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Q9NZC9

- SMAL1_HUMAN

UniProt

Q9NZC9 - SMAL1_HUMAN

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Protein

SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1

Gene

SMARCAL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi458 – 4658ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. annealing helicase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. DNA binding Source: InterPro
  4. DNA-dependent ATPase activity Source: UniProtKB
  5. helicase activity Source: UniProtKB-KW

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. chromatin modification Source: InterPro
  3. DNA metabolic process Source: UniProtKB
  4. DNA strand renaturation Source: GOC
  5. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  6. replication fork processing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SMARCAL1
Synonyms:HARP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:11102. SMARCAL1.

Subcellular locationi

Nucleus 2 Publications
Note: Recruited to damaged DNA regions.

GO - Cellular componenti

  1. nucleus Source: UniProtKB
  2. site of double-strand break Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti468 – 4681A → P in SIOD. 1 Publication
VAR_021370
Natural varianti548 – 5481I → N in SIOD. 1 Publication
VAR_021371
Natural varianti579 – 5791S → L in SIOD. 1 Publication
VAR_021372
Natural varianti586 – 5861R → 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. 1 Publication
VAR_021373
Natural varianti644 – 6441R → W in SIOD. 1 Publication
VAR_021374
Natural varianti645 – 6451R → C in SIOD. 1 Publication
VAR_021375
Natural varianti647 – 6471K → Q in SIOD. 1 Publication
VAR_021376
Natural varianti647 – 6471K → T in SIOD. 1 Publication
VAR_021377
Natural varianti705 – 7051T → I in SIOD. 1 Publication
VAR_021379
Natural varianti764 – 7641R → Q in SIOD; abolishes annealing helicase activity; no effect on specific binding to fork DNA; no effect on recruitment to sites of DNA damage. 1 Publication
VAR_021381
Natural varianti820 – 8201R → H in SIOD. 1 Publication
VAR_021382

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 193RQK → AAA: Loss of interaction with RPA2 and impaired recruitment by the RPA complex to sites of DNA damage. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi242900. phenotype.
Orphaneti1830. Schimke immuno-osseous dysplasia.
PharmGKBiPA35952.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 954953SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1PRO_0000074348Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei151 – 1511Phosphoserine1 Publication

Post-translational modificationi

DNA damage-regulated phosphorylation by kinases that may include ATM, ATR and PRKDC.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9NZC9.
PaxDbiQ9NZC9.
PRIDEiQ9NZC9.

PTM databases

PhosphoSiteiQ9NZC9.

Expressioni

Tissue specificityi

Ubiquitously expressed, with high levels in testis.2 Publications

Gene expression databases

BgeeiQ9NZC9.
CleanExiHS_SMARCAL1.
ExpressionAtlasiQ9NZC9. baseline and differential.
GenevestigatoriQ9NZC9.

Organism-specific databases

HPAiHPA020337.

Interactioni

Subunit structurei

Interacts with RPA2; the interaction is direct and mediates the recruitment by the RPA complex of SMARCAL1 to sites of DNA damage.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RPA2P1592712EBI-5457961,EBI-621404

Protein-protein interaction databases

BioGridi119072. 6 interactions.
IntActiQ9NZC9. 3 interactions.
MINTiMINT-8415341.
STRINGi9606.ENSP00000349823.

Structurei

Secondary structure

1
954
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MQVX-ray1.95B/D5-30[»]
ProteinModelPortaliQ9NZC9.
SMRiQ9NZC9. Positions 238-302, 330-397, 409-840.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini226 – 30378HARP 1PROSITE-ProRule annotationAdd
BLAST
Domaini327 – 39872HARP 2PROSITE-ProRule annotationAdd
BLAST
Domaini445 – 600156Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini716 – 869154Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 3029Mediates interaction with RPA2Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili3 – 3432Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi549 – 5524DESH box

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family. SMARCAL1 subfamily.PROSITE-ProRule annotation
Contains 2 HARP domains.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG0553.
GeneTreeiENSGT00630000089754.
HOVERGENiHBG054110.
InParanoidiQ9NZC9.
KOiK14440.
OMAiSIHYLVA.
OrthoDBiEOG7XSTD5.
PhylomeDBiQ9NZC9.
TreeFamiTF106474.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR010003. HARP_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PfamiPF07443. HARP. 2 hits.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
PROSITEiPS51467. HARP. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9NZC9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLPLTEEQR KKIEENRQKA LARRAEKLLA EQHQRTSSGT SIAGNPFQAK
60 70 80 90 100
QGPSQNFPRE SCKPVSHGVI FKQQNLSSSS NADQRPHDSH SFQAKGIWKK
110 120 130 140 150
PEEMPTACPG HSPRSQMALT GISPPLAQSP PEVPKQQLLS YELGQGHAQA
160 170 180 190 200
SPEIRFTPFA NPTHKPLAKP KSSQETPAHS SGQPPRDAKL EAKTAKASPS
210 220 230 240 250
GQNISYIHSS SESVTPRTEG RLQQKSGSSV QKGVNSQKGK CVRNGDRFQV
260 270 280 290 300
LIGYNAELIA VFKTLPSKNY DPDTKTWNFS MNDYSALMKA AQSLPTVNLQ
310 320 330 340 350
PLEWAYGSSE SPSTSSEGQA GLPSAPSLSF VKGRCMLISR AYFEADISYS
360 370 380 390 400
QDLIALFKQM DSRRYDVKTR KWSFLLEEHS KLIAKVRCLP QVQLDPLPTT
410 420 430 440 450
LTLAFASQLK KTSLSLTPDV PEADLSEVDP KLVSNLMPFQ RAGVNFAIAK
460 470 480 490 500
GGRLLLADDM GLGKTIQAIC IAAFYRKEWP LLVVVPSSVR FTWEQAFLRW
510 520 530 540 550
LPSLSPDCIN VVVTGKDRLT AGLINIVSFD LLSKLEKQLK TPFKVVIIDE
560 570 580 590 600
SHFLKNSRTA RCRAAMPVLK VAKRVILLSG TPAMSRPAEL YTQIIAVKPT
610 620 630 640 650
FFPQFHAFGL RYCDAKRMPW GWDYSGSSNL GELKLLLEEA VMLRRLKSDV
660 670 680 690 700
LSQLPAKQRK IVVIAPGRIN ARTRAALDAA AKEMTTKDKT KQQQKDALIL
710 720 730 740 750
FFNRTAEAKI PSVIEYILDL LESGREKFLV FAHHKVVLDA ITQELERKHV
760 770 780 790 800
QHIRIDGSTS SAEREDLCQQ FQLSERHAVA VLSITAANMG LTFSSADLVV
810 820 830 840 850
FAELFWNPGV LIQAEDRVHR IGQTSSVGIH YLVAKGTADD YLWPLIQEKI
860 870 880 890 900
KVLAEAGLSE TNFSEMTEST DYLYKDPKQQ KIYDLFQKSF EKEGSDMELL
910 920 930 940 950
EAAESFDPGS ASGTSGSSSQ NMGDTLDESS LTASPQKKRR FEFFDNWDSF

TSPL
Length:954
Mass (Da):105,938
Last modified:October 1, 2000 - v1
Checksum:iC5C762C24A2FDD3A
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181A → T in AAF24984. (PubMed:10857751)Curated
Sequence conflicti335 – 3351C → G in AAF24984. (PubMed:10857751)Curated
Sequence conflicti344 – 3441E → K in BAA90955. (PubMed:14702039)Curated
Sequence conflicti882 – 8821I → M in AAF24984. (PubMed:10857751)Curated
Sequence conflicti900 – 9001L → V in AAF24984. (PubMed:10857751)Curated
Sequence conflicti911 – 9111A → G in AAF24984. (PubMed:10857751)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221A → G.1 Publication
Corresponds to variant rs17851400 [ dbSNP | Ensembl ].
VAR_038370
Natural varianti43 – 431A → T.
Corresponds to variant rs2066524 [ dbSNP | Ensembl ].
VAR_021363
Natural varianti114 – 1141R → H.
Corresponds to variant rs11555797 [ dbSNP | Ensembl ].
VAR_021364
Natural varianti206 – 2061Y → D.
Corresponds to variant rs5014982 [ dbSNP | Ensembl ].
VAR_021365
Natural varianti207 – 2071I → F.
Corresponds to variant rs6734114 [ dbSNP | Ensembl ].
VAR_021366
Natural varianti315 – 3151S → R.
Corresponds to variant rs2066522 [ dbSNP | Ensembl ].
VAR_021367
Natural varianti377 – 3771E → Q.2 Publications
Corresponds to variant rs2066518 [ dbSNP | Ensembl ].
VAR_021368
Natural varianti424 – 4241D → V.
Corresponds to variant rs2066520 [ dbSNP | Ensembl ].
VAR_021369
Natural varianti432 – 4321L → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_036026
Natural varianti468 – 4681A → P in SIOD. 1 Publication
VAR_021370
Natural varianti548 – 5481I → N in SIOD. 1 Publication
VAR_021371
Natural varianti579 – 5791S → L in SIOD. 1 Publication
VAR_021372
Natural varianti586 – 5861R → 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. 1 Publication
VAR_021373
Natural varianti644 – 6441R → W in SIOD. 1 Publication
VAR_021374
Natural varianti645 – 6451R → C in SIOD. 1 Publication
VAR_021375
Natural varianti647 – 6471K → Q in SIOD. 1 Publication
VAR_021376
Natural varianti647 – 6471K → T in SIOD. 1 Publication
VAR_021377
Natural varianti649 – 6491D → N.
Corresponds to variant rs2066523 [ dbSNP | Ensembl ].
VAR_021378
Natural varianti705 – 7051T → I in SIOD. 1 Publication
VAR_021379
Natural varianti742 – 7421T → M.
Corresponds to variant rs2271336 [ dbSNP | Ensembl ].
VAR_021380
Natural varianti764 – 7641R → Q in SIOD; abolishes annealing helicase activity; no effect on specific binding to fork DNA; no effect on recruitment to sites of DNA damage. 1 Publication
VAR_021381
Natural varianti820 – 8201R → H in SIOD. 1 Publication
VAR_021382

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF082179 mRNA. Translation: AAF24984.1.
AF210842
, 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.
CCDSiCCDS2403.1.
PIRiT34557.
RefSeqiNP_001120679.1. NM_001127207.1.
NP_054859.2. NM_014140.3.
XP_005246688.1. XM_005246631.2.
XP_005246689.1. XM_005246632.1.
UniGeneiHs.516674.

Genome annotation databases

EnsembliENST00000357276; ENSP00000349823; ENSG00000138375.
ENST00000358207; ENSP00000350940; ENSG00000138375.
GeneIDi50485.
KEGGihsa:50485.
UCSCiuc002vgc.4. human.

Polymorphism databases

DMDMi60390962.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SMARCAL1base

SMARCAL1 mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF082179 mRNA. Translation: AAF24984.1 .
AF210842
, 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.
CCDSi CCDS2403.1.
PIRi T34557.
RefSeqi NP_001120679.1. NM_001127207.1.
NP_054859.2. NM_014140.3.
XP_005246688.1. XM_005246631.2.
XP_005246689.1. XM_005246632.1.
UniGenei Hs.516674.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4MQV X-ray 1.95 B/D 5-30 [» ]
ProteinModelPortali Q9NZC9.
SMRi Q9NZC9. Positions 238-302, 330-397, 409-840.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119072. 6 interactions.
IntActi Q9NZC9. 3 interactions.
MINTi MINT-8415341.
STRINGi 9606.ENSP00000349823.

PTM databases

PhosphoSitei Q9NZC9.

Polymorphism databases

DMDMi 60390962.

Proteomic databases

MaxQBi Q9NZC9.
PaxDbi Q9NZC9.
PRIDEi Q9NZC9.

Protocols and materials databases

DNASUi 50485.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000357276 ; ENSP00000349823 ; ENSG00000138375 .
ENST00000358207 ; ENSP00000350940 ; ENSG00000138375 .
GeneIDi 50485.
KEGGi hsa:50485.
UCSCi uc002vgc.4. human.

Organism-specific databases

CTDi 50485.
GeneCardsi GC02P217277.
GeneReviewsi SMARCAL1.
HGNCi HGNC:11102. SMARCAL1.
HPAi HPA020337.
MIMi 242900. phenotype.
606622. gene.
neXtProti NX_Q9NZC9.
Orphaneti 1830. Schimke immuno-osseous dysplasia.
PharmGKBi PA35952.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0553.
GeneTreei ENSGT00630000089754.
HOVERGENi HBG054110.
InParanoidi Q9NZC9.
KOi K14440.
OMAi SIHYLVA.
OrthoDBi EOG7XSTD5.
PhylomeDBi Q9NZC9.
TreeFami TF106474.

Miscellaneous databases

ChiTaRSi SMARCAL1. human.
GeneWikii SMARCAL1.
GenomeRNAii 50485.
NextBioi 53040.
PROi Q9NZC9.
SOURCEi Search...

Gene expression databases

Bgeei Q9NZC9.
CleanExi HS_SMARCAL1.
ExpressionAtlasi Q9NZC9. baseline and differential.
Genevestigatori Q9NZC9.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR010003. HARP_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view ]
Pfami PF07443. HARP. 2 hits.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 3 hits.
PROSITEi PS51467. HARP. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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. 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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. 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.

Entry informationi

Entry nameiSMAL1_HUMAN
AccessioniPrimary (citable) accession number: Q9NZC9
Secondary accession number(s): A6NEH0
, Q53R00, Q96AY1, Q9NXQ5, Q9UFH3, Q9UI93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3