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Protein

ATPase SWSAP1

Gene

SWSAP1

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

Functioni

ATPase which is preferentially stimulated by single-stranded DNA and is involved in homologous recombination repair (HRR). Has a DNA-binding activity which is independent of its ATPase activity.1 Publication

GO - Molecular functioni

  • ATPase activity Source: UniProtKB
  • single-stranded DNA binding Source: UniProtKB

GO - Biological processi

  • double-strand break repair via homologous recombination Source: UniProtKB
  • protein stabilization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATPase SWSAP1
Alternative name(s):
SWIM-type zinc finger 7-associated protein 1
SWS1-associated protein 1
ZSWIM7-associated protein 1
Short name:
ZSWIM7AP1
Gene namesi
Name:SWSAP1
Synonyms:C19orf39
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:26638. SWSAP1.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • nucleus Source: UniProtKB-SubCell
  • Shu complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi18 – 181K → A: Loss of function in HRR associated with altered ssDNA-stimulated ATPase activity. 1 Publication
Mutagenesisi96 – 961D → A: Loss of function in HRR associated with altered ssDNA-stimulated ATPase activity. 1 Publication

Organism-specific databases

PharmGKBiPA144596472.

Polymorphism and mutation databases

BioMutaiSWSAP1.
DMDMi74736850.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 229229ATPase SWSAP1PRO_0000294240Add
BLAST

Proteomic databases

EPDiQ6NVH7.
MaxQBiQ6NVH7.
PaxDbiQ6NVH7.
PeptideAtlasiQ6NVH7.
PRIDEiQ6NVH7.

PTM databases

iPTMnetiQ6NVH7.
PhosphoSiteiQ6NVH7.

Expressioni

Gene expression databases

BgeeiQ6NVH7.
CleanExiHS_C19orf39.
GenevisibleiQ6NVH7. HS.

Organism-specific databases

HPAiHPA052712.

Interactioni

Subunit structurei

Interacts with ZSWIM7; they form a functional complex involved in homologous recombination repair and stabilize each other. Interacts with RAD51, RAD51B, RAD51C, RAD51D and XRCC3; involved in homologous recombination repair.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RAD51Q066092EBI-5281637,EBI-297202
RAD51BO153152EBI-5281637,EBI-2824089
RAD51CO435022EBI-5281637,EBI-2267048
RAD51DO757712EBI-5281637,EBI-1055693
XRCC3O435422EBI-5281637,EBI-2849976
ZSWIM7Q19AV67EBI-5281637,EBI-5281647

Protein-protein interaction databases

BioGridi125954. 10 interactions.
IntActiQ6NVH7. 6 interactions.
STRINGi9606.ENSP00000310008.

Structurei

3D structure databases

ProteinModelPortaliQ6NVH7.
SMRiQ6NVH7. Positions 6-103.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiENOG410IGP0. Eukaryota.
ENOG41128AG. LUCA.
GeneTreeiENSGT00390000007170.
HOGENOMiHOG000001573.
HOVERGENiHBG094964.
InParanoidiQ6NVH7.
OMAiWPTQAGD.
OrthoDBiEOG7K9K4S.
PhylomeDBiQ6NVH7.
TreeFamiTF337313.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR033586. SWSAP1.
[Graphical view]
PANTHERiPTHR28653. PTHR28653. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6NVH7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAAGPPLLL LGTPGSGKTA LLFAAALEAA GEGQGPVLFL TRRPLQSMPR
60 70 80 90 100
GTGTTLDPMR LQKIRFQYPP STRELFRLLC SAHEAPGPAP SLLLLDGLEE
110 120 130 140 150
YLAEDPEPQE AAYLIALLLD TAAHFSHRLG PGRDCGLMVA LQTQEEAGSG
160 170 180 190 200
DVLHLALLQR YFPAQCWLQP DAPGPGEHGL RACLEPGGLG PRTEWWVTFR
210 220
SDGEMMIAPW PTQAGDPSSG KGSSSGGQP
Length:229
Mass (Da):24,311
Last modified:July 5, 2004 - v1
Checksum:iAB940178B7A4A6C6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1131Y → C in BAC03891 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti171 – 1711D → G.
Corresponds to variant rs317926 [ dbSNP | Ensembl ].
VAR_033151

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK092438 mRNA. Translation: BAC03891.1.
AC024575 Genomic DNA. No translation available.
BC068071 mRNA. Translation: AAH68071.1.
BC119677 mRNA. Translation: AAI19678.1.
CCDSiCCDS12259.1.
RefSeqiNP_787067.2. NM_175871.3.
UniGeneiHs.631619.

Genome annotation databases

EnsembliENST00000312423; ENSP00000310008; ENSG00000173928.
GeneIDi126074.
KEGGihsa:126074.
UCSCiuc002mrg.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK092438 mRNA. Translation: BAC03891.1.
AC024575 Genomic DNA. No translation available.
BC068071 mRNA. Translation: AAH68071.1.
BC119677 mRNA. Translation: AAI19678.1.
CCDSiCCDS12259.1.
RefSeqiNP_787067.2. NM_175871.3.
UniGeneiHs.631619.

3D structure databases

ProteinModelPortaliQ6NVH7.
SMRiQ6NVH7. Positions 6-103.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125954. 10 interactions.
IntActiQ6NVH7. 6 interactions.
STRINGi9606.ENSP00000310008.

PTM databases

iPTMnetiQ6NVH7.
PhosphoSiteiQ6NVH7.

Polymorphism and mutation databases

BioMutaiSWSAP1.
DMDMi74736850.

Proteomic databases

EPDiQ6NVH7.
MaxQBiQ6NVH7.
PaxDbiQ6NVH7.
PeptideAtlasiQ6NVH7.
PRIDEiQ6NVH7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312423; ENSP00000310008; ENSG00000173928.
GeneIDi126074.
KEGGihsa:126074.
UCSCiuc002mrg.2. human.

Organism-specific databases

CTDi126074.
GeneCardsiSWSAP1.
HGNCiHGNC:26638. SWSAP1.
HPAiHPA052712.
MIMi614536. gene.
neXtProtiNX_Q6NVH7.
PharmGKBiPA144596472.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGP0. Eukaryota.
ENOG41128AG. LUCA.
GeneTreeiENSGT00390000007170.
HOGENOMiHOG000001573.
HOVERGENiHBG094964.
InParanoidiQ6NVH7.
OMAiWPTQAGD.
OrthoDBiEOG7K9K4S.
PhylomeDBiQ6NVH7.
TreeFamiTF337313.

Miscellaneous databases

GenomeRNAii126074.
PROiQ6NVH7.
SOURCEiSearch...

Gene expression databases

BgeeiQ6NVH7.
CleanExiHS_C19orf39.
GenevisibleiQ6NVH7. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR033586. SWSAP1.
[Graphical view]
PANTHERiPTHR28653. PTHR28653. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Placenta.
  2. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Spleen.
  4. "hSWS1.SWSAP1 is an evolutionarily conserved complex required for efficient homologous recombination repair."
    Liu T., Wan L., Wu Y., Chen J., Huang J.
    J. Biol. Chem. 286:41758-41766(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HOMOLOGOUS RECOMBINATION REPAIR, SUBCELLULAR LOCATION, ATPASE ACTIVITY, DNA-BINDING ACTIVITY, INTERACTION WITH RAD51; RAD51B; RAD51C; RAD51D; XRCC3; ZSWIM7, MUTAGENESIS OF LYS-18 AND ASP-96.

Entry informationi

Entry nameiSWAP1_HUMAN
AccessioniPrimary (citable) accession number: Q6NVH7
Secondary accession number(s): Q8NAM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 89 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.