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Q9H4L7 (SMRCD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. 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:
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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1026 AA.
Sequence statusComplete.
Protein existenceEvidence 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.18

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.18

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 processDNA damage
DNA repair
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionChromatin regulator
Helicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP-dependent chromatin remodeling

Inferred from mutant phenotype Ref.18. Source: UniProtKB

DNA double-strand break processing

Inferred from mutant phenotype Ref.18. Source: UniProtKB

chromatin modification

Non-traceable author statement Ref.1. Source: UniProtKB

chromatin remodeling

Non-traceable author statement Ref.15. 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-templated

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_componentheterochromatin

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

nucleus

Inferred from direct assay. Source: HPA

site of double-strand break

Inferred from direct assay Ref.18. Source: UniProtKB

   Molecular_functionATP 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

nucleic acid binding

Non-traceable author statement Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.9Ref.15. Source: UniProtKB

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10261026SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1
PRO_0000074356

Regions

Domain157 – 19943CUE 1
Domain251 – 29444CUE 2
Domain509 – 677169Helicase ATP-binding
Domain858 – 1010153Helicase C-terminal
Nucleotide binding521 – 5299ATP By similarity
Nucleotide binding897 – 9048ATP By similarity
Motif628 – 6314DEGH box
Motif721 – 73818Nuclear localization signal Potential
Motif1005 – 10084DEGD box

Amino acid modifications

Modified residue11N-acetylmethionine Ref.19
Modified residue541Phosphothreonine Ref.11 Ref.16
Modified residue571Phosphoserine Ref.16
Modified residue791Phosphoserine Ref.10
Modified residue1241Phosphoserine Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.16
Modified residue1271Phosphoserine Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.16
Modified residue1321Phosphoserine Ref.8 Ref.10 Ref.11
Modified residue1461Phosphoserine Ref.11 Ref.16
Modified residue1521Phosphoserine Ref.16
Modified residue2111Phosphoserine Ref.10
Modified residue2141Phosphoserine Ref.10
Modified residue2391Phosphoserine Ref.7 Ref.16
Modified residue2421Phosphoserine Ref.7 Ref.16
Modified residue3021Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 430430Missing in isoform 3.
VSP_043110
Alternative sequence7651L → LVT in isoform 2.
VSP_007104
Natural variant661S → F.
Corresponds to variant rs11723410 [ dbSNP | Ensembl ].
VAR_028037
Natural variant1351L → F.
Corresponds to variant rs2664891 [ dbSNP | Ensembl ].
VAR_028038
Natural variant1401R → C.
Corresponds to variant rs2632398 [ dbSNP | Ensembl ].
VAR_028039
Natural variant2451S → Y.
Corresponds to variant rs3103117 [ dbSNP | Ensembl ].
VAR_028040
Natural variant2471S → N. Ref.5 Ref.7
Corresponds to variant rs11722476 [ dbSNP | Ensembl ].
VAR_028041
Natural variant3011V → A. Ref.1 Ref.5 Ref.8 Ref.20
Corresponds to variant rs7439869 [ dbSNP | Ensembl ].
VAR_028042
Natural variant3511P → Q. Ref.5
Corresponds to variant rs17854344 [ dbSNP | Ensembl ].
VAR_028043
Natural variant9721V → A. Ref.5
Corresponds to variant rs17857297 [ dbSNP | Ensembl ].
VAR_028044

Experimental info

Mutagenesis5281K → R: No effect on subcellular localization and on histone deacetylation. Ref.15
Sequence conflict2151E → D in AAH17953. Ref.5
Sequence conflict9371N → D in BAB14759. Ref.3

Sequences

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

Last modified October 5, 2010. Version 2.
Checksum: 0A5DB5653F478413

FASTA1,026117,402
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 0F1C3F3AB7224F23
Show »

FASTA1,028117,603
Isoform 3 (Short) [UniParc].

Checksum: 6BBB9C2EB02E2A97
Show »

FASTA59668,774

References

« Hide '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. 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 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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.
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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.
CCDSCCDS3639.1. [Q9H4L7-1]
CCDS47101.1. [Q9H4L7-2]
CCDS58914.1. [Q9H4L7-3]
RefSeqNP_001121901.1. NM_001128429.2. [Q9H4L7-2]
NP_001121902.1. NM_001128430.1. [Q9H4L7-2]
NP_001241878.1. NM_001254949.1. [Q9H4L7-3]
NP_064544.2. NM_020159.4. [Q9H4L7-1]
UniGeneHs.410406.

3D structure databases

ProteinModelPortalQ9H4L7.
SMRQ9H4L7. Positions 497-1006.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121244. 120 interactions.
IntActQ9H4L7. 2 interactions.
STRING9606.ENSP00000351947.

PTM databases

PhosphoSiteQ9H4L7.

Polymorphism databases

DMDM306526240.

Proteomic databases

MaxQBQ9H4L7.
PaxDbQ9H4L7.
PRIDEQ9H4L7.

Protocols and materials databases

DNASU56916.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354268; ENSP00000346217; ENSG00000163104. [Q9H4L7-1]
ENST00000359052; ENSP00000351947; ENSG00000163104. [Q9H4L7-2]
ENST00000457823; ENSP00000415576; ENSG00000163104. [Q9H4L7-2]
ENST00000509418; ENSP00000423286; ENSG00000163104. [Q9H4L7-3]
GeneID56916.
KEGGhsa:56916.
UCSCuc003htb.4. human. [Q9H4L7-2]
uc003htc.4. human. [Q9H4L7-1]

Organism-specific databases

CTD56916.
GeneCardsGC04P095128.
H-InvDBHIX0004380.
HGNCHGNC:18398. SMARCAD1.
HPAHPA016737.
MIM136000. phenotype.
612761. gene.
neXtProtNX_Q9H4L7.
Orphanet289465. Isolated adermatoglyphia.
PharmGKBPA134954731.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOGENOMHOG000172362.
HOVERGENHBG055804.
KOK14439.
OMAKNQRGIQ.
OrthoDBEOG7QNVKC.
PhylomeDBQ9H4L7.
TreeFamTF105768.

Gene expression databases

ArrayExpressQ9H4L7.
BgeeQ9H4L7.
CleanExHS_SMARCAD1.
GenevestigatorQ9H4L7.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003892. CUE.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PfamPF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS51140. CUE. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSMARCAD1. human.
GeneWikiSMARCAD1.
GenomeRNAi56916.
NextBio62407.
PROQ9H4L7.
SOURCESearch...

Entry information

Entry nameSMRCD_HUMAN
AccessionPrimary (citable) accession number: Q9H4L7
Secondary accession number(s): B7Z799 expand/collapse secondary AC list , Q05D56, Q96SX1, Q9H017, Q9H860, Q9NPU9, Q9ULU7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 129 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 4

Human chromosome 4: entries, gene names and cross-references to MIM