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Q9NP58 (ABCB6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length842 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Endosome By similarity. Note: localized to the endosome-like compartement and dendrite tips. 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, and other abnormalities 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

Dyschromatosis universalis hereditaria 3 (DUH3) [MIM:615402]: An autosomal dominant pigmentary genodermatosis characterized by a mixture of hyperpigmented and hypopigmented macules distributed randomly over the body, that appear in infancy or early childhood. The trunk and extremities are the dominant sites of abnormal pigmentation. Facial lesions can be seen in 50% of affected individuals, but involvement of palms and soles is unusual. Abnormalities of hair and nails have also been reported. Dyschromatosis universalis hereditaria may be associated with abnormalities of dermal connective tissue, nerve tissue, or other systemic complications.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15

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. Translation N-terminally shortened.

The sequence AAG33618.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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 processTransport
   Cellular componentCell membrane
Endoplasmic reticulum
Endosome
Golgi apparatus
Membrane
Mitochondrion
Mitochondrion outer membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Dyskeratosis congenita
Microphthalmia
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrain 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

heme transport

Inferred from direct assay Ref.9. Source: UniProtKB

porphyrin-containing compound biosynthetic process

Inferred from direct assay Ref.8. Source: UniProtKB

skin development

Inferred from mutant phenotype PubMed 22100072. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

transport

Inferred from direct assay Ref.1. Source: MGI

   Cellular_componentATP-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

endosome

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

integral component of mitochondrial outer membrane

Inferred from direct assay Ref.9. Source: UniProtKB

mitochondrial envelope

Inferred from direct assay Ref.1. Source: MGI

mitochondrial outer membrane

Inferred from direct assay Ref.8. Source: UniProtKB

mitochondrion

Inferred from direct assay Ref.1. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.9. Source: UniProtKB

vacuolar membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionATP 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 transporter activity

Traceable author statement. Source: Reactome

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 842842ATP-binding cassette sub-family B member 6, mitochondrial
PRO_0000000248

Regions

Transmembrane27 – 4721Helical; Potential
Transmembrane73 – 9321Helical; Potential
Transmembrane107 – 12721Helical; Potential
Transmembrane148 – 16821Helical; Potential
Transmembrane186 – 20621Helical; Potential
Transmembrane265 – 28521Helical; Potential
Transmembrane376 – 39621Helical; Potential
Transmembrane409 – 43123Helical; Potential
Transmembrane502 – 52221Helical; Potential
Transmembrane530 – 55021Helical; Potential
Domain265 – 556292ABC transmembrane type-1
Domain590 – 824235ABC transporter
Nucleotide binding623 – 6308ATP Potential

Natural variations

Alternative sequence183 – 22846Missing in isoform 2.
VSP_021973
Natural variant571A → T in MCOPCB7; hypomorphic mutation. Ref.11
VAR_067394
Natural variant691R → G in a breast cancer sample; somatic mutation. Ref.14
VAR_035732
Natural variant1701S → G in DUH3; the protein is retained in the Golgi apparatus. Ref.15
VAR_070602
Natural variant2931L → V.
Corresponds to variant rs13018440 [ dbSNP | Ensembl ].
VAR_047552
Natural variant3431R → Q.
Corresponds to variant rs60322991 [ dbSNP | Ensembl ].
VAR_060986
Natural variant3561L → P in DUH3; the protein is retained in the Golgi apparatus. Ref.15
VAR_070603
Natural variant5791G → E in DUH3; the protein is retained in the Golgi apparatus. Ref.15
VAR_070604
Natural variant6481R → Q.
Corresponds to variant rs13402964 [ dbSNP | Ensembl ].
VAR_029749
Natural variant8111L → V in MCOPCB7; hypomorphic mutation. Ref.11
VAR_067395

Experimental info

Sequence conflict1701S → N in AAG33618. Ref.2
Sequence conflict3201T → S in BAD18782. Ref.4
Sequence conflict4131F → S in BAD18782. Ref.4
Sequence conflict6161G → E in BAD18782. Ref.4
Sequence conflict6381R → L in BAD18782. Ref.4

Secondary structure

................................................ 842
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: E63A7D59DCE5B9ED

FASTA84293,886
        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 

« Hide

Isoform 2 [UniParc].

Checksum: A72DFA31D8C77FFE
Show »

FASTA79688,600

References

« Hide '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. 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] (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. expand/collapse author list , 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. expand/collapse author list , 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.
[15]"Mutations in ABCB6 cause dyschromatosis universalis hereditaria."
Zhang C., Li D., Zhang J., Chen X., Huang M., Archacki S., Tian Y., Ren W., Mei A., Zhang Q., Fang M., Su Z., Yin Y., Liu D., Chen Y., Cui X., Li C., Yang H. expand/collapse author list , Wang Q., Wang J., Liu M., Deng Y.
J. Invest. Dermatol. 133:2221-2228(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DUH3 GLY-170; PRO-356 AND GLU-579, CHARACTERIZATION OF VARIANTS DUH3 GLY-170; PRO-356 AND GLU-579.
+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.
RefSeqNP_005680.1. NM_005689.2.
UniGeneHs.107911.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3NH6X-ray2.00A558-842[»]
3NH9X-ray2.10A558-842[»]
3NHAX-ray2.10A558-842[»]
3NHBX-ray2.15A558-842[»]
ProteinModelPortalQ9NP58.
SMRQ9NP58. Positions 239-828.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115369. 4 interactions.
IntActQ9NP58. 3 interactions.
MINTMINT-3071268.
STRING9606.ENSP00000265316.

Chemistry

BindingDBQ9NP58.
ChEMBLCHEMBL2007630.

Protein family/group databases

TCDB3.A.1.210.6. the atp-binding cassette (abc) superfamily.

PTM databases

PhosphoSiteQ9NP58.

Polymorphism databases

DMDM13123949.

Proteomic databases

PaxDbQ9NP58.
PRIDEQ9NP58.

Protocols and materials databases

DNASU10058.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265316; ENSP00000265316; ENSG00000115657. [Q9NP58-1]
ENST00000439002; ENSP00000394333; ENSG00000115657. [Q9NP58-4]
GeneID10058.
KEGGhsa:10058.
UCSCuc002vkc.2. human. [Q9NP58-1]
uc010fwe.2. human. [Q9NP58-4]

Organism-specific databases

CTD10058.
GeneCardsGC02M220038.
HGNCHGNC:47. ABCB6.
HPAHPA046723.
MIM111600. phenotype.
605452. gene.
614497. phenotype.
615402. phenotype.
neXtProtNX_Q9NP58.
Orphanet98938. Colobomatous microphthalmia.
241. Dyschromatosis universalis.
194. Ocular coloboma.
PharmGKBPA24388.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5265.
HOVERGENHBG080810.
InParanoidQ9NP58.
KOK05661.
OMAKPQTMER.
OrthoDBEOG7Z69BT.
PhylomeDBQ9NP58.
TreeFamTF105194.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

BgeeQ9NP58.
CleanExHS_ABCB6.
GenevestigatorQ9NP58.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR001140. ABC_transptr_TM_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
SSF90123. SSF90123. 1 hit.
PROSITEPS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSABCB6. human.
EvolutionaryTraceQ9NP58.
GeneWikiABCB6.
GenomeRNAi10058.
NextBio38003.
PROQ9NP58.
SOURCESearch...

Entry information

Entry nameABCB6_HUMAN
AccessionPrimary (citable) accession number: Q9NP58
Secondary accession number(s): O75542 expand/collapse secondary AC list , Q49A66, Q59GQ5, Q6ZME6, Q96ME8, Q9HAQ6, Q9HAQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 139 of the entry and version 1 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 2

Human chromosome 2: entries, gene names and cross-references to MIM