Q9NP58 (ABCB6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-binding cassette sub-family B member 6, mitochondrial

Alternative name(s):
Mitochondrial ABC transporter 3
Short name=Mt-ABC transporter 3
P-glycoprotein-related protein
Ubiquitously-expressed mammalian ABC half transporter

Gene names

Name:	ABCB6
Synonyms:	MTABC3, PRP, UMAT

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	842 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds heme and porphyrins and functions in their ATP-dependent uptake into the mitochondria. Plays a crucial role in heme synthesis. Ref.1 Ref.8
Subunit structure	Homodimer. Ref.8
Subcellular location	Cell membrane. Mitochondrion outer membrane; Multi-pass membrane protein. Endoplasmic reticulum. Golgi apparatus Ref.1 Ref.8 Ref.9 Ref.10 Ref.11.
Tissue specificity	Widely expressed. High expression is detected in the retinal epithelium. Ref.1 Ref.11
Developmental stage	Highly expressed in fetal liver. Ref.8
Induction	Up-regulated by cellular porphyrins (at protein level). Ref.8
Polymorphism	Genetic variations in ABCB6 define the Langereis blood group system (LAN) [MIM:111600]. Individuals with Lan- blood group lack the Lan antigen on their red blood cells. These individuals may have anti-Lan antibodies in their serum, which can cause transfusion reactions or hemolytic disease of the fetus or newborn. The Lan- blood group is only clinically significant in transfusion settings or during pregnancy; otherwise Lan- individuals have no clinical features.
Involvement in disease	Microphthalmia, isolated, with coloboma, 7 (MCOPCB7) [MIM:614497]: A disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues. Ocular abnormalities like opacities of the cornea and lens, scaring of the retina and choroid, cataract and other abnormalities like cataract may also be present. Ocular colobomas are a set of malformations resulting from abnormal morphogenesis of the optic cup and stalk, and the fusion of the fetal fissure (optic fissure). Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11
Miscellaneous	Depletion of Abcb6 by RNAi abrogates heme biosynthesis. Overexpression enhances porphyrin biosynthesis.
Sequence similarities	Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily. [View classification] Contains 1 ABC transmembrane type-1 domain. Contains 1 ABC transporter domain.
Sequence caution	The sequence AAG33617.1 differs from that shown. Reason: Erroneous initiation. The sequence AAG33618.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH43423.1 differs from that shown. Reason: Intron retention. The sequence BAD18782.1 differs from that shown. Reason: Erroneous termination at position 168. Translated as Trp. The sequence BAD92291.1 differs from that shown. Reason: Chimeric cDNA. Isoform 2: The sequence BAB71347.1 differs from that shown. Reason: splicing through aberrant splice sites

Ontologies

Keywords
Biological process	Transport
Cellular component	Cell membrane Endoplasmic reticulum Golgi apparatus Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Microphthalmia
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	brain development Inferred from mutant phenotype PubMed 22100072. Source: UniProtKB cadmium ion transmembrane transport Inferred from Biological aspect of Ancestor. Source: RefGenome cellular iron ion homeostasis Non-traceable author statement PubMed 11977179. Source: UniProtKB detoxification of cadmium ion Inferred from Biological aspect of Ancestor. Source: RefGenome porphyrin-containing compound biosynthetic process Inferred from direct assay Ref.8. Source: UniProtKB skin development Inferred from mutant phenotype PubMed 22100072. Source: UniProtKB
Cellular_component	ATP-binding cassette (ABC) transporter complex Non-traceable author statement Ref.2. Source: UniProtKB Golgi apparatus Inferred from direct assay Ref.10Ref.11. Source: UniProtKB endoplasmic reticulum Inferred from direct assay Ref.11. Source: UniProtKB integral to mitochondrial outer membrane Inferred from direct assay Ref.9. Source: UniProtKB plasma membrane Inferred from direct assay Ref.9. Source: UniProtKB vacuolar membrane Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	ATP binding Inferred from direct assay Ref.1. Source: MGI efflux transmembrane transporter activity Inferred from direct assay Ref.9. Source: UniProtKB heme binding Inferred from direct assay Ref.8. Source: UniProtKB heme-transporting ATPase activity Inferred from mutant phenotype Ref.8. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NP58-1)

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: Q9NP58-4)

The sequence of this isoform differs from the canonical sequence as follows:
     183-228: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 842

842

ATP-binding cassette sub-family B member 6, mitochondrial

PRO_0000000248

Regions

Transmembrane

27 – 47

21

Helical; Potential

Transmembrane

73 – 93

21

Helical; Potential

Transmembrane

107 – 127

21

Helical; Potential

Transmembrane

148 – 168

21

Helical; Potential

Transmembrane

186 – 206

21

Helical; Potential

Transmembrane

265 – 285

21

Helical; Potential

Transmembrane

376 – 396

21

Helical; Potential

Transmembrane

409 – 431

23

Helical; Potential

Transmembrane

502 – 522

21

Helical; Potential

Transmembrane

530 – 550

21

Helical; Potential

Domain

265 – 556

292

ABC transmembrane type-1

Domain

590 – 824

235

ABC transporter

Nucleotide binding

623 – 630

8

ATP Potential

Natural variations

Alternative sequence

183 – 228

46

Missing in isoform 2.

VSP_021973

Natural variant

57

1

A → T in MCOPCB7; hypomorphic mutation. Ref.11

VAR_067394

Natural variant

69

1

R → G in a breast cancer sample; somatic mutation. Ref.14

VAR_035732

Natural variant

293

1

L → V.
Corresponds to variant rs13018440 [ dbSNP | Ensembl ].

VAR_047552

Natural variant

343

1

R → Q.
Corresponds to variant rs60322991 [ dbSNP | Ensembl ].

VAR_060986

Natural variant

648

1

R → Q.
Corresponds to variant rs13402964 [ dbSNP | Ensembl ].

VAR_029749

Natural variant

811

1

L → V in MCOPCB7; hypomorphic mutation. Ref.11

VAR_067395

Experimental info

Sequence conflict

170

1

S → N in AAG33618. Ref.2

Sequence conflict

320

1

T → S in BAD18782. Ref.4

Sequence conflict

413

1

F → S in BAD18782. Ref.4

Sequence conflict

616

1

G → E in BAD18782. Ref.4

Sequence conflict

638

1

R → L in BAD18782. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

842

Helix Strand Turn

Details...

Helix

561 – 572

12

Beta strand

590 – 600

11

Beta strand

604 – 613

10

Beta strand

618 – 625

8

Helix

628 – 636

9

Beta strand

643 – 649

7

Helix

654 – 656

3

Helix

659 – 664

6

Beta strand

666 – 669

4

Beta strand

677 – 679

3

Helix

680 – 685

6

Helix

693 – 702

10

Helix

706 – 711

6

Helix

715 – 717

3

Beta strand

719 – 721

3

Helix

729 – 743

15

Beta strand

746 – 751

6

Helix

759 – 773

15

Beta strand

776 – 781

6

Helix

785 – 789

5

Beta strand

792 – 798

7

Beta strand

801 – 806

6

Helix

808 – 814

7

Helix

817 – 826

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: E63A7D59DCE5B9ED	FASTA	842	93,886
	10 20 30 40 50 60 MVTVGNYCEA EGPVGPAWMQ DGLSPCFFFT LVPSTRMALG TLALVLALPC RRRERPAGAD 70 80 90 100 110 120 SLSWGAGPRI SPYVLQLLLA TLQAALPLAG LAGRVGTARG APLPSYLLLA SVLESLAGAC 130 140 150 160 170 180 GLWLLVVERS QARQRLAMGI WIKFRHSPGL LLLWTVAFAA ENLALVSWNS PQWWWARADL 190 200 210 220 230 240 GQQVQFSLWV LRYVVSGGLF VLGLWAPGLR PQSYTLQVHE EDQDVERSQV RSAAQQSTWR 250 260 270 280 290 300 DFGRKLRLLS GYLWPRGSPA LQLVVLICLG LMGLERALNV LVPIFYRNIV NLLTEKAPWN 310 320 330 340 350 360 SLAWTVTSYV FLKFLQGGGT GSTGFVSNLR TFLWIRVQQF TSRRVELLIF SHLHELSLRW 370 380 390 400 410 420 HLGRRTGEVL RIADRGTSSV TGLLSYLVFN VIPTLADIII GIIYFSMFFN AWFGLIVFLC 430 440 450 460 470 480 MSLYLTLTIV VTEWRTKFRR AMNTQENATR ARAVDSLLNF ETVKYYNAES YEVERYREAI 490 500 510 520 530 540 IKYQGLEWKS SASLVLLNQT QNLVIGLGLL AGSLLCAYFV TEQKLQVGDY VLFGTYIIQL 550 560 570 580 590 600 YMPLNWFGTY YRMIQTNFID MENMFDLLKE ETEVKDLPGA GPLRFQKGRI EFENVHFSYA 610 620 630 640 650 660 DGRETLQDVS FTVMPGQTLA LVGPSGAGKS TILRLLFRFY DISSGCIRID GQDISQVTQA 670 680 690 700 710 720 SLRSHIGVVP QDTVLFNDTI ADNIRYGRVT AGNDEVEAAA QAAGIHDAIM AFPEGYRTQV 730 740 750 760 770 780 GERGLKLSGG EKQRVAIART ILKAPGIILL DEATSALDTS NERAIQASLA KVCANRTTIV 790 800 810 820 830 840 VAHRLSTVVN ADQILVIKDG CIVERGRHEA LLSRGGVYAD MWQLQQGQEE TSEDTKPQTM ER
	Isoform 2 [UniParc]. Checksum: A72DFA31D8C77FFE	FASTA	796	88,600
	10 20 30 40 50 60 MVTVGNYCEA EGPVGPAWMQ DGLSPCFFFT LVPSTRMALG TLALVLALPC RRRERPAGAD 70 80 90 100 110 120 SLSWGAGPRI SPYVLQLLLA TLQAALPLAG LAGRVGTARG APLPSYLLLA SVLESLAGAC 130 140 150 160 170 180 GLWLLVVERS QARQRLAMGI WIKFRHSPGL LLLWTVAFAA ENLALVSWNS PQWWWARADL 190 200 210 220 230 240 GQQVRSAAQQ STWRDFGRKL RLLSGYLWPR GSPALQLVVL ICLGLMGLER ALNVLVPIFY 250 260 270 280 290 300 RNIVNLLTEK APWNSLAWTV TSYVFLKFLQ GGGTGSTGFV SNLRTFLWIR VQQFTSRRVE 310 320 330 340 350 360 LLIFSHLHEL SLRWHLGRRT GEVLRIADRG TSSVTGLLSY LVFNVIPTLA DIIIGIIYFS 370 380 390 400 410 420 MFFNAWFGLI VFLCMSLYLT LTIVVTEWRT KFRRAMNTQE NATRARAVDS LLNFETVKYY 430 440 450 460 470 480 NAESYEVERY REAIIKYQGL EWKSSASLVL LNQTQNLVIG LGLLAGSLLC AYFVTEQKLQ 490 500 510 520 530 540 VGDYVLFGTY IIQLYMPLNW FGTYYRMIQT NFIDMENMFD LLKEETEVKD LPGAGPLRFQ 550 560 570 580 590 600 KGRIEFENVH FSYADGRETL QDVSFTVMPG QTLALVGPSG AGKSTILRLL FRFYDISSGC 610 620 630 640 650 660 IRIDGQDISQ VTQASLRSHI GVVPQDTVLF NDTIADNIRY GRVTAGNDEV EAAAQAAGIH 670 680 690 700 710 720 DAIMAFPEGY RTQVGERGLK LSGGEKQRVA IARTILKAPG IILLDEATSA LDTSNERAIQ 730 740 750 760 770 780 ASLAKVCANR TTIVVAHRLS TVVNADQILV IKDGCIVERG RHEALLSRGG VYADMWQLQQ 790 GQEETSEDTK PQTMER

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MTABC3, a novel mitochondrial ATP-binding cassette protein involved in iron homeostasis." Mitsuhashi N., Miki T., Senbongi H., Yokoi N., Yano H., Miyazaki M., Nakajima N., Iwanaga T., Yokoyama Y., Shibata T., Seino S. J. Biol. Chem. 275:17536-17540(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]	"Isolation of a genomic clone containing the promoter region of the human ATP binding cassette (ABC) transporter, ABCB6." Emadi-Konjin H.-P., Zhang H., Anandan V., Sun D., Schuetz J.D., Furuya K.N. Biochim. Biophys. Acta 1574:117-130(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-229. Tissue: Colon and Liver.
[3]	"Subcellular localization of the ABC transporter umat." Hirsch-Ernst K.I., Schaefer A., Ernst B.-P., Schmitz-Salue C., Awuah D., Kahl G.F. Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 112-842 (ISOFORM 1). Tissue: Hepatoma and Neuroepithelium.
[5]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[6]	"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] (ISOFORM 1). Tissue: Brain.
[7]	Yu W., Gibbs R.A. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 332-842 (ISOFORM 1). Tissue: Brain.
[8]	"Identification of a mammalian mitochondrial porphyrin transporter." Krishnamurthy P.C., Du G., Fukuda Y., Sun D., Sampath J., Mercer K.E., Wang J., Sosa-Pineda B., Murti K.G., Schuetz J.D. Nature 443:586-589(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE, INDUCTION BY CELLULAR PORPHYRINS, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH HEMIN.
[9]	"Human ABCB6 localizes to both the outer mitochondrial membrane and the plasma membrane." Paterson J.K., Shukla S., Black C.M., Tachiwada T., Garfield S., Wincovitch S., Ernst D.N., Agadir A., Li X., Ambudkar S.V., Szakacs G., Akiyama S., Gottesman M.M. Biochemistry 46:9443-9452(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[10]	"Human ABC transporter isoform B6 (ABCB6) localizes primarily in the Golgi apparatus." Tsuchida M., Emi Y., Kida Y., Sakaguchi M. Biochem. Biophys. Res. Commun. 369:369-375(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[11]	"ABCB6 mutations cause ocular coloboma." Wang L., He F., Bu J., Liu X., Du W., Dong J., Cooney J.D., Dubey S.K., Shi Y., Gong B., Li J., McBride P.F., Jia Y., Lu F., Soltis K.A., Lin Y., Namburi P., Liang C. , Sundaresan P., Paw B.H., Li D.Y., Phillips J.D., Yang Z. Am. J. Hum. Genet. 90:40-48(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS MCOPCB7 THR-57 AND VAL-811, CHARACTERIZATION OF VARIANTS MCOPCB7 THR-57 AND VAL-811.
[12]	"ABCB6 is dispensable for erythropoiesis and specifies the new blood group system Langereis." Helias V., Saison C., Ballif B.A., Peyrard T., Takahashi J., Takahashi H., Tanaka M., Deybach J.C., Puy H., Le Gall M., Sureau C., Pham B.N., Le Pennec P.Y., Tani Y., Cartron J.P., Arnaud L. Nat. Genet. 44:170-173(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN LANGEREIS BLOOD GROUP SYSTEM.
[13]	"Heteronuclear multidimensional NMR and homology modelling studies of the C-terminal nucleotide-binding domain of the human mitochondrial ABC transporter ABCB6." Kurashima-Ito K., Ikeya T., Senbongi H., Tochio H., Mikawa T., Shibata T., Ito Y. J. Biomol. NMR 35:53-71(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 558-842 IN COMPLEX WITH ADP.
[14]	"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] GLY-69.
+	Additional computationally mapped references.

Web resources

ABCMdb

Database for mutations in ABC proteins

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB039371 Genomic DNA. Translation: BAA96733.1.
AF076775 mRNA. Translation: AAF75107.1.
AF308472 mRNA. Translation: AAG33617.1. Different initiation.
AF308473 Genomic DNA. Translation: AAG33618.1. Different initiation.
AJ289233 mRNA. Translation: CAB95766.2.
AK057026 mRNA. Translation: BAB71347.1. Sequence problems.
AK172812 mRNA. Translation: BAD18782.1. Sequence problems.
AB209054 mRNA. Translation: BAD92291.1. Sequence problems.
BC000559 mRNA. Translation: AAH00559.1.
BC043423 mRNA. Translation: AAH43423.1. Sequence problems.
AF070598 mRNA. Translation: AAC28653.1.

IPI

IPI00065486.
IPI00742677.

RefSeq

NP_005680.1. NM_005689.2.

UniGene

Hs.107911.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3NH6	X-ray	2.00	A	558-842	[»]
3NH9	X-ray	2.10	A	558-842	[»]
3NHA	X-ray	2.10	A	558-842	[»]
3NHB	X-ray	2.15	A	558-842	[»]

ProteinModelPortal

Q9NP58.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NP58. 3 interactions.

MINT

MINT-3071268.

STRING

9606.ENSP00000265316.

Protein family/group databases

TCDB

3.A.1.210.6. ATP-binding cassette (ABC) superfamily.

PTM databases

PhosphoSite

Q9NP58.

Polymorphism databases

DMDM

13123949.

Proteomic databases

PaxDb

Q9NP58.

PRIDE

Q9NP58.

Protocols and materials databases

DNASU

10058.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265316; ENSP00000265316; ENSG00000115657.
ENST00000439002; ENSP00000394333; ENSG00000115657.

GeneID

10058.

KEGG

hsa:10058.

UCSC

uc002vkc.2. human.
uc010fwe.2. human.

Organism-specific databases

CTD

10058.

GeneCards

GC02M220038.

HGNC

HGNC:47. ABCB6.

HPA

HPA046723.

MIM

111600. phenotype.
605452. gene.
614497. phenotype.

neXtProt

NX_Q9NP58.

Orphanet

98938. Colobomatous microphthalmia.
194. Ocular coloboma.

PharmGKB

PA24388.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5265.

HOVERGEN

HBG080810.

InParanoid

Q9NP58.

KO

K05661.

OMA

YEVERYR.

OrthoDB

EOG45QHCP.

PhylomeDB

Q9NP58.

Enzyme and pathway databases

Reactome

REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpress

Q9NP58.

Bgee

Q9NP58.

CleanEx

HS_ABCB6.

Genevestigator

Q9NP58.

GermOnline

ENSG00000115657. 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.
IPR027417. P-loop_NTPase.
[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.
SSF52540. SSF52540. 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

BindingDB

Q9NP58.

ChEMBL

CHEMBL2007630.

ChiTaRS

ABCB6. human.

EvolutionaryTrace

Q9NP58.

GenomeRNAi

10058.

NextBio

38003.

SOURCE

Search...

Entry information

Entry name

ABCB6_HUMAN

Accession

Primary (citable) accession number: Q9NP58
Secondary accession number(s): O75542 , Q49A66, Q59GQ5, Q6ZME6, Q96ME8, Q9HAQ6, Q9HAQ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	October 1, 2000
Last modified:	May 29, 2013
This is version 129 of the entry and version 1 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.