Q7Z5K2 (WAPL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Wings apart-like protein homolog

Alternative name(s):
Friend of EBNA2 protein

Gene names

Name:	WAPAL
Synonyms:	FOE, KIAA0261, WAPL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1190 AA.
Sequence status	Complete.
Protein existence	Evidence 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.13 Ref.15 Ref.18
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 SORORIN. Interacts (via FGF motifs) with PDS5B; the interaction is direct. Interacts with SMC3. Isoform 2 interacts with Epstein-Barr virus EBNA2. Ref.2 Ref.8 Ref.9 Ref.13 Ref.15 Ref.18
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 process	Cell cycle Cell division Host-virus interaction Mitosis
Cellular component	Chromosome Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of DNA replication Inferred from mutant phenotype Ref.15. Source: UniProtKB negative regulation of chromatin binding Inferred from mutant phenotype Ref.8Ref.13. Source: UniProtKB negative regulation of sister chromatid cohesion Inferred from mutant phenotype Ref.8Ref.13Ref.18. Source: UniProtKB protein localization to chromatin Inferred from mutant phenotype Ref.18. Source: UniProtKB regulation of cohesin localization to chromatin Inferred from mutant phenotype Ref.8. Source: UniProtKB response to toxin Inferred from electronic annotation. Source: Compara virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chromatin Inferred from direct assay Ref.8Ref.13. Source: UniProtKB cohesin complex Inferred from direct assay Ref.8Ref.13. Source: UniProtKB cytoplasm Inferred from direct assay Ref.8Ref.13. Source: UniProtKB microtubule cytoskeleton Inferred from direct assay. Source: HPA nucleus Inferred from direct assay Ref.8Ref.13. Source: UniProtKB synaptonemal complex Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PDS5B	Q9NTI5	9	EBI-1022242,EBI-1175604
RAD21	O60216	11	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1190	1190	Wings apart-like protein homolog		PRO_0000245232
Regions
	Domain	626 – 1169	544	WAPL
	Region	1 – 659	659	Mediates interaction with the cohesin complex
	Coiled coil	260 – 286	27	Potential
	Coiled coil	749 – 782	34	Potential
	Motif	73 – 75	3	FGF motif 1
	Motif	429 – 431	3	FGF motif 2
	Motif	453 – 455	3	FGF motif 3
Amino acid modifications
	Modified residue	77	1	Phosphoserine Ref.10 Ref.11 Ref.14 Ref.16 Ref.19 Ref.21
	Modified residue	168	1	N6-acetyllysine Ref.17
	Modified residue	221	1	Phosphoserine Ref.11 Ref.19 Ref.21
	Modified residue	223	1	Phosphoserine Ref.11 Ref.12
	Modified residue	226	1	Phosphoserine Ref.7 Ref.10 Ref.11 Ref.19 Ref.21
	Modified residue	380	1	Phosphoserine Ref.11 Ref.16
	Modified residue	459	1	Phosphoserine Ref.11
	Modified residue	461	1	Phosphoserine Ref.11
	Modified residue	904	1	Phosphoserine Ref.11
Natural variations
	Alternative sequence	1	1	M → MVQGPVQTPALTIHRRKRRR RRRRRPVAKAPARLRGEYET GVKM in isoform 2.		VSP_019649
	Alternative sequence	1	1	M → MVQGPVQTPALTIHRRKRRR SCPPNRASYLPKAESLASLG SHLPALLSRARVPRPPAGRR ERERRRRPVAKAPARLRGEY ETGVKM in isoform 3.		VSP_019650
	Alternative sequence	510 – 515	6	Missing in isoform 2.		VSP_019651
	Natural variant	124	1	V → I. Corresponds to variant rs10887621 [ dbSNP | Ensembl ].		VAR_026967
Experimental info
	Mutagenesis	73 – 75	3	FGF → EGE: Loss of interaction with PDS5B; when associated with 429-E--E-431 and 453-E--E-455.
	Mutagenesis	429 – 431	3	FGF → EGE: Loss of interaction with PDS5B; when associated with 73-E--E-75 and 453-E--E-455. Ref.13
	Mutagenesis	453 – 455	3	FGF → EGE: Loss of interaction with PDS5B; when associated with 73-E--E-75 and 429-E--E-431. Ref.13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: A01026E520BFAB2F	FASTA	1,190	132,946
	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
	Isoform 2 [UniParc]. Checksum: 5431910072375C05	FASTA	1,227	137,314
	10 20 30 40 50 60 MVQGPVQTPA LTIHRRKRRR RRRRRPVAKA PARLRGEYET GVKMTSRFGK TYSRKGGNGS 70 80 90 100 110 120 SKFDEVFSNK RTTLSTKWGE TTFMAKLGQK RPNFKPDIQE IPKKPKVEEE STGDPFGFDS 130 140 150 160 170 180 DDESLPVSSK NLAQVKCSSY SESSEAAQLE EVTSVLEANS KISHVVVEDT VVSDKCFPLE 190 200 210 220 230 240 DTLLGKEKST NRIVEDDASI SSCNKLITSD KVENFHEEHE KNSHHIHKNA DDSTKKPNAE 250 260 270 280 290 300 TTVASEIKET NDTWNSQFGK RPESPSEISP IKGSVRTGLF EWDNDFEDIR SEDCILSLDS 310 320 330 340 350 360 DPLLEMKDDD FKNRLENLNE AIEEDIVQSV LRPTNCRTYC RANKTKSSQG ASNFDKLMDG 370 380 390 400 410 420 TSQALAKANS ESSKDGLNQA KKGGVSCGTS FRGTVGRTRD YTVLHPSCLS VCNVTIQDTM 430 440 450 460 470 480 ERSMDEFTAS TPADLGEAGR LRKKADIATS KTTTRFRPSN TKSKKDVKLE FFGFEDHETG 490 500 510 520 530 540 GDEGGSGSSN YKIKYFGFDD LSESEDDEDD DCQVERKTSK KRTKTAPSPS LQPPPESNDN 550 560 570 580 590 600 SQDSQSGTNN AEDLPGVPES VKKPINKQGD KSKENTRKIF SGPKRSPTKA VYNARHWNHP 610 620 630 640 650 660 DSEELPGPPV VKPQSVTVRL SSKEPNQKDD GVFKAPAPPS KVIKTVTIPT QPYQDIVTAL 670 680 690 700 710 720 KCRREDKELY TVVQHVKHFN DVVEFGENQE FTDDIEYLLS GLKSTQPLNT RCLSVISLAT 730 740 750 760 770 780 KCAMPSFRMH LRAHGMVAMV FKTLDDSQHH QNLSLCTAAL MYILSRDRLN MDLDRASLDL 790 800 810 820 830 840 MIRLLELEQD ASSAKLLNEK DMNKIKEKIR RLCETVHNKH LDLENITTGH LAMETLLSLT 850 860 870 880 890 900 SKRAGDWFKE ELRLLGGLDH IVDKVKECVD HLSRDEDEEK LVASLWGAER CLRVLESVTV 910 920 930 940 950 960 HNPENQSYLI AYKDSQLIVS SAKALQHCEE LIQQYNRAED SICLADSKPL PHQNVTNHVG 970 980 990 1000 1010 1020 KAVEDCMRAI IGVLLNLTND NEWGSTKTGE QDGLIGTALN CVLQVPKYLP QEQRFDIRVL 1030 1040 1050 1060 1070 1080 GLGLLINLVE YSARNRHCLV NMETSCSFDS SICSGEGDDS LRIGGQVHAV QALVQLFLER 1090 1100 1110 1120 1130 1140 ERAAQLAESK TDELIKDAPT TQHDKSGEWQ ETSGEIQWVS TEKTDGTEEK HKKEEEDEEL 1150 1160 1170 1180 1190 1200 DLNKALQHAG KHMEDCIVAS YTALLLGCLC QESPINVTTV REYLPEGDFS IMTEMLKKFL 1210 1220 SFMNLTCAVG TTGQKSISRV IEYLEHC
	Isoform 3 [UniParc]. Checksum: 5588D17DBB5C782F	FASTA	1,275	142,525
	10 20 30 40 50 60 MVQGPVQTPA LTIHRRKRRR SCPPNRASYL PKAESLASLG SHLPALLSRA RVPRPPAGRR 70 80 90 100 110 120 ERERRRRPVA KAPARLRGEY ETGVKMTSRF GKTYSRKGGN GSSKFDEVFS NKRTTLSTKW 130 140 150 160 170 180 GETTFMAKLG QKRPNFKPDI QEIPKKPKVE EESTGDPFGF DSDDESLPVS SKNLAQVKCS 190 200 210 220 230 240 SYSESSEAAQ LEEVTSVLEA NSKISHVVVE DTVVSDKCFP LEDTLLGKEK STNRIVEDDA 250 260 270 280 290 300 SISSCNKLIT SDKVENFHEE HEKNSHHIHK NADDSTKKPN AETTVASEIK ETNDTWNSQF 310 320 330 340 350 360 GKRPESPSEI SPIKGSVRTG LFEWDNDFED IRSEDCILSL DSDPLLEMKD DDFKNRLENL 370 380 390 400 410 420 NEAIEEDIVQ SVLRPTNCRT YCRANKTKSS QGASNFDKLM DGTSQALAKA NSESSKDGLN 430 440 450 460 470 480 QAKKGGVSCG TSFRGTVGRT RDYTVLHPSC LSVCNVTIQD TMERSMDEFT ASTPADLGEA 490 500 510 520 530 540 GRLRKKADIA TSKTTTRFRP SNTKSKKDVK LEFFGFEDHE TGGDEGGSGS SNYKIKYFGF 550 560 570 580 590 600 DDLSESEDDE DDDCQVERKT SKKRTKTAPS PSLQPPPESN DNSQDSQSGT NNAENLDFTE 610 620 630 640 650 660 DLPGVPESVK KPINKQGDKS KENTRKIFSG PKRSPTKAVY NARHWNHPDS EELPGPPVVK 670 680 690 700 710 720 PQSVTVRLSS KEPNQKDDGV FKAPAPPSKV IKTVTIPTQP YQDIVTALKC RREDKELYTV 730 740 750 760 770 780 VQHVKHFNDV VEFGENQEFT DDIEYLLSGL KSTQPLNTRC LSVISLATKC AMPSFRMHLR 790 800 810 820 830 840 AHGMVAMVFK TLDDSQHHQN LSLCTAALMY ILSRDRLNMD LDRASLDLMI RLLELEQDAS 850 860 870 880 890 900 SAKLLNEKDM NKIKEKIRRL CETVHNKHLD LENITTGHLA METLLSLTSK RAGDWFKEEL 910 920 930 940 950 960 RLLGGLDHIV DKVKECVDHL SRDEDEEKLV ASLWGAERCL RVLESVTVHN PENQSYLIAY 970 980 990 1000 1010 1020 KDSQLIVSSA KALQHCEELI QQYNRAEDSI CLADSKPLPH QNVTNHVGKA VEDCMRAIIG 1030 1040 1050 1060 1070 1080 VLLNLTNDNE WGSTKTGEQD GLIGTALNCV LQVPKYLPQE QRFDIRVLGL GLLINLVEYS 1090 1100 1110 1120 1130 1140 ARNRHCLVNM ETSCSFDSSI CSGEGDDSLR IGGQVHAVQA LVQLFLERER AAQLAESKTD 1150 1160 1170 1180 1190 1200 ELIKDAPTTQ HDKSGEWQET SGEIQWVSTE KTDGTEEKHK KEEEDEELDL NKALQHAGKH 1210 1220 1230 1240 1250 1260 MEDCIVASYT ALLLGCLCQE SPINVTTVRE YLPEGDFSIM TEMLKKFLSF MNLTCAVGTT 1270 GQKSISRVIE YLEHC

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	Carrascal M., Abian J. Submitted (JAN-2008) to UniProtKB Cited for: PHOSPHORYLATION AT SER-223, MASS SPECTROMETRY. Tissue: T-cell.
[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]	"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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[18]	"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.
[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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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].
[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, MASS SPECTROMETRY.
+	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.
IPI	IPI00375330. IPI00412441. IPI00744918.
RefSeq	NP_055860.1. NM_015045.2.
UniGene	Hs.203099. Hs.714876.
3D structure databases
ProteinModelPortal	Q7Z5K2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q7Z5K2. 13 interactions.
STRING	9606.ENSP00000298767.
PTM databases
PhosphoSite	Q7Z5K2.
Polymorphism databases
DMDM	74713658.
Proteomic databases
PaxDb	Q7Z5K2.
PRIDE	Q7Z5K2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000298767; ENSP00000298767; ENSG00000062650. ENST00000342368; ENSP00000345162; ENSG00000062650.
GeneID	23063.
KEGG	hsa:23063.
UCSC	uc001kdn.3. human. uc001kdo.3. human.
Organism-specific databases
CTD	23063.
GeneCards	GC10M088185.
HGNC	HGNC:23293. WAPAL.
HPA	HPA037874. HPA037875.
MIM	610754. gene.
neXtProt	NX_Q7Z5K2.
PharmGKB	PA134872402.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG297597.
HOGENOM	HOG000001563.
HOVERGEN	HBG088338.
InParanoid	Q7Z5K2.
OMA	NARHWNQ.
OrthoDB	EOG4TXBR6.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases.
Gene expression databases
ArrayExpress	Q7Z5K2.
Bgee	Q7Z5K2.
CleanEx	HS_WAPAL.
Genevestigator	Q7Z5K2.
GermOnline	ENSG00000062650. Homo sapiens.
Family and domain databases
InterPro	IPR016024. ARM-type_fold. IPR012502. WAPL_metazoan_plants. IPR022771. WAPL_prot. [Graphical view]
Pfam	PF07814. WAPL. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
PROSITE	PS51271. WAPL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	WAPAL. human.
GenomeRNAi	23063.
NextBio	44141.
SOURCE	Search...

Entry information

Entry name

WAPL_HUMAN

Accession

Primary (citable) accession number: Q7Z5K2
Secondary accession number(s): A7E2B5 , Q5VSK5, Q8IX10, Q92549

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	October 1, 2003
Last modified:	May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.