Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q7Z5K2 (WAPL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Wings apart-like protein homolog
Alternative name(s):
Friend of EBNA2 protein
Gene names
Name:WAPAL
Synonyms:FOE, KIAA0261, WAPL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1190 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulator of sister chromatid cohesion in mitosis which negatively regulates cohesin association with chromatin. Involved in both sister chromatid cohesion during interphase and sister-chromatid resolution during early stages of mitosis. Couples DNA replication to sister chromatid cohesion. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Ref.1 Ref.8 Ref.9 Ref.14 Ref.16 Ref.19 Ref.23

Subunit structure

Interacts with the cohesin complex throughout the cell cycle; interacts with both chromatin-bound and soluble pools of the complex. Interacts with RAD21; the interaction is direct. Interacts with PDS5A; the interaction is direct, cohesin-dependent and competitive with CDCA5/SORORIN. Interacts (via FGF motifs) with PDS5B; the interaction is direct. Interacts with a SMC1 protein (SMC1A or SMC1B) and SMC3. Isoform 2 interacts with Epstein-Barr virus EBNA2. Ref.2 Ref.8 Ref.9 Ref.14 Ref.16 Ref.19 Ref.23

Subcellular location

Isoform 2: Nucleus.

Nucleus. Chromosome. Cytoplasm. Note: Associates with chromatin through the cohesin complex during interphase. Released in the cytoplasm from nuclear envelope breakdown until anaphase, it reaccumulates in nucleus at telophase. Ref.2 Ref.8 Ref.9

Tissue specificity

Isoform 1 is highly expressed in uterine cervix tumor. Isoform 2 is widely expressed with a high level in skeletal muscle and heart. Ref.1 Ref.2

Sequence similarities

Belongs to the WAPL family.

Contains 1 WAPL domain.

Sequence caution

The sequence BAA13391.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAH73376.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI16708.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Host-virus interaction
Mitosis
   Cellular componentChromosome
Cytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of DNA replication

Inferred from mutant phenotype Ref.16. Source: UniProtKB

negative regulation of chromatin binding

Inferred from mutant phenotype Ref.8Ref.14. Source: UniProtKB

negative regulation of sister chromatid cohesion

Inferred from mutant phenotype Ref.8Ref.14Ref.19. Source: UniProtKB

protein localization to chromatin

Inferred from mutant phenotype Ref.19. Source: UniProtKB

regulation of cohesin localization to chromatin

Inferred from mutant phenotype Ref.8. Source: UniProtKB

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromatin

Inferred from direct assay Ref.8Ref.14. Source: UniProtKB

chromosome

Traceable author statement. Source: Reactome

chromosome, centromeric region

Traceable author statement. Source: Reactome

cohesin complex

Inferred from direct assay Ref.8Ref.14. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.8Ref.14. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.8Ref.14. Source: UniProtKB

synaptonemal complex

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDS5BQ9NTI59EBI-1022242,EBI-1175604
RAD21O6021611EBI-1022242,EBI-80739

Alternative products

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

Note: Named isoforms=2.
Isoform 1 (identifier: Q7Z5K2-1)

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: Q7Z5K2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVQGPVQTPALTIHRRKRRRRRRRRPVAKAPARLRGEYETGVKM
     510-515: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q7Z5K2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVQGPVQTPA...RGEYETGVKM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11901190Wings apart-like protein homolog
PRO_0000245232

Regions

Domain626 – 1169544WAPL
Region1 – 659659Mediates interaction with the cohesin complex
Coiled coil260 – 28627 Potential
Coiled coil749 – 78234 Potential
Motif73 – 753FGF motif 1
Motif429 – 4313FGF motif 2
Motif453 – 4553FGF motif 3

Amino acid modifications

Modified residue771Phosphoserine Ref.10 Ref.11 Ref.15 Ref.17 Ref.20 Ref.22
Modified residue1681N6-acetyllysine Ref.18
Modified residue2211Phosphoserine Ref.11 Ref.20 Ref.22
Modified residue2231Phosphoserine Ref.11 Ref.12
Modified residue2261Phosphoserine Ref.7 Ref.10 Ref.11 Ref.20 Ref.22
Modified residue3801Phosphoserine Ref.11 Ref.17
Modified residue4591Phosphoserine Ref.11
Modified residue4611Phosphoserine Ref.11
Modified residue9041Phosphoserine Ref.11

Natural variations

Alternative sequence11M → MVQGPVQTPALTIHRRKRRR RRRRRPVAKAPARLRGEYET GVKM in isoform 2.
VSP_019649
Alternative sequence11M → MVQGPVQTPALTIHRRKRRR SCPPNRASYLPKAESLASLG SHLPALLSRARVPRPPAGRR ERERRRRPVAKAPARLRGEY ETGVKM in isoform 3.
VSP_019650
Alternative sequence510 – 5156Missing in isoform 2.
VSP_019651
Natural variant1241V → I.
Corresponds to variant rs10887621 [ dbSNP | Ensembl ].
VAR_026967

Experimental info

Mutagenesis73 – 753FGF → EGE: Loss of interaction with PDS5B; when associated with 429-E--E-431 and 453-E--E-455.
Mutagenesis429 – 4313FGF → EGE: Loss of interaction with PDS5B; when associated with 73-E--E-75 and 453-E--E-455. Ref.14
Mutagenesis453 – 4553FGF → EGE: Loss of interaction with PDS5B; when associated with 73-E--E-75 and 429-E--E-431. Ref.14
Mutagenesis639 – 6402VK → AE: Impaired sister chromatid cohesion and resolution.
Mutagenesis656 – 6572DD → KK: Impaired sister chromatid cohesion and resolution.
Mutagenesis7701E → K: No effect. Ref.23
Mutagenesis7771E → K: No effect. Ref.23
Mutagenesis7871E → K: No effect. Ref.23
Mutagenesis7901T → A: No effect. Ref.23
Mutagenesis11161M → A: Impaired sister chromatid cohesion and resolution; when associated with A-1120. Ref.23
Mutagenesis11201I → A: Impaired sister chromatid cohesion and resolution; when associated with A-1116. Ref.23

Secondary structure

.............................................................. 1190
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 2003. Version 1.
Checksum: A01026E520BFAB2F

FASTA1,190132,946
        10         20         30         40         50         60 
MTSRFGKTYS RKGGNGSSKF DEVFSNKRTT LSTKWGETTF MAKLGQKRPN FKPDIQEIPK 

        70         80         90        100        110        120 
KPKVEEESTG DPFGFDSDDE SLPVSSKNLA QVKCSSYSES SEAAQLEEVT SVLEANSKIS 

       130        140        150        160        170        180 
HVVVEDTVVS DKCFPLEDTL LGKEKSTNRI VEDDASISSC NKLITSDKVE NFHEEHEKNS 

       190        200        210        220        230        240 
HHIHKNADDS TKKPNAETTV ASEIKETNDT WNSQFGKRPE SPSEISPIKG SVRTGLFEWD 

       250        260        270        280        290        300 
NDFEDIRSED CILSLDSDPL LEMKDDDFKN RLENLNEAIE EDIVQSVLRP TNCRTYCRAN 

       310        320        330        340        350        360 
KTKSSQGASN FDKLMDGTSQ ALAKANSESS KDGLNQAKKG GVSCGTSFRG TVGRTRDYTV 

       370        380        390        400        410        420 
LHPSCLSVCN VTIQDTMERS MDEFTASTPA DLGEAGRLRK KADIATSKTT TRFRPSNTKS 

       430        440        450        460        470        480 
KKDVKLEFFG FEDHETGGDE GGSGSSNYKI KYFGFDDLSE SEDDEDDDCQ VERKTSKKRT 

       490        500        510        520        530        540 
KTAPSPSLQP PPESNDNSQD SQSGTNNAEN LDFTEDLPGV PESVKKPINK QGDKSKENTR 

       550        560        570        580        590        600 
KIFSGPKRSP TKAVYNARHW NHPDSEELPG PPVVKPQSVT VRLSSKEPNQ KDDGVFKAPA 

       610        620        630        640        650        660 
PPSKVIKTVT IPTQPYQDIV TALKCRREDK ELYTVVQHVK HFNDVVEFGE NQEFTDDIEY 

       670        680        690        700        710        720 
LLSGLKSTQP LNTRCLSVIS LATKCAMPSF RMHLRAHGMV AMVFKTLDDS QHHQNLSLCT 

       730        740        750        760        770        780 
AALMYILSRD RLNMDLDRAS LDLMIRLLEL EQDASSAKLL NEKDMNKIKE KIRRLCETVH 

       790        800        810        820        830        840 
NKHLDLENIT TGHLAMETLL SLTSKRAGDW FKEELRLLGG LDHIVDKVKE CVDHLSRDED 

       850        860        870        880        890        900 
EEKLVASLWG AERCLRVLES VTVHNPENQS YLIAYKDSQL IVSSAKALQH CEELIQQYNR 

       910        920        930        940        950        960 
AEDSICLADS KPLPHQNVTN HVGKAVEDCM RAIIGVLLNL TNDNEWGSTK TGEQDGLIGT 

       970        980        990       1000       1010       1020 
ALNCVLQVPK YLPQEQRFDI RVLGLGLLIN LVEYSARNRH CLVNMETSCS FDSSICSGEG 

      1030       1040       1050       1060       1070       1080 
DDSLRIGGQV HAVQALVQLF LERERAAQLA ESKTDELIKD APTTQHDKSG EWQETSGEIQ 

      1090       1100       1110       1120       1130       1140 
WVSTEKTDGT EEKHKKEEED EELDLNKALQ HAGKHMEDCI VASYTALLLG CLCQESPINV 

      1150       1160       1170       1180       1190 
TTVREYLPEG DFSIMTEMLK KFLSFMNLTC AVGTTGQKSI SRVIEYLEHC 

« Hide

Isoform 2 [UniParc].

Checksum: 5431910072375C05
Show »

FASTA1,227137,314
Isoform 3 [UniParc].

Checksum: 5588D17DBB5C782F
Show »

FASTA1,275142,525

References

« Hide 'large scale' references
[1]"Expression of a novel human gene, human wings apart-like (hWAPL), is associated with cervical carcinogenesis and tumor progression."
Oikawa K., Ohbayashi T., Kiyono T., Nishi H., Isaka K., Umezawa A., Kuroda M., Mukai K.
Cancer Res. 64:3545-3549(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
[2]"Identification and cloning of a novel chromatin-associated protein partner of Epstein-Barr nuclear protein 2."
Kwiatkowski B.A., Ragoczy T., Ehly J., Schubach W.H.
Exp. Cell Res. 300:223-233(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH EPSTEIN-BARR VIRUS EBNA2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]"Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Bone marrow.
[4]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 1).
[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-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Wapl controls the dynamic association of cohesin with chromatin."
Kueng S., Hegemann B., Peters B.H., Lipp J.J., Schleiffer A., Mechtler K., Peters J.M.
Cell 127:955-967(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH THE COHESIN COMPLEX AND PDS5A, SUBCELLULAR LOCATION.
[9]"Human Wapl is a cohesin-binding protein that promotes sister-chromatid resolution in mitotic prophase."
Gandhi R., Gillespie P.J., Hirano T.
Curr. Biol. 16:2406-2417(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH THE COHESIN COMPLEX, SUBCELLULAR LOCATION.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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-77; SER-221; SER-223; SER-226; SER-380; SER-459; SER-461 AND SER-904, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]Carrascal M., Abian J.
Submitted (JAN-2008) to UniProtKB
Cited for: PHOSPHORYLATION AT SER-223, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: T-cell.
[13]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Releasing cohesin from chromosome arms in early mitosis: opposing actions of Wapl-Pds5 and Sgo1."
Shintomi K., Hirano T.
Genes Dev. 23:2224-2236(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PDS5B AND RAD21, MUTAGENESIS OF 73-PHE--PHE-75; 429-PHE--PHE-431 AND 453-PHE--PHE-455, FGF MOTIFS.
[15]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Cohesin acetylation speeds the replication fork."
Terret M.E., Sherwood R., Rahman S., Qin J., Jallepalli P.V.
Nature 462:231-234(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SMC3.
[17]"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 SER-77 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-168, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Sororin mediates sister chromatid cohesion by antagonizing wapl."
Nishiyama T., Ladurner R., Schmitz J., Kreidl E., Schleiffer A., Bhaskara V., Bando M., Shirahige K., Hyman A.A., Mechtler K., Peters J.M.
Cell 143:737-749(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PDS5A.
[20]"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-77; SER-221 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"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].
[22]"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 SER-77; SER-221 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Structure of the human cohesin inhibitor Wapl."
Ouyang Z., Zheng G., Song J., Borek D.M., Otwinowski Z., Brautigam C.A., Tomchick D.R., Rankin S., Yu H.
Proc. Natl. Acad. Sci. U.S.A. 110:11355-11360(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 631-1190, FUNCTION, INTERACTION WITH PDS5A; SMC1; SMC3; STAG2 AND CDCA5, SUBUNIT, MUTAGENESIS OF 639-VAL-LYS-640; 656-ASP-ASP-657; GLU-770; GLU-777; GLU-787; THR-790; MET-1116 AND ILE-1120.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB065003 mRNA. Translation: BAC78631.1.
AF479418 mRNA. Translation: AAO14651.1.
D87450 mRNA. Translation: BAA13391.1. Different initiation.
AL844892, AL731569 Genomic DNA. Translation: CAH73376.1. Sequence problems.
AL731569, AL844892 Genomic DNA. Translation: CAI16708.1. Sequence problems.
CH471142 Genomic DNA. Translation: EAW80336.1.
BC150269 mRNA. Translation: AAI50270.1.
RefSeqNP_055860.1. NM_015045.2.
UniGeneHs.203099.
Hs.714876.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4K6JX-ray2.62A/B631-1190[»]
ProteinModelPortalQ7Z5K2.
SMRQ7Z5K2. Positions 631-1190.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116698. 23 interactions.
IntActQ7Z5K2. 14 interactions.
MINTMINT-4123122.
STRING9606.ENSP00000298767.

PTM databases

PhosphoSiteQ7Z5K2.

Polymorphism databases

DMDM74713658.

Proteomic databases

PaxDbQ7Z5K2.
PRIDEQ7Z5K2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000298767; ENSP00000298767; ENSG00000062650. [Q7Z5K2-1]
GeneID23063.
KEGGhsa:23063.
UCSCuc001kdn.3. human. [Q7Z5K2-2]
uc001kdo.3. human. [Q7Z5K2-1]

Organism-specific databases

CTD23063.
GeneCardsGC10M088185.
HGNCHGNC:23293. WAPAL.
HPAHPA037874.
HPA037875.
MIM610754. gene.
neXtProtNX_Q7Z5K2.
PharmGKBPA134872402.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG297597.
HOGENOMHOG000001563.
HOVERGENHBG088338.
InParanoidQ7Z5K2.
OMAWNSQFGK.
OrthoDBEOG7DZ8J3.
PhylomeDBQ7Z5K2.
TreeFamTF323477.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ7Z5K2.
BgeeQ7Z5K2.
CleanExHS_WAPAL.
GenevestigatorQ7Z5K2.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR012502. WAPL_metazoan_plants.
IPR022771. WAPL_prot.
[Graphical view]
PfamPF07814. WAPL. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 2 hits.
PROSITEPS51271. WAPL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSWAPAL. human.
GeneWikiWAPAL.
GenomeRNAi23063.
NextBio44141.
PROQ7Z5K2.
SOURCESearch...

Entry information

Entry nameWAPL_HUMAN
AccessionPrimary (citable) accession number: Q7Z5K2
Secondary accession number(s): A7E2B5 expand/collapse secondary AC list , Q5VSK5, Q8IX10, Q92549
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: October 1, 2003
Last modified: April 16, 2014
This is version 87 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 10

Human chromosome 10: entries, gene names and cross-references to MIM