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Q9NZC9 (SMAL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. 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·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-like protein 1

EC=3.6.4.-
Alternative name(s):
HepA-related protein
Short name=hHARP
Sucrose nonfermenting protein 2-like 1
Gene names
Name:SMARCAL1
Synonyms:HARP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length954 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ATP-dependent annealing helicase that binds selectively to fork DNA relative to ssDNA or dsDNA and catalyzes the rewinding of the stably unwound DNA. Rewinds single-stranded DNA bubbles that are stably bound by replication protein A (RPA). Acts throughout the genome to reanneal stably unwound DNA, performing the opposite reaction of many enzymes, such as helicases and polymerases, that unwind DNA. May play an important role in DNA damage response by acting at stalled replication forks. Ref.10 Ref.11 Ref.16

Subunit structure

Interacts with RPA2; the interaction is direct and mediates the recruitment by the RPA complex of SMARCAL1 to sites of DNA damage. Ref.9 Ref.10 Ref.11

Subcellular location

Nucleus. Note: Recruited to damaged DNA regions. Ref.9 Ref.11

Tissue specificity

Ubiquitously expressed, with high levels in testis. Ref.1 Ref.2

Post-translational modification

DNA damage-regulated phosphorylation by kinases that may include ATM, ATR and PRKDC.

Involvement in disease

Schimke immuno-osseous dysplasia (SIOD) [MIM:242900]: Causes spondyloepiphyseal dysplasia, renal dysfunction and T-cell immunodeficiency. Approximately half of all patients also exhibit hyperthyroidism, while around half also exhibit episodal cerebral ischemia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.11 Ref.16

Sequence similarities

Belongs to the SNF2/RAD54 helicase family. SMARCAL1 subfamily.

Contains 2 HARP domains.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Sequence caution

The sequence BAA90955.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainCoiled coil
Repeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from mutant phenotype Ref.16. Source: GOC

DNA metabolic process

Inferred from mutant phenotype Ref.16. Source: UniProtKB

DNA strand renaturation

Inferred from direct assay PubMed 22705370. Source: GOC

cellular response to DNA damage stimulus

Inferred from mutant phenotype Ref.11. Source: UniProtKB

chromatin modification

Inferred from electronic annotation. Source: InterPro

regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.16. Source: UniProtKB

replication fork processing

Inferred from mutant phenotype Ref.11. Source: UniProtKB

   Cellular_componentnucleus

Inferred from direct assay Ref.16. Source: UniProtKB

site of double-strand break

Inferred from direct assay Ref.11Ref.9. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: InterPro

DNA-dependent ATPase activity

Inferred from mutant phenotype Ref.16. Source: UniProtKB

annealing helicase activity

Inferred from direct assay PubMed 22705370. Source: UniProtKB

helicase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.11Ref.9. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 954953SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1
PRO_0000074348

Regions

Domain226 – 30378HARP 1
Domain327 – 39872HARP 2
Domain445 – 600156Helicase ATP-binding
Domain716 – 869154Helicase C-terminal
Nucleotide binding458 – 4658ATP By similarity
Region2 – 3029Mediates interaction with RPA2
Coiled coil3 – 3432 Potential
Motif549 – 5524DESH box

Amino acid modifications

Modified residue21N-acetylserine Ref.14
Modified residue1511Phosphoserine Ref.12

Natural variations

Natural variant221A → G. Ref.5
Corresponds to variant rs17851400 [ dbSNP | Ensembl ].
VAR_038370
Natural variant431A → T.
Corresponds to variant rs2066524 [ dbSNP | Ensembl ].
VAR_021363
Natural variant1141R → H.
Corresponds to variant rs11555797 [ dbSNP | Ensembl ].
VAR_021364
Natural variant2061Y → D.
Corresponds to variant rs5014982 [ dbSNP | Ensembl ].
VAR_021365
Natural variant2071I → F.
Corresponds to variant rs6734114 [ dbSNP | Ensembl ].
VAR_021366
Natural variant3151S → R.
Corresponds to variant rs2066522 [ dbSNP | Ensembl ].
VAR_021367
Natural variant3771E → Q. Ref.5 Ref.7
Corresponds to variant rs2066518 [ dbSNP | Ensembl ].
VAR_021368
Natural variant4241D → V.
Corresponds to variant rs2066520 [ dbSNP | Ensembl ].
VAR_021369
Natural variant4321L → V in a breast cancer sample; somatic mutation. Ref.15
VAR_036026
Natural variant4681A → P in SIOD. Ref.2
VAR_021370
Natural variant5481I → N in SIOD. Ref.2
VAR_021371
Natural variant5791S → L in SIOD. Ref.2
VAR_021372
Natural variant5861R → W in SIOD; impairs without abolishing annealing helicase activity; no effect on specific binding to fork DNA; no effect on recruitment to sites of DNA damage. Ref.2 Ref.11 Ref.16
VAR_021373
Natural variant6441R → W in SIOD. Ref.2
VAR_021374
Natural variant6451R → C in SIOD. Ref.2
VAR_021375
Natural variant6471K → Q in SIOD. Ref.2
VAR_021376
Natural variant6471K → T in SIOD. Ref.2
VAR_021377
Natural variant6491D → N.
Corresponds to variant rs2066523 [ dbSNP | Ensembl ].
VAR_021378
Natural variant7051T → I in SIOD. Ref.2
VAR_021379
Natural variant7421T → M.
Corresponds to variant rs2271336 [ dbSNP | Ensembl ].
VAR_021380
Natural variant7641R → Q in SIOD; abolishes annealing helicase activity; no effect on specific binding to fork DNA; no effect on recruitment to sites of DNA damage. Ref.2 Ref.11 Ref.16
VAR_021381
Natural variant8201R → H in SIOD. Ref.2
VAR_021382

Experimental info

Mutagenesis17 – 193RQK → AAA: Loss of interaction with RPA2 and impaired recruitment by the RPA complex to sites of DNA damage. Ref.11
Sequence conflict1181A → T in AAF24984. Ref.1
Sequence conflict3351C → G in AAF24984. Ref.1
Sequence conflict3441E → K in BAA90955. Ref.7
Sequence conflict8821I → M in AAF24984. Ref.1
Sequence conflict9001L → V in AAF24984. Ref.1
Sequence conflict9111A → G in AAF24984. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9NZC9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C5C762C24A2FDD3A

FASTA954105,938
        10         20         30         40         50         60 
MSLPLTEEQR KKIEENRQKA LARRAEKLLA EQHQRTSSGT SIAGNPFQAK QGPSQNFPRE 

        70         80         90        100        110        120 
SCKPVSHGVI FKQQNLSSSS NADQRPHDSH SFQAKGIWKK PEEMPTACPG HSPRSQMALT 

       130        140        150        160        170        180 
GISPPLAQSP PEVPKQQLLS YELGQGHAQA SPEIRFTPFA NPTHKPLAKP KSSQETPAHS 

       190        200        210        220        230        240 
SGQPPRDAKL EAKTAKASPS GQNISYIHSS SESVTPRTEG RLQQKSGSSV QKGVNSQKGK 

       250        260        270        280        290        300 
CVRNGDRFQV LIGYNAELIA VFKTLPSKNY DPDTKTWNFS MNDYSALMKA AQSLPTVNLQ 

       310        320        330        340        350        360 
PLEWAYGSSE SPSTSSEGQA GLPSAPSLSF VKGRCMLISR AYFEADISYS QDLIALFKQM 

       370        380        390        400        410        420 
DSRRYDVKTR KWSFLLEEHS KLIAKVRCLP QVQLDPLPTT LTLAFASQLK KTSLSLTPDV 

       430        440        450        460        470        480 
PEADLSEVDP KLVSNLMPFQ RAGVNFAIAK GGRLLLADDM GLGKTIQAIC IAAFYRKEWP 

       490        500        510        520        530        540 
LLVVVPSSVR FTWEQAFLRW LPSLSPDCIN VVVTGKDRLT AGLINIVSFD LLSKLEKQLK 

       550        560        570        580        590        600 
TPFKVVIIDE SHFLKNSRTA RCRAAMPVLK VAKRVILLSG TPAMSRPAEL YTQIIAVKPT 

       610        620        630        640        650        660 
FFPQFHAFGL RYCDAKRMPW GWDYSGSSNL GELKLLLEEA VMLRRLKSDV LSQLPAKQRK 

       670        680        690        700        710        720 
IVVIAPGRIN ARTRAALDAA AKEMTTKDKT KQQQKDALIL FFNRTAEAKI PSVIEYILDL 

       730        740        750        760        770        780 
LESGREKFLV FAHHKVVLDA ITQELERKHV QHIRIDGSTS SAEREDLCQQ FQLSERHAVA 

       790        800        810        820        830        840 
VLSITAANMG LTFSSADLVV FAELFWNPGV LIQAEDRVHR IGQTSSVGIH YLVAKGTADD 

       850        860        870        880        890        900 
YLWPLIQEKI KVLAEAGLSE TNFSEMTEST DYLYKDPKQQ KIYDLFQKSF EKEGSDMELL 

       910        920        930        940        950 
EAAESFDPGS ASGTSGSSSQ NMGDTLDESS LTASPQKKRR FEFFDNWDSF TSPL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of HARP/SMARCAL1: a prokaryotic HepA-related SNF2 helicase protein from human and mouse."
Coleman M.A., Eisen J.A., Mohrenweiser H.W.
Genomics 65:274-282(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
[2]"Mutant chromatin remodeling protein SMARCAL1 causes Schimke immuno-osseous dysplasia."
Boerkoel C.F., Takashima H., John J., Yan J., Stankiewicz P., Rosenbarker L., Andre J.-L., Bogdanovic R., Burguet A., Cockfield S., Cordeiro I., Frund S., Illies F., Joseph M., Kaitila I., Lama G., Loirat C., McLeod D.R. expand/collapse author list , Milford D.V., Petty E.M., Rodrigo F., Saraiva J.M., Schmidt B., Smith G.C., Spranger J., Stein A., Thiele H., Tizard J., Weksberg R., Lupski J.R., Stockton D.W.
Nat. Genet. 30:215-220(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS SIOD PRO-468; ASN-548; LEU-579; TRP-586; TRP-644; CYS-645; GLN-647; THR-647; ILE-705; GLN-764 AND HIS-820.
[3]"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].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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], VARIANTS GLY-22 AND GLN-377.
Tissue: Lung and Lymph.
[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 147-954.
Tissue: Testis.
[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] OF 335-954, VARIANT GLN-377.
[8]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"The annealing helicase HARP is recruited to DNA repair sites via an interaction with RPA."
Yusufzai T., Kong X., Yokomori K., Kadonaga J.T.
Genes Dev. 23:2400-2404(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RPA2 AND THE RPA COMPLEX, REGION, SUBCELLULAR LOCATION.
[10]"The annealing helicase SMARCAL1 maintains genome integrity at stalled replication forks."
Bansbach C.E., Betous R., Lovejoy C.A., Glick G.G., Cortez D.
Genes Dev. 23:2405-2414(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA DAMAGE RESPONSE, INTERACTION WITH RPA2, PHOSPHORYLATION.
[11]"The SIOD disorder protein SMARCAL1 is an RPA-interacting protein involved in replication fork restart."
Ciccia A., Bredemeyer A.L., Sowa M.E., Terret M.E., Jallepalli P.V., Harper J.W., Elledge S.J.
Genes Dev. 23:2415-2425(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA REPLICATION, INTERACTION WITH RPA2 AND THE RPA COMPLEX, REGION, SUBCELLULAR LOCATION, MUTAGENESIS OF 17-ARG--LYS-19, CHARACTERIZATION OF VARIANTS SIOD TRP-586 AND GLN-764.
[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-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[15]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-432.
[16]"HARP is an ATP-driven annealing helicase."
Yusufzai T., Kadonaga J.T.
Science 322:748-750(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS SIOD TRP-586 AND GLN-764, FUNCTION, DNA-BINDING.
+Additional computationally mapped references.

Web resources

SMARCAL1base

SMARCAL1 mutation db

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF082179 mRNA. Translation: AAF24984.1.
AF210842 expand/collapse EMBL AC list , AF210833, AF210834, AF210835, AF210836, AF210837, AF210838, AF210839, AF210840, AF210841 Genomic DNA. Translation: AAF70454.1.
AF432223 mRNA. Translation: AAL73034.1.
AC098820 Genomic DNA. Translation: AAX93097.1.
CH471063 Genomic DNA. Translation: EAW70567.1.
BC016482 mRNA. Translation: AAH16482.1.
BC043341 mRNA. Translation: AAH43341.1.
AL122076 mRNA. Translation: CAB59251.1.
AK000117 mRNA. Translation: BAA90955.1. Different initiation.
CCDSCCDS2403.1.
PIRT34557.
RefSeqNP_001120679.1. NM_001127207.1.
NP_054859.2. NM_014140.3.
XP_005246688.1. XM_005246631.2.
XP_005246689.1. XM_005246632.1.
UniGeneHs.516674.

3D structure databases

ProteinModelPortalQ9NZC9.
SMRQ9NZC9. Positions 409-840.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119072. 6 interactions.
IntActQ9NZC9. 2 interactions.
MINTMINT-8415341.
STRING9606.ENSP00000349823.

PTM databases

PhosphoSiteQ9NZC9.

Polymorphism databases

DMDM60390962.

Proteomic databases

MaxQBQ9NZC9.
PaxDbQ9NZC9.
PRIDEQ9NZC9.

Protocols and materials databases

DNASU50485.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357276; ENSP00000349823; ENSG00000138375.
ENST00000358207; ENSP00000350940; ENSG00000138375.
GeneID50485.
KEGGhsa:50485.
UCSCuc002vgc.4. human.

Organism-specific databases

CTD50485.
GeneCardsGC02P217277.
GeneReviewsSMARCAL1.
HGNCHGNC:11102. SMARCAL1.
HPAHPA020337.
MIM242900. phenotype.
606622. gene.
neXtProtNX_Q9NZC9.
Orphanet1830. Schimke immuno-osseous dysplasia.
PharmGKBPA35952.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOVERGENHBG054110.
InParanoidQ9NZC9.
KOK14440.
OMASIHYLVA.
OrthoDBEOG7XSTD5.
PhylomeDBQ9NZC9.
TreeFamTF106474.

Gene expression databases

ArrayExpressQ9NZC9.
BgeeQ9NZC9.
CleanExHS_SMARCAL1.
GenevestigatorQ9NZC9.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR010003. HARP_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PfamPF07443. HARP. 2 hits.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 3 hits.
PROSITEPS51467. HARP. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSMARCAL1.
GenomeRNAi50485.
NextBio53040.
PROQ9NZC9.
SOURCESearch...

Entry information

Entry nameSMAL1_HUMAN
AccessionPrimary (citable) accession number: Q9NZC9
Secondary accession number(s): A6NEH0 expand/collapse secondary AC list , Q53R00, Q96AY1, Q9NXQ5, Q9UFH3, Q9UI93
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 116 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 2

Human chromosome 2: entries, gene names and cross-references to MIM