Reviewed, UniProtKB/Swiss-Prot Q15788 (NCOA1_HUMAN)

Names and origin

Protein names

Recommended name:
    Nuclear receptor coactivator 1
      Short name=NCoA-1
    EC=2.3.1.48
Alternative name(s):
    Steroid receptor coactivator 1
      Short name=SRC-1
    RIP160
    Protein Hin-2
    Renal carcinoma antigen NY-REN-52

Gene names

Name:	NCOA1
Synonyms:	SRC1

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	1441 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs). Also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors. Displays histone acetyltransferase activity toward H3 and H4; the relevance of such activity remains however unclear. Plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and recruitment of general transcription factors. Required with NCOA2 to control energy balance between white and brown adipose tissues. Required for mediating steroid hormone response. Isoform 2 has a higher thyroid hormone-dependent transactivation activity than isoform 1 and isoform 3.
Catalytic activity	Acetyl-CoA + histone = CoA + acetylhistone.
Subunit structure	Interacts with the methyltransferase CARM1 By similarity. Interacts with NCOA6 and NCOA2. Interacts with the FDL motif of STAT5A and STAT5B. Interacts with the LXXLL motif of STAT6. Interacts with STAT3 following IL-6 stimulation. Interacts with the basal transcription factor GTF2B. Interacts with the histone acetyltransferases EP300 and CREBBP. Interacts with PCAF, COPS5, NR3C1 and TTLL5/STAMP.
Subcellular location	NucleusBy similarity.
Tissue specificity	Widely expressed.
Domain	The C-terminal (1107-1441) part mediates the histone acetyltransferase (HAT) activity. Contains 7 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. LXXLL motifs 3, 4 and 5 are essential for the association with nuclear receptors. LXXLL motif 7, which is not present in isoform 2, increases the affinity for steroid receptors in vitro.
Post-translational modification	Sumoylated; sumoylation increases its interaction with PGR and prolongs its retention in the nucleus. It does not prevent its ubiquitination and does not exert a clear effect on the stability of the protein. Ubiquitinated; leading to proteasome-mediated degradation. Ubiquitination and sumoylation take place at different sites. Phosphorylated upon DNA damage, probably by ATM or ATR.
Involvement in disease	A chromosomal aberration involving NCOA1 is a cause of rhabdomyosarcoma. Translocation t(2;2)(q35;p23) with PAX3 generates the NCOA1-PAX3 oncogene consisting of the N-terminus part of PAX3 and the C-terminus part of NCOA1. The fusion protein acts as a transcriptional activator. Rhabdomyosarcoma is the most common soft tissue carcinoma in childhood, representing 5-8% of all malignancies in children.
Sequence similarities	Belongs to the SRC/p160 nuclear receptor coactivator family. Contains 1 basic helix-loop-helix (bHLH) domain. Contains 1 PAS (PER-ARNT-SIM) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Domain	Repeat
Molecular function	Activator Acyltransferase Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	androgen receptor signaling pathway Non-traceable author statement. Source: UniProtKB positive regulation of transcription, DNA-dependent Non-traceable author statement. Source: UniProtKB
Cellular component	nucleus Ref.11 Traceable author statement. Source: ProtInc
Molecular function	androgen receptor binding Non-traceable author statement. Source: UniProtKB histone acetyltransferase activity Inferred from electronic annotation. Source: InterPro protein N-terminus binding Ref.24 Inferred from physical interaction. Source: UniProtKB signal transducer activity Inferred from electronic annotation. Source: InterPro transcription coactivator activity Ref.11 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Nfkb1	P25799	1	EBI-455189,EBI-643958	From a different organism.
Nr3c1	P06536	2	EBI-455189,EBI-1187143	From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15788-1)

Also known as: SRC-1A; SRC1a;

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: Q15788-2)

Also known as: SRC-1E; SRC1e;

The sequence of this isoform differs from the canonical sequence as follows:
     1386-1441: QVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQTPQAQQKSLLQQLLTE → DKKTEEFFSVVTTD

Notes: Major form. Contains a domain at its C-terminus (1241-1399) that is able to mediate transactivation.

Isoform 3 (identifier: Q15788-3)

Also known as: SRC-1 (-Q);

The sequence of this isoform differs from the canonical sequence as follows:
     1385-1385: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1441

1441

Nuclear receptor coactivator 1

PRO_0000094400

Regions

Domain

21 – 81

61

Helix-loop-helix motif

Domain

109 – 180

72

PAS

DNA binding

17 – 20

4

Basic motif

Region

361 – 567

207

Interaction with STAT3

Region

781 – 988

208

Interaction with CREBBP

Motif

46 – 50

5

LXXLL motif 1

Motif

112 – 116

5

LXXLL motif 2

Motif

633 – 637

5

LXXLL motif 3

Motif

690 – 694

5

LXXLL motif 4

Motif

749 – 753

5

LXXLL motif 5

Motif

913 – 917

5

LXXLL motif 6

Motif

1435 – 1439

5

LXXLL motif 7

Compositional bias

389 – 682

294

Ser-rich

Compositional bias

1053 – 1138

86

Gln-rich

Sites

Site

867 – 868

2

Breakpoint for translocation to form PAX3-NCOA1 oncogene

Amino acid modifications

Modified residue

103

1

Phosphoserine

Modified residue

372

1

Phosphoserine

Modified residue

395

1

Phosphoserine

Modified residue

517

1

Phosphoserine

Modified residue

569

1

Phosphoserine

Modified residue

1033

1

Phosphoserine

Modified residue

1179

1

Phosphothreonine

Modified residue

1185

1

Phosphoserine

Cross-link

732

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Cross-link

774

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Natural variations

Alternative sequence

1385

1

Missing in isoform 3.

VSP_011738

Alternative sequence

1386 – 1441

56

QVQQV…QLLTE → DKKTEEFFSVVTTD in isoform 2.

VSP_011739

Natural variant

457

1

Q → K: dbSNP rs1049015.

VAR_019768

Natural variant

466

1

N → K: dbSNP rs1049016.

VAR_019769

Natural variant

474

1

S → P: dbSNP rs1049018.

VAR_019770

Natural variant

591

1

I → T: dbSNP rs1049020.

VAR_019771

Natural variant

685

1

E → A: dbSNP rs1049021.

VAR_019772

Natural variant

794

1

P → A: dbSNP rs1049025.

VAR_019773

Natural variant

999

1

S → F: dbSNP rs1049032.

VAR_019774

Natural variant

1154

1

M → T: dbSNP rs1049038.

VAR_019775

Natural variant

1238

1

V → I

VAR_038832

Natural variant

1272

1

P → S: dbSNP rs1804645.

VAR_034882

Experimental info

Mutagenesis

636 – 637

2

LL → AA: Slightly affects interactions with steroid receptors. Abolishes interactions with steroid receptors; when associated with A-693; A-694; A-752 and A-753

Mutagenesis

693 – 694

2

LL → AA: Slightly affects interactions with steroid receptors. Abolishes interactions with steroid receptors; when associated with A-636; A-637; A-752 and A-753

Mutagenesis

732

1

K → R: Abolishes sumoylation; when associated with R-774

Mutagenesis

752 – 753

2

LL → AA: Slightly affects interactions with steroid receptors. Abolishes interactions with steroid receptors; when associated with A-636; A-637; A-693 and A-694

Mutagenesis

774

1

K → R: Abolishes sumoylation; when associated with R-732

Mutagenesis

800

1

K → R: Does not affect sumoylation of the protein

Mutagenesis

846

1

K → R: Does not affect sumoylation of the protein

Mutagenesis

1378

1

K → R: Does not affect sumoylation of the protein

Sequence conflict

1035

1

Missing in AAT47737. Ref.10

Sequence conflict

1370

1

Q → H in AAA64187. Ref.9

Sequence conflict

1382

1

D → G in AAT47737. Ref.10

Sequence conflict

1435

1

L → R in AAB50242. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1441

Helix Strand Turn

Details...

Helix

688 – 694

7

Turn

924 – 926

3

Helix

929 – 941

13

Helix

945 – 947

3

Helix

952 – 954

3

Turn

958 – 962

5

Beta strand

964 – 966

3

Helix

1434 – 1440

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (SRC-1A) (SRC1a) [UniParc]. Last modified September 11, 2007. Version 3. Checksum: 25EF6F389489121E	FASTA	1,441	156,757
	10 20 30 40 50 60 MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL SANISDIDSL 70 80 90 100 110 120 SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDDVQKSDIS SSSQGVIEKE SLGPLLLEAL 130 140 150 160 170 180 DGFFFVVNCE GRIVFVSENV TSYLGYNQEE LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG 190 200 210 220 230 240 VPWPQEATRR NSHTFNCRML IHPPDEPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ 250 260 270 280 290 300 SCLICIARRL PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF 310 320 330 340 350 360 QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ SPDMQPFIMG 370 380 390 400 410 420 IHIIDREHSG LSPQDDTNSG MSIPRVNPSV NPSISPAHGV ARSSTLPPSN SNMVSTRINR 430 440 450 460 470 480 QQSSDLHSSS HSNSSNSQGS FGCSPGSQIV ANVALNQGQA SSQSSNPSLN LNNSPMEGTG 490 500 510 520 530 540 ISLAQFMSPR RQVTSGLATR PRMPNNSFPP NISTLSSPVG MTSSACNNNN RSYSNIPVTS 550 560 570 580 590 600 LQGMNEGPNN SVGFSASSPV LRQMSSQNSP SRLNIQPAKA ESKDNKEIAS ILNEMIQSDN 610 620 630 640 650 660 SSSDGKPLDS GLLHNNDRLS DGDSKYSQTS HKLVQLLTTT AEQQLRHADI DTSCKDVLSC 670 680 690 700 710 720 TGTSNSASAN SSGGSCPSSH SSLTERHKIL HRLLQEGSPS DITTLSVEPD KKDSASTSVS 730 740 750 760 770 780 VTGQVQGNSS IKLELDASKK KESKDHQLLR YLLDKDEKDL RSTPNLSLDD VKVKVEKKEQ 790 800 810 820 830 840 MDPCNTNPTP MTKPTPEEIK LEAQSQFTAD LDQFDQLLPT LEKAAQLPGL CETDRMDGAV 850 860 870 880 890 900 TSVTIKSEIL PASLQSATAR PTSRLNRLPE LELEAIDNQF GQPGTGDQIP WTNNTVTAIN 910 920 930 940 950 960 QSKSEDQCIS SQLDELLCPP TTVEGRNDEK ALLEQLVSFL SGKDETELAE LDRALGIDKL 970 980 990 1000 1010 1020 VQGGGLDVLS ERFPPQQATP PLIMEERPNL YSQPYSSPSP TANLPSPFQG MVRQKPSLGT 1030 1040 1050 1060 1070 1080 MPVQVTPPRG AFSPGMGMQP RQTLNRPPAA PNQLRLQLQQ RLQGQQQLIH QNRQAILNQF 1090 1100 1110 1120 1130 1140 AATAPVGINM RSGMQQQITP QPPLNAQMLA QRQRELYSQQ HRQRQLIQQQ RAMLMRQQSF 1150 1160 1170 1180 1190 1200 GNNLPPSSGL PVQMGNPRLP QGAPQQFPYP PNYGTNPGTP PASTSPFSQL AANPEASLAN 1210 1220 1230 1240 1250 1260 RNSMVSRGMT GNIGGQFGTG INPQMQQNVF QYPGAGMVPQ GEANFAPSLS PGSSMVPMPI 1270 1280 1290 1300 1310 1320 PPPQSSLLQQ TPPASGYQSP DMKAWQQGAI GNNNVFSQAV QNQPTPAQPG VYNNMSITVS 1330 1340 1350 1360 1370 1380 MAGGNTNVQN MNPMMAQMQM SSLQMPGMNT VCPEQINDPA LRHTGLYCNQ LSSTDLLKTE 1390 1400 1410 1420 1430 1440 ADGTQQVQQV QVFADVQCTV NLVGGDPYLN QPGPLGTQKP TSGPQTPQAQ QKSLLQQLLT E
	Isoform 2 (SRC-1E) (SRC1e) [UniParc]. Checksum: DACE967B31AC6B69		1,399	152,385
	10 20 30 40 50 60 MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL SANISDIDSL 70 80 90 100 110 120 SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDDVQKSDIS SSSQGVIEKE SLGPLLLEAL 130 140 150 160 170 180 DGFFFVVNCE GRIVFVSENV TSYLGYNQEE LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG 190 200 210 220 230 240 VPWPQEATRR NSHTFNCRML IHPPDEPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ 250 260 270 280 290 300 SCLICIARRL PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF 310 320 330 340 350 360 QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ SPDMQPFIMG 370 380 390 400 410 420 IHIIDREHSG LSPQDDTNSG MSIPRVNPSV NPSISPAHGV ARSSTLPPSN SNMVSTRINR 430 440 450 460 470 480 QQSSDLHSSS HSNSSNSQGS FGCSPGSQIV ANVALNQGQA SSQSSNPSLN LNNSPMEGTG 490 500 510 520 530 540 ISLAQFMSPR RQVTSGLATR PRMPNNSFPP NISTLSSPVG MTSSACNNNN RSYSNIPVTS 550 560 570 580 590 600 LQGMNEGPNN SVGFSASSPV LRQMSSQNSP SRLNIQPAKA ESKDNKEIAS ILNEMIQSDN 610 620 630 640 650 660 SSSDGKPLDS GLLHNNDRLS DGDSKYSQTS HKLVQLLTTT AEQQLRHADI DTSCKDVLSC 670 680 690 700 710 720 TGTSNSASAN SSGGSCPSSH SSLTERHKIL HRLLQEGSPS DITTLSVEPD KKDSASTSVS 730 740 750 760 770 780 VTGQVQGNSS IKLELDASKK KESKDHQLLR YLLDKDEKDL RSTPNLSLDD VKVKVEKKEQ 790 800 810 820 830 840 MDPCNTNPTP MTKPTPEEIK LEAQSQFTAD LDQFDQLLPT LEKAAQLPGL CETDRMDGAV 850 860 870 880 890 900 TSVTIKSEIL PASLQSATAR PTSRLNRLPE LELEAIDNQF GQPGTGDQIP WTNNTVTAIN 910 920 930 940 950 960 QSKSEDQCIS SQLDELLCPP TTVEGRNDEK ALLEQLVSFL SGKDETELAE LDRALGIDKL 970 980 990 1000 1010 1020 VQGGGLDVLS ERFPPQQATP PLIMEERPNL YSQPYSSPSP TANLPSPFQG MVRQKPSLGT 1030 1040 1050 1060 1070 1080 MPVQVTPPRG AFSPGMGMQP RQTLNRPPAA PNQLRLQLQQ RLQGQQQLIH QNRQAILNQF 1090 1100 1110 1120 1130 1140 AATAPVGINM RSGMQQQITP QPPLNAQMLA QRQRELYSQQ HRQRQLIQQQ RAMLMRQQSF 1150 1160 1170 1180 1190 1200 GNNLPPSSGL PVQMGNPRLP QGAPQQFPYP PNYGTNPGTP PASTSPFSQL AANPEASLAN 1210 1220 1230 1240 1250 1260 RNSMVSRGMT GNIGGQFGTG INPQMQQNVF QYPGAGMVPQ GEANFAPSLS PGSSMVPMPI 1270 1280 1290 1300 1310 1320 PPPQSSLLQQ TPPASGYQSP DMKAWQQGAI GNNNVFSQAV QNQPTPAQPG VYNNMSITVS 1330 1340 1350 1360 1370 1380 MAGGNTNVQN MNPMMAQMQM SSLQMPGMNT VCPEQINDPA LRHTGLYCNQ LSSTDLLKTE 1390 ADGTQDKKTE EFFSVVTTD
	Isoform 3 (SRC-1 (-Q)) [UniParc]. Checksum: 4E3FFED7088CDBF8		1,440	156,628
	10 20 30 40 50 60 MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL SANISDIDSL 70 80 90 100 110 120 SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDDVQKSDIS SSSQGVIEKE SLGPLLLEAL 130 140 150 160 170 180 DGFFFVVNCE GRIVFVSENV TSYLGYNQEE LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG 190 200 210 220 230 240 VPWPQEATRR NSHTFNCRML IHPPDEPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ 250 260 270 280 290 300 SCLICIARRL PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF 310 320 330 340 350 360 QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ SPDMQPFIMG 370 380 390 400 410 420 IHIIDREHSG LSPQDDTNSG MSIPRVNPSV NPSISPAHGV ARSSTLPPSN SNMVSTRINR 430 440 450 460 470 480 QQSSDLHSSS HSNSSNSQGS FGCSPGSQIV ANVALNQGQA SSQSSNPSLN LNNSPMEGTG 490 500 510 520 530 540 ISLAQFMSPR RQVTSGLATR PRMPNNSFPP NISTLSSPVG MTSSACNNNN RSYSNIPVTS 550 560 570 580 590 600 LQGMNEGPNN SVGFSASSPV LRQMSSQNSP SRLNIQPAKA ESKDNKEIAS ILNEMIQSDN 610 620 630 640 650 660 SSSDGKPLDS GLLHNNDRLS DGDSKYSQTS HKLVQLLTTT AEQQLRHADI DTSCKDVLSC 670 680 690 700 710 720 TGTSNSASAN SSGGSCPSSH SSLTERHKIL HRLLQEGSPS DITTLSVEPD KKDSASTSVS 730 740 750 760 770 780 VTGQVQGNSS IKLELDASKK KESKDHQLLR YLLDKDEKDL RSTPNLSLDD VKVKVEKKEQ 790 800 810 820 830 840 MDPCNTNPTP MTKPTPEEIK LEAQSQFTAD LDQFDQLLPT LEKAAQLPGL CETDRMDGAV 850 860 870 880 890 900 TSVTIKSEIL PASLQSATAR PTSRLNRLPE LELEAIDNQF GQPGTGDQIP WTNNTVTAIN 910 920 930 940 950 960 QSKSEDQCIS SQLDELLCPP TTVEGRNDEK ALLEQLVSFL SGKDETELAE LDRALGIDKL 970 980 990 1000 1010 1020 VQGGGLDVLS ERFPPQQATP PLIMEERPNL YSQPYSSPSP TANLPSPFQG MVRQKPSLGT 1030 1040 1050 1060 1070 1080 MPVQVTPPRG AFSPGMGMQP RQTLNRPPAA PNQLRLQLQQ RLQGQQQLIH QNRQAILNQF 1090 1100 1110 1120 1130 1140 AATAPVGINM RSGMQQQITP QPPLNAQMLA QRQRELYSQQ HRQRQLIQQQ RAMLMRQQSF 1150 1160 1170 1180 1190 1200 GNNLPPSSGL PVQMGNPRLP QGAPQQFPYP PNYGTNPGTP PASTSPFSQL AANPEASLAN 1210 1220 1230 1240 1250 1260 RNSMVSRGMT GNIGGQFGTG INPQMQQNVF QYPGAGMVPQ GEANFAPSLS PGSSMVPMPI 1270 1280 1290 1300 1310 1320 PPPQSSLLQQ TPPASGYQSP DMKAWQQGAI GNNNVFSQAV QNQPTPAQPG VYNNMSITVS 1330 1340 1350 1360 1370 1380 MAGGNTNVQN MNPMMAQMQM SSLQMPGMNT VCPEQINDPA LRHTGLYCNQ LSSTDLLKTE 1390 1400 1410 1420 1430 1440 ADGTQVQQVQ VFADVQCTVN LVGGDPYLNQ PGPLGTQKPT SGPQTPQAQQ KSLLQQLLTE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and properties of a full-length putative thyroid hormone receptor coactivator." Takeshita A., Yen P.M., Misiti S., Cardona G.R., Liu Y., Chin W.W. Endocrinology 137:3594-3597(1996) [PubMed: 8754792] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH GTF2B, VARIANTS LYS-457; LYS-466; PRO-474; THR-591; ALA-685; PHE-999 AND THR-1154.
[2]	"Isoforms of steroid receptor coactivator 1 differ in their ability to potentiate transcription by the oestrogen receptor." Kalkhoven E., Valentine J.E., Heery D.M., Parker M.G. EMBO J. 17:232-243(1998) [PubMed: 9427757] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF 636-LEU-LEU-637; 693-LEU-LEU-694 AND 752-LEU-LEU-753.
[3]	"The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors." Onate S.A., Boonyaratanakornkit V., Spencer T.E., Tsai S.Y., Tsai M.-J., Edwards D.P., O'Malley B.W. J. Biol. Chem. 273:12101-12108(1998) [PubMed: 9575154] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS LYS-457; LYS-466; PRO-474; THR-591; ALA-685; PHE-999 AND THR-1154. Tissue: Heart muscle and Skeletal muscle.
[4]	SeattleSNPs program for genomic applications Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-1238 AND SER-1272.
[5]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."