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P48029 (SC6A8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sodium- and chloride-dependent creatine transporter 1

Short name=CT1
Short name=Creatine transporter 1
Alternative name(s):
Solute carrier family 6 member 8
Gene names
Name:SLC6A8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length635 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for the uptake of creatine in muscles and brain.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Predominantly expressed in skeletal muscle and kidney. Also found in brain, heart, colon, testis and prostate. Ref.1 Ref.2

Involvement in disease

Cerebral creatine deficiency syndrome 1 (CCDS1) [MIM:300352]: An X-linked disorder of creatine transport characterized by mental retardation, severe speech delay, behavioral abnormalities, and seizures. Carrier females may show mild neuropsychologic impairment.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16

Sequence similarities

Belongs to the sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family. SLC6A8 subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Sodium transport
Symport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Mental retardation
   DomainTransmembrane
Transmembrane helix
   LigandSodium
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

creatine metabolic process

Traceable author statement. Source: Reactome

creatine transmembrane transport

Non-traceable author statement PubMed 8661037. Source: GOC

creatine transport

Non-traceable author statement PubMed 8661037. Source: UniProtKB

muscle contraction

Traceable author statement Ref.3. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

transport

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentintegral component of membrane

Traceable author statement Ref.1. Source: ProtInc

integral component of plasma membrane

Inferred from electronic annotation. Source: InterPro

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functioncholine transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

creatine transmembrane transporter activity

Non-traceable author statement PubMed 8661037. Source: UniProtKB

creatine:sodium symporter activity

Traceable author statement Ref.1. Source: ProtInc

neurotransmitter:sodium symporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P48029-1)

Also known as: CRT1;

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: P48029-2)

Also known as: CRT2; SLC6A8B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-259: MAKKSAENGI...VWKGVKSTGK → MLPTLQIQGP...TASAEQPGPQ
     417-417: S → SQVCMGLWDREPGGGRREGCRQGKGWRRCGDRPELPWP
     464-464: D → DVSGVGGLPVTSGGRLPSSLTGLCPQ
     498-498: Y → YGRSWLRAGLGDGGGEGRSPAWPSRLTSPQ
Isoform 3 (identifier: P48029-3)

Also known as: SLC6A8C;

The sequence of this isoform differs from the canonical sequence as follows:
     1-365: Missing.
Isoform 4 (identifier: P48029-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-115: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 635635Sodium- and chloride-dependent creatine transporter 1
PRO_0000214774

Regions

Topological domain1 – 6060Cytoplasmic Potential
Transmembrane61 – 8121Helical; Potential
Topological domain82 – 876Extracellular Potential
Transmembrane88 – 10821Helical; Potential
Topological domain109 – 13830Cytoplasmic Potential
Transmembrane139 – 15921Helical; Potential
Topological domain160 – 23071Extracellular Potential
Transmembrane231 – 25121Helical; Potential
Topological domain252 – 26918Cytoplasmic Potential
Transmembrane270 – 29021Helical; Potential
Topological domain291 – 30414Extracellular Potential
Transmembrane305 – 32521Helical; Potential
Topological domain326 – 34116Cytoplasmic Potential
Transmembrane342 – 36221Helical; Potential
Topological domain363 – 39432Extracellular Potential
Transmembrane395 – 41521Helical; Potential
Topological domain416 – 44429Cytoplasmic Potential
Transmembrane445 – 46521Helical; Potential
Topological domain466 – 47914Extracellular Potential
Transmembrane480 – 50021Helical; Potential
Topological domain501 – 52020Cytoplasmic Potential
Transmembrane521 – 54121Helical; Potential
Topological domain542 – 56019Extracellular Potential
Transmembrane561 – 58121Helical; Potential
Topological domain582 – 63554Cytoplasmic Potential

Amino acid modifications

Modified residue421Phosphothreonine Ref.11
Glycosylation1921N-linked (GlcNAc...) Potential
Glycosylation1971N-linked (GlcNAc...) Potential
Glycosylation5481N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 365365Missing in isoform 3.
VSP_043916
Alternative sequence1 – 259259MAKKS…KSTGK → MLPTLQIQGPAAFAPGDRGP GRHCPFPVPITPTGALLPVS DSCDSLVDLVWPSVTYLALG TQSRVWPHPLGAPGQAGESP EQRRQCLELWDMASSLGDKV PRAACGKRGQTVWQLHLACL CLAQFHSPPAQPPPLSRRGG GPDPDPISRSLPGPPTPALP THSYSSHSPRAPRLLSPLRR APRGSPAPHRHASLQTNEAP RELPHCTWPGLPGRSLAPSF LWREPWLGGQWGPLNIPARK GDRRRWEWGCEGGGATASAE QPGPQ in isoform 2.
VSP_043917
Alternative sequence1 – 115115Missing in isoform 4.
VSP_046316
Alternative sequence4171S → SQVCMGLWDREPGGGRREGC RQGKGWRRCGDRPELPWP in isoform 2.
VSP_043918
Alternative sequence4641D → DVSGVGGLPVTSGGRLPSSL TGLCPQ in isoform 2.
VSP_043919
Alternative sequence4981Y → YGRSWLRAGLGDGGGEGRSP AWPSRLTSPQ in isoform 2.
VSP_043920
Natural variant871G → R in CCDS1. Ref.14
VAR_020525
Natural variant1321G → V in CCDS1. Ref.15
VAR_063707
Natural variant1641T → S.
Corresponds to variant rs642454 [ dbSNP | Ensembl ].
VAR_034483
Natural variant3361Missing. Ref.16
VAR_070563
Natural variant3371C → W in CCDS1. Ref.14
VAR_063708
Natural variant3811G → R in CCDS1. Ref.12
VAR_020526
Natural variant3901P → L in CCDS1. Ref.14
VAR_020527
Natural variant4081Missing in CCDS1. Ref.13
VAR_020528
Natural variant4911C → W in CCDS1. Ref.15
VAR_063709
Natural variant5541P → L in CCDS1. Ref.14
VAR_020529
Natural variant5601M → V. Ref.14
VAR_063710

Experimental info

Sequence conflict24 – 252AP → VS in AAB32284. Ref.2
Sequence conflict321A → S in AAB32284. Ref.2
Sequence conflict381V → A in AAB32284. Ref.2
Sequence conflict42 – 454TPGG → APSS in AAB32284. Ref.2
Sequence conflict1361A → G in BAG58415. Ref.7
Sequence conflict1931A → D in AAB32284. Ref.2
Sequence conflict2231G → T in AAB32284. Ref.2
Sequence conflict2851A → P in AAC41688. Ref.1
Sequence conflict3681A → T in AAB32284. Ref.2
Sequence conflict4341P → R in AAH81558. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (CRT1) [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 9FAFE100B2A5B845

FASTA63570,523
        10         20         30         40         50         60 
MAKKSAENGI YSVSGDEKKG PLIAPGPDGA PAKGDGPVGL GTPGGRLAVP PRETWTRQMD 

        70         80         90        100        110        120 
FIMSCVGFAV GLGNVWRFPY LCYKNGGGVF LIPYVLIALV GGIPIFFLEI SLGQFMKAGS 

       130        140        150        160        170        180 
INVWNICPLF KGLGYASMVI VFYCNTYYIM VLAWGFYYLV KSFTTTLPWA TCGHTWNTPD 

       190        200        210        220        230        240 
CVEIFRHEDC ANASLANLTC DQLADRRSPV IEFWENKVLR LSGGLEVPGA LNWEVTLCLL 

       250        260        270        280        290        300 
ACWVLVYFCV WKGVKSTGKI VYFTATFPYV VLVVLLVRGV LLPGALDGII YYLKPDWSKL 

       310        320        330        340        350        360 
GSPQVWIDAG TQIFFSYAIG LGALTALGSY NRFNNNCYKD AIILALINSG TSFFAGFVVF 

       370        380        390        400        410        420 
SILGFMAAEQ GVHISKVAES GPGLAFIAYP RAVTLMPVAP LWAALFFFML LLLGLDSQFV 

       430        440        450        460        470        480 
GVEGFITGLL DLLPASYYFR FQREISVALC CALCFVIDLS MVTDGGMYVF QLFDYYSASG 

       490        500        510        520        530        540 
TTLLWQAFWE CVVVAWVYGA DRFMDDIACM IGYRPCPWMK WCWSFFTPLV CMGIFIFNVV 

       550        560        570        580        590        600 
YYEPLVYNNT YVYPWWGEAM GWAFALSSML CVPLHLLGCL LRAKGTMAER WQHLTQPIWG 

       610        620        630 
LHHLEYRAQD ADVRGLTTLT PVSESSKVVV VESVM 

« Hide

Isoform 2 (CRT2) (SLC6A8B) [UniParc].

Checksum: 1BC824884EC299A8
Show »

FASTA73280,137
Isoform 3 (SLC6A8C) [UniParc].

Checksum: 398EA89851EAE536
Show »

FASTA27030,580
Isoform 4 [UniParc].

Checksum: 83FF6FA9A9A8C1A3
Show »

FASTA52058,453

References

« Hide 'large scale' references
[1]"Cloning, pharmacological characterization, and genomic localization of the human creatine transporter."
Nash S.R., Giros B., Kingsmore S.F., Rochelle J.M., Suter S.T., Gregor P., Seldin M.F., Caron M.G.
Recept. Channels 2:165-174(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Kidney.
[2]"The cloning and expression of a human creatine transporter."
Sora I., Richman J., Santoro G., Wei H., Wang Y., Vanderah T., Horvath R., Nguyen M., Waite S., Roeske W.R.
Biochem. Biophys. Res. Commun. 204:419-427(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Brain.
[3]"The genomic organization of a human creatine transporter (CRTR) gene located in Xq28."
Sandoval N., Bauer D., Brenner V., Coy J.F., Drescher B., Kioschis P., Korn B., Nyakatura G., Poustka A., Reichwald K., Rosenthal A., Platzer M.
Genomics 35:383-385(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Cloning and sequencing of a cDNA encoding a novel member of the human brain GABA/noradrenaline neurotransmitter transporter family."
Barnwell L.F., Chaudhuri G., Townsel J.G.
Gene 159:287-288(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Hippocampus.
[5]"Identification, characterization and cloning of SLC6A8C, a novel splice variant of the creatine transporter gene."
Martinez-Munoz C., Rosenberg E.H., Jakobs C., Salomons G.S.
Gene 418:53-59(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[6]"Genomic organization of the human creatine transporter and CDM genes."
Eichler E.E., Lu F., Shen Y., Muzny D.M., Gibbs R.A., Nelson D.L.
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"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 4).
Tissue: Hippocampus.
[8]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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: Eye and Testis.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"X-linked mental retardation with seizures and carrier manifestations is caused by a mutation in the creatine-transporter gene (SLC6A8) located in Xq28."
Hahn K.A., Salomons G.S., Tackels-Horne D., Wood T.C., Taylor H.A., Schroer R.J., Lubs H.A., Jakobs C., Olson R.L., Holden K.R., Stevenson R.E., Schwartz C.E.
Am. J. Hum. Genet. 70:1349-1356(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CCDS1 ARG-381.
[13]"X-linked creatine deficiency syndrome: a novel mutation in creatine transporter gene SLC6A8."
Bizzi A., Bugiani M., Salomons G.S., Hunneman D.H., Moroni I., Estienne M., Danesi U., Jakobs C., Uziel G.
Ann. Neurol. 52:227-231(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CCDS1 PHE-408 DEL.
[14]"High prevalence of SLC6A8 deficiency in X-linked mental retardation."
Rosenberg E.H., Almeida L.S., Kleefstra T., deGrauw R.S., Yntema H.G., Bahi N., Moraine C., Ropers H.-H., Fryns J.-P., deGrauw T.J., Jakobs C., Salomons G.S.
Am. J. Hum. Genet. 75:97-105(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CCDS1 ARG-87; TRP-337; LEU-390 AND LEU-554, VARIANT VAL-560.
[15]"High frequency of creatine deficiency syndromes in patients with unexplained mental retardation."
Lion-Francois L., Cheillan D., Pitelet G., Acquaviva-Bourdain C., Bussy G., Cotton F., Guibaud L., Gerard D., Rivier C., Vianey-Saban C., Jakobs C., Salomons G.S., des Portes V.
Neurology 67:1713-1714(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CCDS1 VAL-132 AND TRP-491.
[16]"Identification of pathogenic gene variants in small families with intellectually disabled siblings by exome sequencing."
Schuurs-Hoeijmakers J.H., Vulto-van Silfhout A.T., Vissers L.E., van de Vondervoort I.I., van Bon B.W., de Ligt J., Gilissen C., Hehir-Kwa J.Y., Neveling K., del Rosario M., Hira G., Reitano S., Vitello A., Failla P., Greco D., Fichera M., Galesi O., Kleefstra T. expand/collapse author list , Greally M.T., Ockeloen C.W., Willemsen M.H., Bongers E.M., Janssen I.M., Pfundt R., Veltman J.A., Romano C., Willemsen M.A., van Bokhoven H., Brunner H.G., de Vries B.B., de Brouwer A.P.
J. Med. Genet. 50:802-811(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CCDS1 ASN-336 DEL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L31409 mRNA. Translation: AAC41688.1.
S74039 mRNA. Translation: AAB32284.1.
U17986 mRNA. Translation: AAA86990.1.
EU280316 mRNA. Translation: ABZ82022.1.
AK295495 mRNA. Translation: BAG58415.1.
U52111 Genomic DNA. No translation available.
Z66539 Genomic DNA. Translation: CAA91442.1.
U36341 Genomic DNA. Translation: AAA79507.1.
BC012355 mRNA. Translation: AAH12355.1.
BC081558 mRNA. Translation: AAH81558.1.
CCDSCCDS14726.1. [P48029-1]
CCDS48190.1. [P48029-4]
PIRG02095.
JC2386.
RefSeqNP_001136277.1. NM_001142805.1.
NP_001136278.1. NM_001142806.1. [P48029-4]
NP_005620.1. NM_005629.3. [P48029-1]
UniGeneHs.540696.

3D structure databases

ProteinModelPortalP48029.
SMRP48029. Positions 52-597.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112426. 1 interaction.
STRING9606.ENSP00000253122.

Chemistry

DrugBankDB00148. Creatine.

Protein family/group databases

TCDB2.A.22.3.11. the neurotransmitter:sodium symporter (nss) family.

PTM databases

PhosphoSiteP48029.

Polymorphism databases

DMDM1352529.

Proteomic databases

MaxQBP48029.
PaxDbP48029.
PRIDEP48029.

Protocols and materials databases

DNASU6535.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253122; ENSP00000253122; ENSG00000130821. [P48029-1]
ENST00000430077; ENSP00000403041; ENSG00000130821. [P48029-4]
ENST00000597046; ENSP00000470814; ENSG00000268982. [P48029-4]
ENST00000598634; ENSP00000472369; ENSG00000268982. [P48029-1]
GeneID6535.
KEGGhsa:6535.
UCSCuc004fib.3. human. [P48029-1]

Organism-specific databases

CTD6535.
GeneCardsGC0XP152953.
GeneReviewsSLC6A8.
H-InvDBHIX0038627.
HGNCHGNC:11055. SLC6A8.
HPAHPA008802.
MIM300036. gene.
300352. phenotype.
neXtProtNX_P48029.
Orphanet52503. X-linked creatine transporter deficiency.
PharmGKBPA35915.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0733.
HOVERGENHBG071421.
KOK05039.
OMAIVFYCNT.
PhylomeDBP48029.
TreeFamTF343812.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP48029.
BgeeP48029.
CleanExHS_SLC6A8.
GenevestigatorP48029.

Family and domain databases

InterProIPR000175. Na/ntran_symport.
IPR002984. Na/ntran_symport_creatine.
[Graphical view]
PANTHERPTHR11616. PTHR11616. 1 hit.
PfamPF00209. SNF. 1 hit.
[Graphical view]
PRINTSPR01199. CRTTRANSPORT.
PR00176. NANEUSMPORT.
PROSITEPS00610. NA_NEUROTRAN_SYMP_1. 1 hit.
PS00754. NA_NEUROTRAN_SYMP_2. 1 hit.
PS50267. NA_NEUROTRAN_SYMP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSLC6A8.
GenomeRNAi6535.
NextBio25427.
PROP48029.
SOURCESearch...

Entry information

Entry nameSC6A8_HUMAN
AccessionPrimary (citable) accession number: P48029
Secondary accession number(s): B2KY47 expand/collapse secondary AC list , B4DIA3, E9PFC0, Q13032, Q66I36
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 138 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

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 X

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