O60706 (ABCC9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-binding cassette sub-family C member 9

Alternative name(s):
Sulfonylurea receptor 2

Gene names

Name:	ABCC9
Synonyms:	SUR2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1549 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Subunit of ATP-sensitive potassium channels (KATP). Can form cardiac and smooth muscle-type KATP channels with KIR6.2. KIR6.2 forms the channel pore while SUR2 is required for activation and regulation.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Involvement in disease	Defects in ABCC9 are the cause of cardiomyopathy dilated type 1O (CMD1O) [MIM:608569]; also known as dilated cardiomyopathy with ventricular tachycardia. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. Ref.3 Defects in ABCC9 are the cause of familial atrial fibrillation type 12 (ATFB12) [MIM:614050]. ATFB12 is 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. Ref.4
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 process	Transport
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Atrial fibrillation Cardiomyopathy Disease mutation
Domain	Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Receptor
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	defense response to virus Inferred from mutant phenotype. Source: MGI potassium ion import Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular component	ATP-sensitive potassium channel complex Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled to transmembrane movement of substances Inferred from electronic annotation. Source: InterPro 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
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1549	1549	ATP-binding cassette sub-family C member 9		PRO_0000093402
Regions
	Topological domain	1 – 30	30	Extracellular Potential
	Transmembrane	31 – 51	21	Helical; Name=1; Potential
	Topological domain	52 – 72	21	Cytoplasmic Potential
	Transmembrane	73 – 93	21	Helical; Name=2; Potential
	Topological domain	94 – 101	8	Extracellular Potential
	Transmembrane	102 – 122	21	Helical; Name=3; Potential
	Topological domain	123 – 132	10	Cytoplasmic Potential
	Transmembrane	133 – 153	21	Helical; Name=4; Potential
	Topological domain	154 – 167	14	Extracellular Potential
	Transmembrane	168 – 188	21	Helical; Name=5; Potential
	Topological domain	189 – 301	113	Cytoplasmic Potential
	Transmembrane	302 – 322	21	Helical; Name=6; Potential
	Topological domain	323 – 350	28	Extracellular Potential
	Transmembrane	351 – 371	21	Helical; Name=7; Potential
	Topological domain	372 – 423	52	Cytoplasmic Potential
	Transmembrane	424 – 444	21	Helical; Name=8; Potential
	Topological domain	445 – 455	11	Extracellular Potential
	Transmembrane	456 – 476	21	Helical; Name=9; Potential
	Topological domain	477 – 531	55	Cytoplasmic Potential
	Transmembrane	532 – 552	21	Helical; Name=10; Potential
	Topological domain	553 – 571	19	Extracellular Potential
	Transmembrane	572 – 592	21	Helical; Name=11; Potential
	Topological domain	593 – 990	398	Cytoplasmic Potential
	Transmembrane	991 – 1011	21	Helical; Name=12; Potential
	Topological domain	1012 – 1034	23	Extracellular Potential
	Transmembrane	1035 – 1055	21	Helical; Name=13; Potential
	Topological domain	1056 – 1127	72	Cytoplasmic Potential
	Transmembrane	1128 – 1148	21	Helical; Name=14; Potential
	Topological domain	1149 – 1245	97	Extracellular Potential
	Transmembrane	1246 – 1266	21	Helical; Name=15; Potential
	Topological domain	1267 – 1549	283	Cytoplasmic Potential
	Domain	297 – 597	301	ABC transmembrane type-1 1
	Domain	672 – 912	241	ABC transporter 1
	Domain	994 – 1274	281	ABC transmembrane type-1 2
	Domain	1312 – 1546	235	ABC transporter 2
	Nucleotide binding	705 – 712	8	ATP 1 Potential
	Nucleotide binding	1346 – 1353	8	ATP 2 Potential
Amino acid modifications
	Glycosylation	9	1	N-linked (GlcNAc...) Potential
	Glycosylation	326	1	N-linked (GlcNAc...) Potential
	Glycosylation	330	1	N-linked (GlcNAc...) Potential
	Glycosylation	333	1	N-linked (GlcNAc...) Potential
	Glycosylation	334	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1508 – 1549	42	SSIMD…VMTNK → HTILTADLVIVMKRGNILEY DTPESLLAQENGVFASFVRA DM in isoform SUR2B.		VSP_000058
	Natural variant	1108	1	P → S. Corresponds to variant rs35404804 [ dbSNP | Ensembl ].		VAR_048143
	Natural variant	1513	1	A → T in CMD1O. Ref.3		VAR_018483
	Natural variant	1547	1	T → 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.4		VAR_066210
Experimental info
	Sequence conflict	586	1	F → S in AAC16057. Ref.1
	Sequence conflict	586	1	F → S in AAC16058. Ref.1
	Sequence conflict	589	1	S → F in AAC16057. Ref.1
	Sequence conflict	589	1	S → F in AAC16058. Ref.1
	Sequence conflict	1503	1	I → M in AAC16057. Ref.1
	Sequence conflict	1503	1	I → M in AAC16058. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform SUR2A [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 55508C9343AB1218	FASTA	1,549	174,223
	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
	Isoform SUR2B [UniParc]. Checksum: A5BB684EEE7156E2	FASTA	1,549	174,425
	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 VTIAHRVHTI LTADLVIVMK RGNILEYDTP ESLLAQENGV FASFVRADM

References

	« Hide 'large scale' referencesShow '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: 9457174] [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. , 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: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 15034580] [Abstract] Cited for: VARIANT CMD1O THR-1513.
[4]	"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: 17245405] [Abstract] Cited for: VARIANT ATFB12 ILE-1547, CHARACTERIZATION OF VARIANT ATFB12 ILE-1547.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF061323 , 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 , 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.
IPI	IPI00024278. IPI00216251.
RefSeq	NP_005682.2. NM_005691.2. NP_064693.2. NM_020297.2.
UniGene	Hs.446050.
3D structure databases
ProteinModelPortal	O60706.
SMR	O60706. Positions 671-914, 980-1548.
ModBase	Search...
Protein-protein interaction databases
STRING	O60706.
PTM databases
PhosphoSite	O60706.
Proteomic databases
PRIDE	O60706.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261201; ENSP00000261201; ENSG00000069431.
GeneID	10060.
KEGG	hsa:10060.
UCSC	uc001rfh.1. human. uc001rfi.1. human.
Organism-specific databases
CTD	10060.
GeneCards	GC12M021852.
HGNC	HGNC:60. ABCC9.
HPA	HPA007279.
MIM	601439. gene. 608569. phenotype. 614050. phenotype.
neXtProt	NX_O60706.
Orphanet	334. Familial atrial fibrillation. 154. Familial isolated dilated cardiomyopathy.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18296.
GeneTree	ENSGT00590000083005.
HOVERGEN	HBG101342.
OMA	HWSNVNE.
PhylomeDB	O60706.
Enzyme and pathway databases
Reactome	REACT_13685. Neuronal System. REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	O60706.
Bgee	O60706.
CleanEx	HS_ABCC9.
Genevestigator	O60706.
GermOnline	ENSG00000069431. Homo sapiens.
Family and domain databases
InterPro	IPR003439. ABC_transporter-like. IPR017871. ABC_transporter_CS. IPR017940. ABC_transporter_type1. IPR001140. ABC_transptr_TM_dom. IPR011527. ABC_transptrTM_dom_typ1. IPR003593. ATPase_AAA+_core. IPR001475. Sulphonylurea_rcpt-2. IPR000388. Sulphorea_rcpt. [Graphical view]
KO	K05033.
Pfam	PF00664. ABC_membrane. 2 hits. PF00005. ABC_tran. 2 hits. [Graphical view]
PRINTS	PR01094. SULFNYLUR2. PR01092. SULFNYLUREAR.
SMART	SM00382. AAA. 2 hits. [Graphical view]
SUPFAM	SSF90123. ABC_TM_1. 2 hits.
PROSITE	PS50929. ABC_TM1F. 2 hits. PS00211. ABC_TRANSPORTER_1. 2 hits. PS50893. ABC_TRANSPORTER_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00171. Adenosine triphosphate. DB01016. Glibenclamide.
SOURCE	Search...

Entry information

Entry name

ABCC9_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 104 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.