

Sequence conflict

615 – 622

8

FIRNFPQG → SPEFPPR in AAA84438. Ref.6

Sequence conflict

691

1

R → S in AAA84438. Ref.6

Secondary structure

1

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738

Helix Strand Turn

Details...

Helix

154 – 164

11

Helix

165 – 167

3

Helix

168 – 185

18

Helix

188 – 201

14

Helix

208 – 255

48

Helix

260 – 265

6

Helix

268 – 285

18

Helix

288 – 310

23

Helix

312 – 359

48

Helix

361 – 366

6

Helix

370 – 422

53

Helix

428 – 469

42

Turn

485 – 487

3

Beta strand

492 – 499

8

Beta strand

502 – 504

3

Beta strand

509 – 517

9

Beta strand

522 – 526

5

Helix

530 – 540

11

Beta strand

547 – 553

7

Helix

558 – 560

3

Helix

563 – 568

6

Beta strand

569 – 573

5

Beta strand

581 – 583

3

Helix

584 – 589

6

Beta strand

592 – 594

3

Turn

595 – 597

3

Helix

600 – 609

10

Helix

613 – 617

5

Beta strand

619 – 621

3

Helix

622 – 624

3

Beta strand

628 – 631

4

Helix

636 – 650

15

Beta strand

653 – 658

6

Helix

666 – 680

15

Beta strand

683 – 688

6

Helix

692 – 697

6

Beta strand

698 – 704

7

Beta strand

706 – 713

8

Helix

715 – 719

5

Sequences

	Sequence		Length	Mass (Da)
	Q9NRK6 [UniParc]. Last modified April 3, 2007. Version 2. Checksum: C68B4FAC0F8B7E43	FASTA	738	79,148
	10 20 30 40 50 60 MRGPPAWPLR LLEPPSPAEP GRLLPVACVW AAASRVPGSL SPFTGLRPAR LWGAGPALLW 70 80 90 100 110 120 GVGAARRWRS GCRGGGPGAS RGVLGLARLL GLWARGPGSC RCGAFAGPGA PRLPRARFPG 130 140 150 160 170 180 GPAAAAWAGD EAWRRGPAAP PGDKGRLRPA AAGLPEARKL LGLAYPERRR LAAAVGFLTM 190 200 210 220 230 240 SSVISMSAPF FLGKIIDVIY TNPTVDYSDN LTRLCLGLSA VFLCGAAANA IRVYLMQTSG 250 260 270 280 290 300 QRIVNRLRTS LFSSILRQEV AFFDKTRTGE LINRLSSDTA LLGRSVTENL SDGLRAGAQA 310 320 330 340 350 360 SVGISMMFFV SPNLATFVLS VVPPVSIIAV IYGRYLRKLT KVTQDSLAQA TQLAEERIGN 370 380 390 400 410 420 VRTVRAFGKE MTEIEKYASK VDHVMQLARK EAFARAGFFG ATGLSGNLIV LSVLYKGGLL 430 440 450 460 470 480 MGSAHMTVGE LSSFLMYAFW VGISIGGLSS FYSELMKGLG AGGRLWELLE REPKLPFNEG 490 500 510 520 530 540 VILNEKSFQG ALEFKNVHFA YPARPEVPIF QDFSLSIPSG SVTALVGPSG SGKSTVLSLL 550 560 570 580 590 600 LRLYDPASGT ISLDGHDIRQ LNPVWLRSKI GTVSQEPILF SCSIAENIAY GADDPSSVTA 610 620 630 640 650 660 EEIQRVAEVA NAVAFIRNFP QGFNTVVGEK GVLLSGGQKQ RIAIARALLK NPKILLLDEA 670 680 690 700 710 720 TSALDAENEY LVQEALDRLM DGRTVLVIAH RLSTIKNANM VAVLDQGKIT EYGKHEELLS 730 KPNGIYRKLM NKQSFISA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"M-ABC2, a new human mitochondrial ATP-binding cassette membrane protein." Zhang F., Hogue D.L., Liu L., Fisher C.L., Hui D., Childs S., Ling V. FEBS Lett. 478:89-94(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-545. Tissue: Lymphoblast.
[2]	"Human mono ATP-binding cassette protein." Ito K., Suzuki H., Sugiyama Y. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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]. Tissue: Eye.
[6]	"Characterization and mapping of three new mammalian ATP-binding transporter genes from an EST database." Allikmets R., Gerrard B., Glavac D., Ravnik-Glavac M., Jenkins N.A., Gilbert D.J., Copeland N.G., Modi W., Dean M. Mamm. Genome 6:114-117(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 510-738.
[7]	"Targeting, import, and dimerization of a mammalian mitochondrial ATP binding cassette (ABC) transporter, ABCB10 (ABC-me)." Graf S.A., Haigh S.E., Corson E.D., Shirihai O.S. J. Biol. Chem. 279:42954-42963(2004) [PubMed] [Europe PMC] [Abstract] Cited for: TRANSIT PEPTIDE, SUBUNIT.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265, MASS SPECTROMETRY.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Three hundred twenty-six genetic variations in genes encoding nine members of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the Japanese population." Saito S., Iida A., Sekine A., Miura Y., Ogawa C., Kawauchi S., Higuchi S., Nakamura Y. J. Hum. Genet. 47:38-50(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SER-150.
[11]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-471.
+	Additional computationally mapped references.

Web resources

ABCMdb

Database for mutations in ABC proteins

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF216833 mRNA. Translation: AAF78198.1.
AB013380 mRNA. Translation: BAB20265.1.
AL121990 Genomic DNA. Translation: CAI22012.1.
CH471098 Genomic DNA. Translation: EAW69901.1.
BC064930 mRNA. Translation: AAH64930.1.
U18237 mRNA. Translation: AAA84438.1.

IPI

IPI00015826.

RefSeq

NP_036221.2. NM_012089.2.

UniGene

Hs.17614.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ZDQ	X-ray	2.85	A	152-738	[»]
4AYT	X-ray	2.85	A	152-738	[»]
4AYW	X-ray	3.30	A	126-738	[»]
4AYX	X-ray	2.90	A	152-738	[»]

ProteinModelPortal

Q9NRK6.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NRK6. 1 interaction.

STRING

9606.ENSP00000355637.

PTM databases

PhosphoSite

Q9NRK6.

Polymorphism databases

DMDM

143811359.

Proteomic databases

PaxDb

Q9NRK6.

PRIDE

Q9NRK6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000344517; ENSP00000355637; ENSG00000135776.

GeneID

23456.

KEGG

hsa:23456.

UCSC

uc001htp.4. human.

Organism-specific databases

CTD

23456.

GeneCards

GC01M229652.

H-InvDB

HIX0028493.

HGNC

HGNC:41. ABCB10.

HPA

CAB044063.
CAB044065.

MIM

605454. gene.

neXtProt

NX_Q9NRK6.

PharmGKB

PA24385.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1132.

HOVERGEN

HBG008358.

InParanoid

Q9NRK6.

KO

K05657.

OMA

KESATQN.

OrthoDB

EOG42BX88.

PhylomeDB

Q9NRK6.

Enzyme and pathway databases

BRENDA

3.6.3.43. 2681.

Reactome

REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpress

Q9NRK6.

Bgee

Q9NRK6.

CleanEx

HS_ABCB10.

Genevestigator

Q9NRK6.

GermOnline

ENSG00000135776. Homo sapiens.

Family and domain databases

InterPro

IPR003593. AAA+_ATPase.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR017940. ABC_transporter_type1.
IPR001140. ABC_transptr_TM_dom.
IPR011527. ABC_transptrTM_dom_typ1.
[Graphical view]

Pfam

PF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 1 hit.
[Graphical view]

SUPFAM

SSF90123. ABC_TM_1. 1 hit.

PROSITE

PS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

23456.

NextBio

45747.

SOURCE

Search...

Entry information

Entry name

ABCBA_HUMAN

Accession

Primary (citable) accession number: Q9NRK6
Secondary accession number(s): Q13040, Q6P1Q8, Q9H3V0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	April 3, 2007
Last modified:	May 1, 2013
This is version 115 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.