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Q7Z5K2

- WAPL_HUMAN

UniProt

Q7Z5K2 - WAPL_HUMAN

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Protein

Wings apart-like protein homolog

Gene

WAPAL

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

Functioni

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.7 Publications

GO - Biological processi

  1. mitotic cell cycle Source: Reactome
  2. mitotic nuclear division Source: UniProtKB-KW
  3. negative regulation of chromatin binding Source: UniProtKB
  4. negative regulation of DNA replication Source: UniProtKB
  5. negative regulation of sister chromatid cohesion Source: UniProtKB
  6. positive regulation of fibroblast proliferation Source: Ensembl
  7. protein localization to chromatin Source: UniProtKB
  8. regulation of chromosome condensation Source: Ensembl
  9. regulation of cohesin localization to chromatin Source: UniProtKB
  10. response to toxic substance Source: Ensembl
  11. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Host-virus interaction, Mitosis

Enzyme and pathway databases

ReactomeiREACT_150266. Establishment of Sister Chromatid Cohesion.
REACT_150421. Cohesin Loading onto Chromatin.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.

Names & Taxonomyi

Protein namesi
Recommended name:
Wings apart-like protein homolog
Alternative name(s):
Friend of EBNA2 protein
Gene namesi
Name:WAPAL
Synonyms:FOE, KIAA0261, WAPL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:23293. WAPAL.

Subcellular locationi

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.

GO - Cellular componenti

  1. chromatin Source: UniProtKB
  2. chromosome Source: Reactome
  3. chromosome, centromeric region Source: Reactome
  4. cohesin complex Source: UniProtKB
  5. cytoplasm Source: UniProtKB
  6. cytosol Source: Reactome
  7. intracellular membrane-bounded organelle Source: HPA
  8. microtubule cytoskeleton Source: HPA
  9. nucleoplasm Source: Reactome
  10. nucleus Source: UniProtKB
  11. synaptonemal complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 753FGF → EGE: Loss of interaction with PDS5B; when associated with 429-E--E-431 and 453-E--E-455. 1 Publication
Mutagenesisi429 – 4313FGF → EGE: Loss of interaction with PDS5B; when associated with 73-E--E-75 and 453-E--E-455. 1 Publication
Mutagenesisi453 – 4553FGF → EGE: Loss of interaction with PDS5B; when associated with 73-E--E-75 and 429-E--E-431. 1 Publication
Mutagenesisi639 – 6402VK → AE: Impaired sister chromatid cohesion and resolution. 1 Publication
Mutagenesisi656 – 6572DD → KK: Impaired sister chromatid cohesion and resolution. 1 Publication
Mutagenesisi770 – 7701E → K: No effect. 1 Publication
Mutagenesisi777 – 7771E → K: No effect. 1 Publication
Mutagenesisi787 – 7871E → K: No effect. 1 Publication
Mutagenesisi790 – 7901T → A: No effect. 1 Publication
Mutagenesisi1116 – 11161M → A: Impaired sister chromatid cohesion and resolution; when associated with A-1120. 1 Publication
Mutagenesisi1120 – 11201I → A: Impaired sister chromatid cohesion and resolution; when associated with A-1116. 1 Publication

Organism-specific databases

PharmGKBiPA134872402.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11901190Wings apart-like protein homologPRO_0000245232Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei77 – 771Phosphoserine6 Publications
Modified residuei168 – 1681N6-acetyllysine1 Publication
Modified residuei221 – 2211Phosphoserine3 Publications
Modified residuei223 – 2231Phosphoserine1 Publication
Modified residuei226 – 2261Phosphoserine5 Publications
Modified residuei380 – 3801Phosphoserine2 Publications
Modified residuei459 – 4591Phosphoserine1 Publication
Modified residuei461 – 4611Phosphoserine1 Publication
Modified residuei904 – 9041Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ7Z5K2.
PaxDbiQ7Z5K2.
PRIDEiQ7Z5K2.

PTM databases

PhosphoSiteiQ7Z5K2.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ7Z5K2.
CleanExiHS_WAPAL.
ExpressionAtlasiQ7Z5K2. baseline and differential.
GenevestigatoriQ7Z5K2.

Organism-specific databases

HPAiHPA037874.
HPA037875.

Interactioni

Subunit structurei

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 EBNA2.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PDS5BQ9NTI59EBI-1022242,EBI-1175604
RAD21O6021611EBI-1022242,EBI-80739

Protein-protein interaction databases

BioGridi116698. 30 interactions.
DIPiDIP-31176N.
IntActiQ7Z5K2. 14 interactions.
MINTiMINT-4123122.
STRINGi9606.ENSP00000298767.

Structurei

Secondary structure

1
1190
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi631 – 64010Combined sources
Helixi652 – 66413Combined sources
Helixi671 – 68414Combined sources
Helixi688 – 6969Combined sources
Helixi700 – 7067Combined sources
Turni707 – 7093Combined sources
Helixi710 – 7123Combined sources
Helixi714 – 72714Combined sources
Turni733 – 7353Combined sources
Helixi738 – 74912Combined sources
Helixi765 – 78016Combined sources
Helixi786 – 7883Combined sources
Helixi791 – 80212Combined sources
Turni805 – 8073Combined sources
Helixi810 – 8178Combined sources
Helixi820 – 83617Combined sources
Helixi841 – 86222Combined sources
Helixi866 – 89732Combined sources
Beta strandi909 – 9113Combined sources
Helixi917 – 94125Combined sources
Helixi945 – 9528Combined sources
Helixi957 – 96610Combined sources
Helixi968 – 9714Combined sources
Helixi974 – 9763Combined sources
Helixi977 – 99216Combined sources
Helixi996 – 10038Combined sources
Helixi1032 – 105827Combined sources
Helixi1107 – 113529Combined sources
Helixi1137 – 114610Combined sources
Helixi1148 – 11503Combined sources
Helixi1153 – 116917Combined sources
Helixi1174 – 118815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4K6JX-ray2.62A/B631-1190[»]
ProteinModelPortaliQ7Z5K2.
SMRiQ7Z5K2. Positions 631-1190.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini626 – 1169544WAPLPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 659659Mediates interaction with the cohesin complexAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili260 – 28627Sequence AnalysisAdd
BLAST
Coiled coili749 – 78234Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi73 – 753FGF motif 1
Motifi429 – 4313FGF motif 2
Motifi453 – 4553FGF motif 3

Sequence similaritiesi

Belongs to the WAPL family.Curated
Contains 1 WAPL domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG297597.
GeneTreeiENSGT00390000015768.
HOGENOMiHOG000001563.
HOVERGENiHBG088338.
InParanoidiQ7Z5K2.
OMAiWNSQFGK.
OrthoDBiEOG7DZ8J3.
PhylomeDBiQ7Z5K2.
TreeFamiTF323477.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR012502. WAPL_metazoan_plants.
IPR022771. WAPL_prot.
[Graphical view]
PfamiPF07814. WAPL. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
PROSITEiPS51271. WAPL. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Named isoforms=2.

Isoform 1 (identifier: Q7Z5K2-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MTSRFGKTYS RKGGNGSSKF DEVFSNKRTT LSTKWGETTF MAKLGQKRPN
60 70 80 90 100
FKPDIQEIPK KPKVEEESTG DPFGFDSDDE SLPVSSKNLA QVKCSSYSES
110 120 130 140 150
SEAAQLEEVT SVLEANSKIS HVVVEDTVVS DKCFPLEDTL LGKEKSTNRI
160 170 180 190 200
VEDDASISSC NKLITSDKVE NFHEEHEKNS HHIHKNADDS TKKPNAETTV
210 220 230 240 250
ASEIKETNDT WNSQFGKRPE SPSEISPIKG SVRTGLFEWD NDFEDIRSED
260 270 280 290 300
CILSLDSDPL LEMKDDDFKN RLENLNEAIE EDIVQSVLRP TNCRTYCRAN
310 320 330 340 350
KTKSSQGASN FDKLMDGTSQ ALAKANSESS KDGLNQAKKG GVSCGTSFRG
360 370 380 390 400
TVGRTRDYTV LHPSCLSVCN VTIQDTMERS MDEFTASTPA DLGEAGRLRK
410 420 430 440 450
KADIATSKTT TRFRPSNTKS KKDVKLEFFG FEDHETGGDE GGSGSSNYKI
460 470 480 490 500
KYFGFDDLSE SEDDEDDDCQ VERKTSKKRT KTAPSPSLQP PPESNDNSQD
510 520 530 540 550
SQSGTNNAEN LDFTEDLPGV PESVKKPINK QGDKSKENTR KIFSGPKRSP
560 570 580 590 600
TKAVYNARHW NHPDSEELPG PPVVKPQSVT VRLSSKEPNQ KDDGVFKAPA
610 620 630 640 650
PPSKVIKTVT IPTQPYQDIV TALKCRREDK ELYTVVQHVK HFNDVVEFGE
660 670 680 690 700
NQEFTDDIEY LLSGLKSTQP LNTRCLSVIS LATKCAMPSF RMHLRAHGMV
710 720 730 740 750
AMVFKTLDDS QHHQNLSLCT AALMYILSRD RLNMDLDRAS LDLMIRLLEL
760 770 780 790 800
EQDASSAKLL NEKDMNKIKE KIRRLCETVH NKHLDLENIT TGHLAMETLL
810 820 830 840 850
SLTSKRAGDW FKEELRLLGG LDHIVDKVKE CVDHLSRDED EEKLVASLWG
860 870 880 890 900
AERCLRVLES VTVHNPENQS YLIAYKDSQL IVSSAKALQH CEELIQQYNR
910 920 930 940 950
AEDSICLADS KPLPHQNVTN HVGKAVEDCM RAIIGVLLNL TNDNEWGSTK
960 970 980 990 1000
TGEQDGLIGT ALNCVLQVPK YLPQEQRFDI RVLGLGLLIN LVEYSARNRH
1010 1020 1030 1040 1050
CLVNMETSCS FDSSICSGEG DDSLRIGGQV HAVQALVQLF LERERAAQLA
1060 1070 1080 1090 1100
ESKTDELIKD APTTQHDKSG EWQETSGEIQ WVSTEKTDGT EEKHKKEEED
1110 1120 1130 1140 1150
EELDLNKALQ HAGKHMEDCI VASYTALLLG CLCQESPINV TTVREYLPEG
1160 1170 1180 1190
DFSIMTEMLK KFLSFMNLTC AVGTTGQKSI SRVIEYLEHC
Length:1,190
Mass (Da):132,946
Last modified:October 1, 2003 - v1
Checksum:iA01026E520BFAB2F
GO
Isoform 2 (identifier: Q7Z5K2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVQGPVQTPALTIHRRKRRRRRRRRPVAKAPARLRGEYETGVKM
     510-515: Missing.

Note: No experimental confirmation available.

Show »
Length:1,227
Mass (Da):137,314
Checksum:i5431910072375C05
GO
Isoform 3 (identifier: Q7Z5K2-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVQGPVQTPA...RGEYETGVKM

Note: No experimental confirmation available.

Show »
Length:1,275
Mass (Da):142,525
Checksum:i5588D17DBB5C782F
GO

Sequence cautioni

The sequence BAA13391.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAH73376.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI16708.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti124 – 1241V → I.
Corresponds to variant rs10887621 [ dbSNP | Ensembl ].
VAR_026967

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MVQGPVQTPALTIHRRKRRR RRRRRPVAKAPARLRGEYET GVKM in isoform 2. 1 PublicationVSP_019649
Alternative sequencei1 – 11M → MVQGPVQTPALTIHRRKRRR SCPPNRASYLPKAESLASLG SHLPALLSRARVPRPPAGRR ERERRRRPVAKAPARLRGEY ETGVKM in isoform 3. 1 PublicationVSP_019650
Alternative sequencei510 – 5156Missing in isoform 2. 1 PublicationVSP_019651

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7375.1. [Q7Z5K2-1]
RefSeqiNP_055860.1. NM_015045.2. [Q7Z5K2-1]
UniGeneiHs.203099.
Hs.714876.

Genome annotation databases

EnsembliENST00000298767; ENSP00000298767; ENSG00000062650. [Q7Z5K2-1]
ENST00000618527; ENSP00000481451; ENSG00000062650. [Q7Z5K2-1]
GeneIDi23063.
KEGGihsa:23063.
UCSCiuc001kdn.3. human. [Q7Z5K2-2]
uc001kdo.3. human. [Q7Z5K2-1]

Polymorphism databases

DMDMi74713658.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS7375.1. [Q7Z5K2-1 ]
RefSeqi NP_055860.1. NM_015045.2. [Q7Z5K2-1 ]
UniGenei Hs.203099.
Hs.714876.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4K6J X-ray 2.62 A/B 631-1190 [» ]
ProteinModelPortali Q7Z5K2.
SMRi Q7Z5K2. Positions 631-1190.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116698. 30 interactions.
DIPi DIP-31176N.
IntActi Q7Z5K2. 14 interactions.
MINTi MINT-4123122.
STRINGi 9606.ENSP00000298767.

PTM databases

PhosphoSitei Q7Z5K2.

Polymorphism databases

DMDMi 74713658.

Proteomic databases

MaxQBi Q7Z5K2.
PaxDbi Q7Z5K2.
PRIDEi Q7Z5K2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000298767 ; ENSP00000298767 ; ENSG00000062650 . [Q7Z5K2-1 ]
ENST00000618527 ; ENSP00000481451 ; ENSG00000062650 . [Q7Z5K2-1 ]
GeneIDi 23063.
KEGGi hsa:23063.
UCSCi uc001kdn.3. human. [Q7Z5K2-2 ]
uc001kdo.3. human. [Q7Z5K2-1 ]

Organism-specific databases

CTDi 23063.
GeneCardsi GC10M088185.
HGNCi HGNC:23293. WAPAL.
HPAi HPA037874.
HPA037875.
MIMi 610754. gene.
neXtProti NX_Q7Z5K2.
PharmGKBi PA134872402.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG297597.
GeneTreei ENSGT00390000015768.
HOGENOMi HOG000001563.
HOVERGENi HBG088338.
InParanoidi Q7Z5K2.
OMAi WNSQFGK.
OrthoDBi EOG7DZ8J3.
PhylomeDBi Q7Z5K2.
TreeFami TF323477.

Enzyme and pathway databases

Reactomei REACT_150266. Establishment of Sister Chromatid Cohesion.
REACT_150421. Cohesin Loading onto Chromatin.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.

Miscellaneous databases

ChiTaRSi WAPAL. human.
GeneWikii WAPAL.
GenomeRNAii 23063.
NextBioi 44141.
PROi Q7Z5K2.
SOURCEi Search...

Gene expression databases

Bgeei Q7Z5K2.
CleanExi HS_WAPAL.
ExpressionAtlasi Q7Z5K2. baseline and differential.
Genevestigatori Q7Z5K2.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR012502. WAPL_metazoan_plants.
IPR022771. WAPL_prot.
[Graphical view ]
Pfami PF07814. WAPL. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 2 hits.
PROSITEi PS51271. WAPL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. "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].
  13. "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.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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.
  16. "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.
  17. "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].
  18. Cited for: FUNCTION, INTERACTION WITH PDS5A.
  19. "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.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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].
  22. 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.

Entry informationi

Entry nameiWAPL_HUMAN
AccessioniPrimary (citable) accession number: Q7Z5K2
Secondary accession number(s): A7E2B5
, Q5VSK5, Q8IX10, Q92549
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: October 1, 2003
Last modified: November 26, 2014
This is version 94 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 10
    Human chromosome 10: 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

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