Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O60706 (ABCC9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. 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 C member 9
Alternative name(s):
Sulfonylurea receptor 2
Gene names
Name:ABCC9
Synonyms:SUR2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1549 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Subunit of ATP-sensitive potassium channels (KATP). Can form cardiac and smooth muscle-type KATP channels with KCNJ11. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation. Ref.3 Ref.4

Subunit structure

Interacts with KCNJ11. Ref.3

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Involvement in disease

Cardiomyopathy, dilated 1O (CMD1O) [MIM:608569]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5

Atrial fibrillation, familial, 12 (ATFB12) [MIM:614050]: A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6

Hypertrichotic osteochondrodysplasia (HTOCD) [MIM:239850]: A rare disorder characterized by congenital hypertrichosis, neonatal macrosomia, a distinct osteochondrodysplasia, and cardiomegaly. The hypertrichosis leads to thick scalp hair, which extends onto the forehead, and a general increase in body hair. In addition, macrocephaly and coarse facial features, including a broad nasal bridge, epicanthal folds, a wide mouth, and full lips, can be suggestive of a storage disorder. About half of affected individuals are macrosomic and edematous at birth, whereas in childhood they usually have a muscular appearance with little subcutaneous fat. Thickened calvarium, narrow thorax, wide ribs, flattened or ovoid vertebral bodies, coxa valga, osteopenia, enlarged medullary canals, and metaphyseal widening of long bones have been reported. Cardiac manifestations such as patent ductus arteriosus, ventricular hypertrophy, pulmonary hypertension, and pericardial effusions are present in approximately 80% of cases. Motor development is usually delayed due to hypotonia. Most patients have a mild speech delay, and a small percentage have learning difficulties or intellectual disability.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8

Miscellaneous

May contribute to the regulation of sleep duration. An intronic variant of this gene may account for about 5% of the variation of sleep duration between individuals (Ref.4). Sleep duration is influenced both by environmental and genetic factors, with an estimated heritability of about 40%. Numerous genes are expected to contribute to the regulation of sleep duration.

Sequence similarities

Belongs to the ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily. [View classification]

Contains 2 ABC transmembrane type-1 domains.

Contains 2 ABC transporter domains.

Ontologies

Keywords
   Biological processTransport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseAtrial fibrillation
Cardiomyopathy
Disease mutation
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionReceptor
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to virus

Inferred from mutant phenotype PubMed 18026101. Source: MGI

potassium ion import

Inferred from sequence or structural similarity. Source: BHF-UCL

potassium ion transport

Traceable author statement PubMed 8826984. Source: ProtInc

signal transduction

Inferred from sequence or structural similarity. Source: GOC

synaptic transmission

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentATP-sensitive potassium channel complex

Inferred from sequence or structural similarity. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

sarcolemma

Inferred from electronic annotation. Source: Ensembl

sarcomere

Inferred from electronic annotation. Source: Ensembl

voltage-gated potassium channel complex

Inferred from direct assay PubMed 20610380. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity, coupled to transmembrane movement of substances

Inferred from electronic annotation. Source: InterPro

ion channel binding

Inferred from physical interaction PubMed 20610380. Source: BHF-UCL

potassium channel activity

Inferred from electronic annotation. Source: Ensembl

potassium channel regulator activity

Inferred from sequence or structural similarity. Source: BHF-UCL

sulfonylurea receptor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

transporter activity

Traceable author statement PubMed 8826984. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform SUR2A (identifier: O60706-1)

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 SUR2B (identifier: O60706-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1508-1549: SSIMDAGLVL...LFSTLVMTNK → HTILTADLVI...VFASFVRADM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15491549ATP-binding cassette sub-family C member 9
PRO_0000093402

Regions

Topological domain1 – 3030Extracellular Potential
Transmembrane31 – 5121Helical; Name=1; Potential
Topological domain52 – 7221Cytoplasmic Potential
Transmembrane73 – 9321Helical; Name=2; Potential
Topological domain94 – 1018Extracellular Potential
Transmembrane102 – 12221Helical; Name=3; Potential
Topological domain123 – 13210Cytoplasmic Potential
Transmembrane133 – 15321Helical; Name=4; Potential
Topological domain154 – 16714Extracellular Potential
Transmembrane168 – 18821Helical; Name=5; Potential
Topological domain189 – 301113Cytoplasmic Potential
Transmembrane302 – 32221Helical; Name=6; Potential
Topological domain323 – 35028Extracellular Potential
Transmembrane351 – 37121Helical; Name=7; Potential
Topological domain372 – 42352Cytoplasmic Potential
Transmembrane424 – 44421Helical; Name=8; Potential
Topological domain445 – 45511Extracellular Potential
Transmembrane456 – 47621Helical; Name=9; Potential
Topological domain477 – 53155Cytoplasmic Potential
Transmembrane532 – 55221Helical; Name=10; Potential
Topological domain553 – 57119Extracellular Potential
Transmembrane572 – 59221Helical; Name=11; Potential
Topological domain593 – 990398Cytoplasmic Potential
Transmembrane991 – 101121Helical; Name=12; Potential
Topological domain1012 – 103423Extracellular Potential
Transmembrane1035 – 105521Helical; Name=13; Potential
Topological domain1056 – 112772Cytoplasmic Potential
Transmembrane1128 – 114821Helical; Name=14; Potential
Topological domain1149 – 124597Extracellular Potential
Transmembrane1246 – 126621Helical; Name=15; Potential
Topological domain1267 – 1549283Cytoplasmic Potential
Domain297 – 597301ABC transmembrane type-1 1
Domain672 – 912241ABC transporter 1
Domain994 – 1274281ABC transmembrane type-1 2
Domain1312 – 1546235ABC transporter 2
Nucleotide binding705 – 7128ATP 1 Potential
Nucleotide binding1346 – 13538ATP 2 Potential

Amino acid modifications

Glycosylation91N-linked (GlcNAc...) Potential
Glycosylation3261N-linked (GlcNAc...) Potential
Glycosylation3301N-linked (GlcNAc...) Potential
Glycosylation3331N-linked (GlcNAc...) Potential
Glycosylation3341N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1508 – 154942SSIMD…VMTNK → HTILTADLVIVMKRGNILEY DTPESLLAQENGVFASFVRA DM in isoform SUR2B.
VSP_000058
Natural variant601H → Y in HTOCD. Ref.8
VAR_068485
Natural variant2071D → E in HTOCD. Ref.8
VAR_068486
Natural variant3801G → C in HTOCD. Ref.8
VAR_068487
Natural variant4321P → L in HTOCD; mutant channels show reduced ATP sensitivity. Ref.8
VAR_068488
Natural variant4781A → V in HTOCD. Ref.7
VAR_068489
Natural variant10201S → P in HTOCD. Ref.8
VAR_068490
Natural variant10391F → S in HTOCD. Ref.8
VAR_068491
Natural variant10431C → Y in HTOCD. Ref.7
VAR_068492
Natural variant10541S → Y in HTOCD. Ref.8
VAR_068493
Natural variant11081P → S.
Corresponds to variant rs35404804 [ dbSNP | Ensembl ].
VAR_048143
Natural variant11161R → C in HTOCD. Ref.8
VAR_068494
Natural variant11161R → H in HTOCD; mutant channels show reduced ATP sensitivity. Ref.8
VAR_068495
Natural variant11541R → Q in HTOCD; mutant channels show reduced ATP sensitivity. Ref.7 Ref.8
VAR_068496
Natural variant11541R → W in HTOCD. Ref.7 Ref.8
VAR_068497
Natural variant15131A → T in CMD1O. Ref.5
VAR_018483
Natural variant15471T → I in ATFB12; compromises adenine nucleotide-dependent induction of KATP current; mutant ABCC9 that is co-expressed with KCNJ11 pore generates an aberrant channel that retains ATP-induced inhibition of potassium current, but shows a blunted response to ADP. Ref.6
VAR_066210

Experimental info

Sequence conflict5861F → S in AAC16057. Ref.1
Sequence conflict5861F → S in AAC16058. Ref.1
Sequence conflict5891S → F in AAC16057. Ref.1
Sequence conflict5891S → F in AAC16058. Ref.1
Sequence conflict15031I → M in AAC16057. Ref.1
Sequence conflict15031I → M in AAC16058. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform SUR2A [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 55508C9343AB1218

FASTA1,549174,223
        10         20         30         40         50         60 
MSLSFCGNNI SSYNINDGVL QNSCFVDALN LVPHVFLLFI TFPILFIGWG SQSSKVQIHH 

        70         80         90        100        110        120 
NTWLHFPGHN LRWILTFALL FVHVCEIAEG IVSDSRRESR HLHLFMPAVM GFVATTTSIV 

       130        140        150        160        170        180 
YYHNIETSNF PKLLLALFLY WVMAFITKTI KLVKYCQSGL DISNLRFCIT GMMVILNGLL 

       190        200        210        220        230        240 
MAVEINVIRV RRYVFFMNPQ KVKPPEDLQD LGVRFLQPFV NLLSKATYWW MNTLIISAHK 

       250        260        270        280        290        300 
KPIDLKAIGK LPIAMRAVTN YVCLKDAYEE QKKKVADHPN RTPSIWLAMY RAFGRPILLS 

       310        320        330        340        350        360 
STFRYLADLL GFAGPLCISG IVQRVNETQN GTNNTTGISE TLSSKEFLEN AYVLAVLLFL 

       370        380        390        400        410        420 
ALILQRTFLQ ASYYVTIETG INLRGALLAM IYNKILRLST SNLSMGEMTL GQINNLVAIE 

       430        440        450        460        470        480 
TNQLMWFLFL CPNLWAMPVQ IIMGVILLYN LLGSSALVGA AVIVLLAPIQ YFIATKLAEA 

       490        500        510        520        530        540 
QKSTLDYSTE RLKKTNEILK GIKLLKLYAW EHIFCKSVEE TRMKELSSLK TFALYTSLSI 

       550        560        570        580        590        600 
FMNAAIPIAA VLATFVTHAY ASGNNLKPAE AFASLSLFHI LVTPLFLLST VVRFAVKAII 

       610        620        630        640        650        660 
SVQKLNEFLL SDEIGDDSWR TGESSLPFES CKKHTGVQPK TINRKQPGRY HLDSYEQSTR 

       670        680        690        700        710        720 
RLRPAETEDI AIKVTNGYFS WGSGLATLSN IDIRIPTGQL TMIVGQVGCG KSSLLLAILG 

       730        740        750        760        770        780 
EMQTLEGKVH WSNVNESEPS FEATRSRNRY SVAYAAQKPW LLNATVEENI TFGSPFNKQR 

       790        800        810        820        830        840 
YKAVTDACSL QPDIDLLPFG DQTEIGERGI NLSGGQRQRI CVARALYQNT NIVFLDDPFS 

       850        860        870        880        890        900 
ALDIHLSDHL MQEGILKFLQ DDKRTLVLVT HKLQYLTHAD WIIAMKDGSV LREGTLKDIQ 

       910        920        930        940        950        960 
TKDVELYEHW KTLMNRQDQE LEKDMEADQT TLERKTLRRA MYSREAKAQM EDEDEEEEEE 

       970        980        990       1000       1010       1020 
EDEDDNMSTV MRLRTKMPWK TCWRYLTSGG FFLLILMIFS KLLKHSVIVA IDYWLATWTS 

      1030       1040       1050       1060       1070       1080 
EYSINNTGKA DQTYYVAGFS ILCGAGIFLC LVTSLTVEWM GLTAAKNLHH NLLNKIILGP 

      1090       1100       1110       1120       1130       1140 
IRFFDTTPLG LILNRFSADT NIIDQHIPPT LESLTRSTLL CLSAIGMISY ATPVFLVALL 

      1150       1160       1170       1180       1190       1200 
PLGVAFYFIQ KYFRVASKDL QELDDSTQLP LLCHFSETAE GLTTIRAFRH ETRFKQRMLE 

      1210       1220       1230       1240       1250       1260 
LTDTNNIAYL FLSAANRWLE VRTDYLGACI VLTASIASIS GSSNSGLVGL GLLYALTITN 

      1270       1280       1290       1300       1310       1320 
YLNWVVRNLA DLEVQMGAVK KVNSFLTMES ENYEGTMDPS QVPEHWPQEG EIKIHDLCVR 

      1330       1340       1350       1360       1370       1380 
YENNLKPVLK HVKAYIKPGQ KVGICGRTGS GKSSLSLAFF RMVDIFDGKI VIDGIDISKL 

      1390       1400       1410       1420       1430       1440 
PLHTLRSRLS IILQDPILFS GSIRFNLDPE CKCTDDRLWE ALEIAQLKNM VKSLPGGLDA 

      1450       1460       1470       1480       1490       1500 
VVTEGGENFS VGQRQLFCLA RAFVRKSSIL IMDEATASID MATENILQKV VMTAFADRTV 

      1510       1520       1530       1540 
VTIAHRVSSI MDAGLVLVFS EGILVECDTV PNLLAHKNGL FSTLVMTNK 

« Hide

Isoform SUR2B [UniParc].

Checksum: A5BB684EEE7156E2
Show »

FASTA1,549174,425

References

« Hide 'large scale' references
[1]"Toward understanding the assembly and structure of KATP channels."
Aguilar-Bryan L., Clement J.P. IV, Gonzalez G., Kunjilwar K., Babenko A., Bryan J.
Physiol. Rev. 78:227-245(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS SUR2A AND SUR2B), REVIEW.
[2]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Reconstituted human cardiac KATP channels: functional identity with the native channels from the sarcolemma of human ventricular cells."
Babenko A.P., Gonzalez G., Aguilar-Bryan L., Bryan J.
Circ. Res. 83:1132-1143(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[4]"A K(ATP) channel gene effect on sleep duration: from genome-wide association studies to function in Drosophila."
Allebrandt K.V., Amin N., Muller-Myhsok B., Esko T., Teder-Laving M., Azevedo R.V., Hayward C., van Mill J., Vogelzangs N., Green E.W., Melville S.A., Lichtner P., Wichmann H.E., Oostra B.A., Janssens A.C., Campbell H., Wilson J.F., Hicks A.A. expand/collapse author list , Pramstaller P.P., Dogas Z., Rudan I., Merrow M., Penninx B., Kyriacou C.P., Metspalu A., van Duijn C.M., Meitinger T., Roenneberg T.
Mol. Psychiatry 18:122-132(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE FUNCTION IN REGULATION OF SLEEP DURATION.
[5]"ABCC9 mutations identified in human dilated cardiomyopathy disrupt catalytic KATP channel gating."
Bienengraeber M., Olson T.M., Selivanov V.A., Kathmann E.C., O'Cochlain F., Gao F., Karger A.B., Ballew J.D., Hodgson D.M., Zingman L.V., Pang Y.-P., Alekseev A.E., Terzic A.
Nat. Genet. 36:382-387(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMD1O THR-1513.
[6]"KATP channel mutation confers risk for vein of Marshall adrenergic atrial fibrillation."
Olson T.M., Alekseev A.E., Moreau C., Liu X.K., Zingman L.V., Miki T., Seino S., Asirvatham S.J., Jahangir A., Terzic A.
Nat. Clin. Pract. Cardiovasc. Med. 4:110-116(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ATFB12 ILE-1547, CHARACTERIZATION OF VARIANT ATFB12 ILE-1547.
[7]"Cantu syndrome is caused by mutations in ABCC9."
van Bon B.W., Gilissen C., Grange D.K., Hennekam R.C., Kayserili H., Engels H., Reutter H., Ostergaard J.R., Morava E., Tsiakas K., Isidor B., Le Merrer M., Eser M., Wieskamp N., de Vries P., Steehouwer M., Veltman J.A., Robertson S.P. expand/collapse author list , Brunner H.G., de Vries B.B., Hoischen A.
Am. J. Hum. Genet. 90:1094-1101(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HTOCD VAL-478; TYR-1043; GLN-1154 AND TRP-1154.
[8]"Dominant missense mutations in ABCC9 cause Cantu syndrome."
Harakalova M., van Harssel J.J., Terhal P.A., van Lieshout S., Duran K., Renkens I., Amor D.J., Wilson L.C., Kirk E.P., Turner C.L., Shears D., Garcia-Minaur S., Lees M.M., Ross A., Venselaar H., Vriend G., Takanari H., Rook M.B. expand/collapse author list , van der Heyden M.A., Asselbergs F.W., Breur H.M., Swinkels M.E., Scurr I.J., Smithson S.F., Knoers N.V., van der Smagt J.J., Nijman I.J., Kloosterman W.P., van Haelst M.M., van Haaften G., Cuppen E.
Nat. Genet. 44:793-796(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HTOCD TYR-60; GLU-207; CYS-380; LEU-432; PRO-1020; SER-1039; TYR-1054; HIS-1116; CYS-1116; GLN-1154 AND TRP-1154, CHARACTERIZATION OF VARIANTS HTOCD LEU-432; HIS-1116 AND GLN-1154.
+Additional computationally mapped references.

Web resources

GeneReviews
Protein Spotlight

On The Other Side - Issue 139 of June 2012

ABCMdb

Database for mutations in ABC proteins

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF061323 expand/collapse EMBL AC list , AF061289, AF061290, AF061291, AF061292, AF061293, AF061294, AF061295, AF061296, AF061297, AF061298, AF061299, AF061300, AF061301, AF061302, AF061303, AF061304, AF061305, AF061306, AF061307, AF061308, AF061309, AF061310, AF061311, AF061312, AF061313, AF061314, AF061315, AF061316, AF061317, AF061318, AF061319, AF061320, AF061321, AF061322 Genomic DNA. Translation: AAC16057.1.
AF061324 expand/collapse EMBL AC list , AF061289, AF061290, AF061291, AF061292, AF061293, AF061294, AF061295, AF061296, AF061297, AF061298, AF061299, AF061300, AF061301, AF061302, AF061303, AF061304, AF061305, AF061306, AF061307, AF061308, AF061309, AF061310, AF061311, AF061312, AF061313, AF061314, AF061315, AF061316, AF061317, AF061318, AF061319, AF061320, AF061321, AF061322 Genomic DNA. Translation: AAC16058.1.
AC008250 Genomic DNA. No translation available.
AC084806 Genomic DNA. No translation available.
RefSeqNP_005682.2. NM_005691.3.
NP_064693.2. NM_020297.3.
XP_005253341.1. XM_005253284.2.
XP_005253343.1. XM_005253286.2.
XP_005253344.1. XM_005253287.2.
XP_005253345.1. XM_005253288.2.
UniGeneHs.732701.

3D structure databases

ProteinModelPortalO60706.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115371. 2 interactions.
STRING9606.ENSP00000261200.

Chemistry

BindingDBO60706.
ChEMBLCHEMBL1971.
DrugBankDB00171. Adenosine triphosphate.
DB01016. Glibenclamide.

Protein family/group databases

TCDB3.A.1.208.23. the atp-binding cassette (abc) superfamily.

PTM databases

PhosphoSiteO60706.

Proteomic databases

PaxDbO60706.
PRIDEO60706.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261200; ENSP00000261200; ENSG00000069431. [O60706-2]
ENST00000261201; ENSP00000261201; ENSG00000069431. [O60706-1]
GeneID10060.
KEGGhsa:10060.
UCSCuc001rfh.3. human. [O60706-2]
uc001rfi.1. human. [O60706-1]

Organism-specific databases

CTD10060.
GeneCardsGC12M021852.
HGNCHGNC:60. ABCC9.
HPAHPA007279.
MIM239850. phenotype.
601439. gene.
608569. phenotype.
614050. phenotype.
neXtProtNX_O60706.
Orphanet965. Acromegaloid facial appearance syndrome.
334. Familial atrial fibrillation.
154. Familial isolated dilated cardiomyopathy.
966. Hypertrichosis-acromegaloid facial appearence syndrome.
1517. Hypertrichotic osteochondrodysplasia, Cantu type.
PharmGKBPA396.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1132.
HOVERGENHBG101342.
KOK05033.
OMAMMVILNG.
OrthoDBEOG7MWGW0.
PhylomeDBO60706.
TreeFamTF105201.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressO60706.
BgeeO60706.
CleanExHS_ABCC9.
GenevestigatorO60706.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR001140. ABC_transptr_TM_dom.
IPR027417. P-loop_NTPase.
IPR001475. Sulphonylurea_rcpt-2.
IPR000388. Sulphorea_rcpt.
[Graphical view]
PfamPF00664. ABC_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
[Graphical view]
PRINTSPR01094. SULFNYLUR2.
PR01092. SULFNYLUREAR.
SMARTSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF90123. SSF90123. 2 hits.
PROSITEPS50929. ABC_TM1F. 2 hits.
PS00211. ABC_TRANSPORTER_1. 2 hits.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiABCC9.
GenomeRNAi10060.
NextBio38015.
PROO60706.
SOURCESearch...

Entry information

Entry nameABCC9_HUMAN
AccessionPrimary (citable) accession number: O60706
Secondary accession number(s): O60707
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 130 of the entry and version 2 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

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

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 12

Human chromosome 12: entries, gene names and cross-references to MIM