Q9H4L7 (SMRCD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1
EC=3.6.4.12

Alternative name(s):
ATP-dependent helicase 1
Short name=hHEL1

Gene names

Name:	SMARCAD1
Synonyms:	KIAA1122

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1026 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs. Required for the restoration of heterochromatin organization after replication. Acts at replication sites to facilitate the maintenance of heterochromatin by directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation (H3K9me3) and restoration of silencing. Ref.15 Ref.17
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Binds to DNA preferentially in the vicinity of transcriptional start sites. Interacts with MSH2 and TRIM28. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with PCNA. Ref.9 Ref.15
Subcellular location	Nucleus. Chromosome. Note: Colocalizes with PCNA at replication forks during S phase. Recruited to double-strand breaks (DSBs) sites of DNA damage. Ref.15 Ref.17
Tissue specificity	Isoform 1 is expressed ubiquitously. Isoform 3 is expressed mainly in skin, fibroblasts, keratinocytes and esophagus. Ref.1 Ref.13
Involvement in disease	Adermatoglyphia (ADERM) [MIM:136000]: An autosomal dominant condition characterized by the lack of epidermal ridges on the palms and soles, which results in the absence of fingerprints, and is associated with a reduced number of sweat gland openings and reduced sweating of palms and soles. Note: The disease is caused by mutations affecting the gene represented in this entry. A splice site mutation causing aberrant splicing of isoform 3 is likely to exert a loss-of-function effect and is associated with ADERM. Ref.13
Sequence similarities	Belongs to the SNF2/RAD54 helicase family. Contains 2 CUE domains. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.
Sequence caution	The sequence AAH17953.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence BAA86436.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAB14759.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Chromosome Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Chromatin regulator Helicase Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP-dependent chromatin remodeling Inferred from mutant phenotype Ref.17. Source: UniProtKB DNA double-strand break processing Inferred from mutant phenotype Ref.17. Source: UniProtKB chromosome separation Inferred from mutant phenotype Ref.15. Source: UniProtKB histone H3 deacetylation Inferred from mutant phenotype Ref.15. Source: UniProtKB histone H4 deacetylation Inferred from mutant phenotype Ref.15. Source: UniProtKB nucleotide metabolic process Non-traceable author statement Ref.1. Source: UniProtKB positive regulation of transcription, DNA-dependent Non-traceable author statement Ref.1. Source: UniProtKB protein homooligomerization Non-traceable author statement Ref.1. Source: UniProtKB regulation of DNA recombination Inferred from expression pattern Ref.1. Source: UniProtKB
Cellular_component	heterochromatin Inferred from sequence or structural similarity. Source: UniProtKB nuclear matrix Non-traceable author statement Ref.1. Source: UniProtKB nuclear replication fork Inferred from direct assay Ref.15. Source: UniProtKB site of double-strand break Inferred from direct assay Ref.17. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from direct assay Ref.9. Source: UniProtKB helicase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9H4L7-1)

Also known as: Long;

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: Q9H4L7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     765-765: L → LVT

Isoform 3 (identifier: Q9H4L7-3)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-430: Missing.

Note: Skin-specific.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1026	1026	SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1		PRO_0000074356
Regions
	Domain	157 – 199	43	CUE 1
	Domain	251 – 294	44	CUE 2
	Domain	509 – 677	169	Helicase ATP-binding
	Domain	858 – 1010	153	Helicase C-terminal
	Nucleotide binding	521 – 529	9	ATP By similarity
	Nucleotide binding	897 – 904	8	ATP By similarity
	Motif	628 – 631	4	DEGH box
	Motif	721 – 738	18	Nuclear localization signal Potential
	Motif	1005 – 1008	4	DEGD box
Amino acid modifications
	Modified residue	54	1	Phosphothreonine Ref.11 Ref.16
	Modified residue	57	1	Phosphoserine Ref.16
	Modified residue	79	1	Phosphoserine Ref.10
	Modified residue	124	1	Phosphoserine Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.16
	Modified residue	127	1	Phosphoserine Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.16
	Modified residue	132	1	Phosphoserine Ref.8 Ref.10 Ref.11
	Modified residue	146	1	Phosphoserine Ref.11 Ref.16
	Modified residue	152	1	Phosphoserine Ref.16
	Modified residue	211	1	Phosphoserine Ref.10
	Modified residue	212	1	Phosphoserine By similarity
	Modified residue	213	1	Phosphoserine By similarity
	Modified residue	214	1	Phosphoserine Ref.10
	Modified residue	239	1	Phosphoserine Ref.7 Ref.16
	Modified residue	242	1	Phosphoserine Ref.7 Ref.16
	Modified residue	302	1	Phosphoserine Ref.8
	Modified residue	408	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 430	430	Missing in isoform 3.		VSP_043110
	Alternative sequence	765	1	L → LVT in isoform 2.		VSP_007104
	Natural variant	66	1	S → F. Corresponds to variant rs11723410 [ dbSNP | Ensembl ].		VAR_028037
	Natural variant	135	1	L → F. Corresponds to variant rs2664891 [ dbSNP | Ensembl ].		VAR_028038
	Natural variant	140	1	R → C. Corresponds to variant rs2632398 [ dbSNP | Ensembl ].		VAR_028039
	Natural variant	245	1	S → Y. Corresponds to variant rs3103117 [ dbSNP | Ensembl ].		VAR_028040
	Natural variant	247	1	S → N. Ref.5 Ref.7 Corresponds to variant rs11722476 [ dbSNP | Ensembl ].		VAR_028041
	Natural variant	301	1	V → A. Ref.1 Ref.5 Ref.8 Corresponds to variant rs7439869 [ dbSNP | Ensembl ].		VAR_028042
	Natural variant	351	1	P → Q. Ref.5 Corresponds to variant rs17854344 [ dbSNP | Ensembl ].		VAR_028043
	Natural variant	972	1	V → A. Ref.5 Corresponds to variant rs17857297 [ dbSNP | Ensembl ].		VAR_028044
Experimental info
	Mutagenesis	528	1	K → R: No effect on subcellular localization and on histone deacetylation. Ref.15
	Sequence conflict	215	1	E → D in AAH17953. Ref.5
	Sequence conflict	937	1	N → D in BAB14759. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified October 5, 2010. Version 2. Checksum: 0A5DB5653F478413	FASTA	1,026	117,402
	10 20 30 40 50 60 MNLFNLDRFR FEKRNKIEEA PEATPQPSQP GPSSPISLSA EEENAEGEVS RANTPDSDIT 70 80 90 100 110 120 EKTEDSSVPE TPDNERKASI SYFKNQRGIQ YIDLSSDSED VVSPNCSNTV QEKTFNKDTV 130 140 150 160 170 180 IIVSEPSEDE ESQGLPTMAR RNDDISELED LSELEDLKDA KLQTLKELFP QRSDNDLLKL 190 200 210 220 230 240 IESTSTMDGA IAAALLMFGD AGGGPRKRKL SSSSEPYEED EFNDDQSIKK TRLDHGEESN 250 260 270 280 290 300 ESAESSSNWE KQESIVLKLQ KEFPNFDKQE LREVLKEHEW MYTEALESLK VFAEDQDMQY 310 320 330 340 350 360 VSQSEVPNGK EVSSRSQNYP KNATKTKLKQ KFSMKAQNGF NKKRKKNVFN PKRVVEDSEY 370 380 390 400 410 420 DSGSDVGSSL DEDYSSGEEV MEDGYKGKIL HFLQDASIGE LTLIPQCSQK KAQKITELRP 430 440 450 460 470 480 FNSWEALFTK MSKTNGLSED LIWHCKTLIQ ERDVVIRLMN KCEDISNKLT KQVTMLTGNG 490 500 510 520 530 540 GGWNIEQPSI LNQSLSLKPY QKVGLNWLAL VHKHGLNGIL ADEMGLGKTI QAIAFLAYLY 550 560 570 580 590 600 QEGNNGPHLI VVPASTIDNW LREVNLWCPT LKVLCYYGSQ EERKQIRFNI HSRYEDYNVI 610 620 630 640 650 660 VTTYNCAISS SDDRSLFRRL KLNYAIFDEG HMLKNMGSIR YQHLMTINAN NRLLLTGTPV 670 680 690 700 710 720 QNNLLELMSL LNFVMPHMFS SSTSEIRRMF SSKTKSADEQ SIYEKERIAH AKQIIKPFIL 730 740 750 760 770 780 RRVKEEVLKQ LPPKKDRIEL CAMSEKQEQL YLGLFNRLKK SINNLEKNTE MCNVMMQLRK 790 800 810 820 830 840 MANHPLLHRQ YYTAEKLKEM SQLMLKEPTH CEANPDLIFE DMEVMTDFEL HVLCKQYRHI 850 860 870 880 890 900 NNFQLDMDLI LDSGKFRVLG CILSELKQKG DRVVLFSQFT MMLDILEVLL KHHQHRYLRL 910 920 930 940 950 960 DGKTQISERI HLIDEFNTDM DIFVFLLSTK AGGLGINLTS ANVVILHDID CNPYNDKQAE 970 980 990 1000 1010 1020 DRCHRVGQTK EVLVIKLISQ GTIEESMLKI NQQKLKLEQD MTTVDEGDEG SMPADIATLL KTSMGL
	Isoform 2 [UniParc]. Checksum: 0F1C3F3AB7224F23	FASTA	1,028	117,603
	10 20 30 40 50 60 MNLFNLDRFR FEKRNKIEEA PEATPQPSQP GPSSPISLSA EEENAEGEVS RANTPDSDIT 70 80 90 100 110 120 EKTEDSSVPE TPDNERKASI SYFKNQRGIQ YIDLSSDSED VVSPNCSNTV QEKTFNKDTV 130 140 150 160 170 180 IIVSEPSEDE ESQGLPTMAR RNDDISELED LSELEDLKDA KLQTLKELFP QRSDNDLLKL 190 200 210 220 230 240 IESTSTMDGA IAAALLMFGD AGGGPRKRKL SSSSEPYEED EFNDDQSIKK TRLDHGEESN 250 260 270 280 290 300 ESAESSSNWE KQESIVLKLQ KEFPNFDKQE LREVLKEHEW MYTEALESLK VFAEDQDMQY 310 320 330 340 350 360 VSQSEVPNGK EVSSRSQNYP KNATKTKLKQ KFSMKAQNGF NKKRKKNVFN PKRVVEDSEY 370 380 390 400 410 420 DSGSDVGSSL DEDYSSGEEV MEDGYKGKIL HFLQDASIGE LTLIPQCSQK KAQKITELRP 430 440 450 460 470 480 FNSWEALFTK MSKTNGLSED LIWHCKTLIQ ERDVVIRLMN KCEDISNKLT KQVTMLTGNG 490 500 510 520 530 540 GGWNIEQPSI LNQSLSLKPY QKVGLNWLAL VHKHGLNGIL ADEMGLGKTI QAIAFLAYLY 550 560 570 580 590 600 QEGNNGPHLI VVPASTIDNW LREVNLWCPT LKVLCYYGSQ EERKQIRFNI HSRYEDYNVI 610 620 630 640 650 660 VTTYNCAISS SDDRSLFRRL KLNYAIFDEG HMLKNMGSIR YQHLMTINAN NRLLLTGTPV 670 680 690 700 710 720 QNNLLELMSL LNFVMPHMFS SSTSEIRRMF SSKTKSADEQ SIYEKERIAH AKQIIKPFIL 730 740 750 760 770 780 RRVKEEVLKQ LPPKKDRIEL CAMSEKQEQL YLGLFNRLKK SINNLVTEKN TEMCNVMMQL 790 800 810 820 830 840 RKMANHPLLH RQYYTAEKLK EMSQLMLKEP THCEANPDLI FEDMEVMTDF ELHVLCKQYR 850 860 870 880 890 900 HINNFQLDMD LILDSGKFRV LGCILSELKQ KGDRVVLFSQ FTMMLDILEV LLKHHQHRYL 910 920 930 940 950 960 RLDGKTQISE RIHLIDEFNT DMDIFVFLLS TKAGGLGINL TSANVVILHD IDCNPYNDKQ 970 980 990 1000 1010 1020 AEDRCHRVGQ TKEVLVIKLI SQGTIEESML KINQQKLKLE QDMTTVDEGD EGSMPADIAT LLKTSMGL
	Isoform 3 (Short) [UniParc]. Checksum: 6BBB9C2EB02E2A97	FASTA	596	68,774
	10 20 30 40 50 60 MSKTNGLSED LIWHCKTLIQ ERDVVIRLMN KCEDISNKLT KQVTMLTGNG GGWNIEQPSI 70 80 90 100 110 120 LNQSLSLKPY QKVGLNWLAL VHKHGLNGIL ADEMGLGKTI QAIAFLAYLY QEGNNGPHLI 130 140 150 160 170 180 VVPASTIDNW LREVNLWCPT LKVLCYYGSQ EERKQIRFNI HSRYEDYNVI VTTYNCAISS 190 200 210 220 230 240 SDDRSLFRRL KLNYAIFDEG HMLKNMGSIR YQHLMTINAN NRLLLTGTPV QNNLLELMSL 250 260 270 280 290 300 LNFVMPHMFS SSTSEIRRMF SSKTKSADEQ SIYEKERIAH AKQIIKPFIL RRVKEEVLKQ 310 320 330 340 350 360 LPPKKDRIEL CAMSEKQEQL YLGLFNRLKK SINNLEKNTE MCNVMMQLRK MANHPLLHRQ 370 380 390 400 410 420 YYTAEKLKEM SQLMLKEPTH CEANPDLIFE DMEVMTDFEL HVLCKQYRHI NNFQLDMDLI 430 440 450 460 470 480 LDSGKFRVLG CILSELKQKG DRVVLFSQFT MMLDILEVLL KHHQHRYLRL DGKTQISERI 490 500 510 520 530 540 HLIDEFNTDM DIFVFLLSTK AGGLGINLTS ANVVILHDID CNPYNDKQAE DRCHRVGQTK 550 560 570 580 590 EVLVIKLISQ GTIEESMLKI NQQKLKLEQD MTTVDEGDEG SMPADIATLL KTSMGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"SMARCAD1, a novel human helicase family-defining member associated with genetic instability: cloning, expression, and mapping to 4q22-q23, a band rich in breakpoints and deletion mutants involved in several human diseases." Adra C.N., Donato J.-L., Badovinac R., Syed F., Kheraj R., Cai H., Moran C., Kolker M.T., Turner H., Weremowicz S., Shirakawa T., Morton C.C., Schnipper L.E., Drews R. Genomics 69:162-173(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT ALA-301. Tissue: Fetal brain.
[2]	"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain." Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O. DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[3]	"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. , 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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-702 (ISOFORMS 1/2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 649-1026 (ISOFORM 2).
[4]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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 2), VARIANTS ASN-247; ALA-301; GLN-351 AND ALA-972. Tissue: Kidney and Testis.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 433-1026 (ISOFORM 1). Tissue: Melanoma and Testis.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-127; SER-239 AND SER-242, VARIANT [LARGE SCALE ANALYSIS] ASN-247, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-127; SER-132 AND SER-302, VARIANT [LARGE SCALE ANALYSIS] ALA-301, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"The novel protein complex with SMARCAD1/KIAA1122 binds to the vicinity of TSS." Okazaki N., Ikeda S., Ohara R., Shimada K., Yanagawa T., Nagase T., Ohara O., Koga H. J. Mol. Biol. 382:257-265(2008) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING, INTERACTION WITH MSH2 AND TRIM28.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-124; SER-127; SER-132; SER-211 AND SER-214, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-124; SER-127; SER-132 AND SER-146, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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 SER-124 AND SER-127, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"A mutation in a skin-specific isoform of SMARCAD1 causes autosomal-dominant adermatoglyphia." Nousbeck J., Burger B., Fuchs-Telem D., Pavlovsky M., Fenig S., Sarig O., Itin P., Sprecher E. Am. J. Hum. Genet. 89:302-307(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN ADERM, TISSUE SPECIFICITY, ALTERNATIVE SPLICING (ISOFORM 3).
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"Maintenance of silent chromatin through replication requires SWI/SNF-like chromatin remodeler SMARCAD1." Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P., Mermoud J.E. Mol. Cell 42:285-296(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PCNA; TRIM28; HDAC1; HDAC2; EHMT2; PARP1 AND CBX3, MUTAGENESIS OF LYS-528.
[16]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-57; SER-124; SER-127; SER-146; SER-152; SER-239 AND SER-242, MASS SPECTROMETRY.
[17]	"The yeast Fun30 and human SMARCAD1 chromatin remodellers promote DNA end resection." Costelloe T., Louge R., Tomimatsu N., Mukherjee B., Martini E., Khadaroo B., Dubois K., Wiegant W.W., Thierry A., Burma S., van Attikum H., Llorente B. Nature 489:581-584(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.

Web resources

Protein Spotlight

The ends of our fingers - Issue 136 of March 2012

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY008271 mRNA. Translation: AAG16639.1. AB032948 mRNA. Translation: BAA86436.2. Different initiation. AK023990 mRNA. Translation: BAB14759.1. Different initiation. AK027490 mRNA. Translation: BAB55150.1. AK301668 mRNA. Translation: BAH13535.1. AC096746 Genomic DNA. No translation available. BC017953 mRNA. Translation: AAH17953.1. Sequence problems. BC045534 mRNA. Translation: AAH45534.1. AL359929 mRNA. Translation: CAB95769.1. AL512768 mRNA. Translation: CAC21685.1.
IPI	IPI00008422. IPI00220119.
RefSeq	NP_001121901.1. NM_001128429.2. NP_001121902.1. NM_001128430.1. NP_001241878.1. NM_001254949.1. NP_064544.2. NM_020159.4.
UniGene	Hs.410406.
3D structure databases
ProteinModelPortal	Q9H4L7.
SMR	Q9H4L7. Positions 497-1025.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000351947.
PTM databases
PhosphoSite	Q9H4L7.
Polymorphism databases
DMDM	306526240.
Proteomic databases
PaxDb	Q9H4L7.
PRIDE	Q9H4L7.
Protocols and materials databases
DNASU	56916.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000354268; ENSP00000346217; ENSG00000163104. ENST00000359052; ENSP00000351947; ENSG00000163104. ENST00000457823; ENSP00000415576; ENSG00000163104. ENST00000509418; ENSP00000423286; ENSG00000163104.
GeneID	56916.
KEGG	hsa:56916.
UCSC	uc003htb.4. human. uc003htc.4. human.
Organism-specific databases
CTD	56916.
GeneCards	GC04P095128.
H-InvDB	HIX0004380.
HGNC	HGNC:18398. SMARCAD1.
HPA	HPA016737.
MIM	136000. phenotype. 612761. gene.
neXtProt	NX_Q9H4L7.
Orphanet	289465. Isolated adermatoglyphia.
PharmGKB	PA134954731.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0553.
HOGENOM	HOG000172362.
HOVERGEN	HBG055804.
KO	K14439.
OMA	KNQRGIQ.
Gene expression databases
ArrayExpress	Q9H4L7.
Bgee	Q9H4L7.
CleanEx	HS_SMARCAD1.
Genevestigator	Q9H4L7.
GermOnline	ENSG00000163104. Homo sapiens.
Family and domain databases
InterPro	IPR003892. CUE. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR000330. SNF2_N. IPR009060. UBA-like. [Graphical view]
Pfam	PF00271. Helicase_C. 1 hit. PF00176. SNF2_N. 1 hit. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. [Graphical view]
SUPFAM	SSF46934. UBA_like. 1 hit.
PROSITE	PS51140. CUE. 2 hits. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SMARCAD1. human.
GenomeRNAi	56916.
NextBio	62407.
SOURCE	Search...

Entry information

Entry name

SMRCD_HUMAN

Accession

Primary (citable) accession number: Q9H4L7
Secondary accession number(s): B7Z799 , Q05D56, Q96SX1, Q9H017, Q9H860, Q9NPU9, Q9ULU7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 28, 2003
Last sequence update:	October 5, 2010
Last modified:	May 1, 2013
This is version 117 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.