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Protein

Ankyrin repeat and LEM domain-containing protein 2

Gene

ANKLE2

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

Functioni

Involved in mitotic nuclear envelope reassembly by promoting dephosphorylation of BAF/BANF1 during mitotic exit. Coordinates the control of BAF/BANF1 dephosphorylation by inhibiting VRK1 kinase and promoting dephosphorylation of BAF/BANF1 by protein phosphatase 2A (PP2A), thereby facilitating nuclear envelope assembly. It is unclear whether it acts as a real PP2A regulatory subunit or whether it is involved in recruitment of the PP2A complex.1 Publication

GO - Molecular functioni

  • protein phosphatase 2A binding Source: UniProtKB
  • protein phosphatase type 2A regulator activity Source: UniProtKB

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • mitotic cell cycle Source: Reactome
  • mitotic nuclear division Source: UniProtKB-KW
  • mitotic nuclear envelope reassembly Source: UniProtKB
  • negative regulation of phosphorylation Source: UniProtKB
  • positive regulation of protein dephosphorylation Source: UniProtKB
  • regulation of catalytic activity Source: UniProtKB
  • regulation of protein phosphatase type 2A activity Source: GOC
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_160242. Initiation of Nuclear Envelope Reformation.

Names & Taxonomyi

Protein namesi
Recommended name:
Ankyrin repeat and LEM domain-containing protein 2
Alternative name(s):
LEM domain-containing protein 4
Gene namesi
Name:ANKLE2
Synonyms:KIAA0692, LEM4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:29101. ANKLE2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212LumenalSequence AnalysisAdd
BLAST
Transmembranei13 – 3220Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
BLAST
Topological domaini33 – 938906CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: Reactome
  • integral component of endoplasmic reticulum membrane Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162376532.

Polymorphism and mutation databases

BioMutaiANKLE2.
DMDMi269849748.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 938938Ankyrin repeat and LEM domain-containing protein 2PRO_0000280242Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei259 – 2591Phosphoserine1 Publication
Modified residuei268 – 2681Phosphoserine1 Publication
Modified residuei488 – 4881Phosphoserine1 Publication
Modified residuei496 – 4961Phosphoserine2 Publications
Modified residuei512 – 5121Phosphoserine1 Publication
Modified residuei528 – 5281Phosphoserine1 Publication
Modified residuei662 – 6621Phosphoserine3 Publications
Modified residuei896 – 8961Phosphoserine1 Publication
Modified residuei914 – 9141Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ86XL3.
PaxDbiQ86XL3.
PRIDEiQ86XL3.

PTM databases

PhosphoSiteiQ86XL3.

Expressioni

Gene expression databases

BgeeiQ86XL3.
CleanExiHS_ANKLE2.
ExpressionAtlasiQ86XL3. baseline and differential.
GenevestigatoriQ86XL3.

Organism-specific databases

HPAiHPA003602.

Interactioni

Subunit structurei

Interacts with BAF/BANF1. Interacts with protein phosphatase 2A (PP2A) components PPP2C (PPP2CA or PPP2CB) and PPP2R1A.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
vrk-1Q198482EBI-1773621,EBI-2414048From a different organism.

Protein-protein interaction databases

BioGridi116758. 16 interactions.
IntActiQ86XL3. 8 interactions.
MINTiMINT-1187128.
STRINGi9606.ENSP00000350686.

Structurei

3D structure databases

ProteinModelPortaliQ86XL3.
SMRiQ86XL3. Positions 399-453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini69 – 11345LEMPROSITE-ProRule annotationAdd
BLAST
Repeati411 – 44030ANKAdd
BLAST

Sequence similaritiesi

Belongs to the ANKLE2 family.Curated
Contains 1 ANK repeat.Curated
Contains 1 LEM domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG83459.
GeneTreeiENSGT00390000016767.
HOGENOMiHOG000234326.
HOVERGENiHBG096073.
InParanoidiQ86XL3.
OMAiKAGFFHN.
OrthoDBiEOG7RBZ81.
PhylomeDBiQ86XL3.
TreeFamiTF317729.

Family and domain databases

Gene3Di1.10.720.40. 1 hit.
1.25.40.20. 1 hit.
3.40.970.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
IPR011320. RNase_H1_N.
[Graphical view]
PfamiPF13606. Ank_3. 1 hit.
PF03020. LEM. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 2 hits.
SSF63451. SSF63451. 1 hit.
PROSITEiPS50954. LEM. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86XL3-1) [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
MLWPRLAAAE WAALAWELLG ASVLLIAVRW LVRRLGPRPG GLGRSGTPVP
60 70 80 90 100
PPSAAAAPAS GEMTMDALLA RLKLLNPDDL REEIVKAGLK CGPITSTTRF
110 120 130 140 150
IFEKKLAQAL LEQGGRLSSF YHHEAGVTAL SQDPQRILKP AEGNPTDQAG
160 170 180 190 200
FSEDRDFGYS VGLNPPEEEA VTSKTCSVPP SDTDTYRAGA TASKEPPLYY
210 220 230 240 250
GVCPVYEDVP ARNERIYVYE NKKEALQAVK MIKGSRFKAF STREDAEKFA
260 270 280 290 300
RGICDYFPSP SKTSLPLSPV KTAPLFSNDR LKDGLCLSES ETVNKERANS
310 320 330 340 350
YKNPRTQDLT AKLRKAVEKG EEDTFSDLIW SNPRYLIGSG DNPTIVQEGC
360 370 380 390 400
RYNVMHVAAK ENQASICQLT LDVLENPDFM RLMYPDDDEA MLQKRIRYVV
410 420 430 440 450
DLYLNTPDKM GYDTPLHFAC KFGNADVVNV LSSHHLIVKN SRNKYDKTPE
460 470 480 490 500
DVICERSKNK SVELKERIRE YLKGHYYVPL LRAEETSSPV IGELWSPDQT
510 520 530 540 550
AEASHVSRYG GSPRDPVLTL RAFAGPLSPA KAEDFRKLWK TPPREKAGFL
560 570 580 590 600
HHVKKSDPER GFERVGRELA HELGYPWVEY WEFLGCFVDL SSQEGLQRLE
610 620 630 640 650
EYLTQQEIGK KAQQETGERE ASCRDKATTS GSNSISVRAF LDEDDMSLEE
660 670 680 690 700
IKNRQNAARN NSPPTVGAFG HTRCSAFPLE QEADLIEAAE PGGPHSSRNG
710 720 730 740 750
LCHPLNHSRT LAGKRPKAPR GEEAHLPPVS DLTVEFDKLN LQNIGRSVSK
760 770 780 790 800
TPDESTKTKD QILTSRINAV ERDLLEPSPA DQLGNGHRRT ESEMSARIAK
810 820 830 840 850
MSLSPSSPRH EDQLEVTREP ARRLFLFGEE PSKLDQDVLA ALECADVDPH
860 870 880 890 900
QFPAVHRWKS AVLCYSPSDR QSWPSPAVKG RFKSQLPDLS GPHSYSPGRN
910 920 930
SVAGSNPAKP GLGSPGRYSP VHGSQLRRMA RLAELAAL
Length:938
Mass (Da):104,114
Last modified:November 24, 2009 - v4
Checksum:iED2F25F05E8106F2
GO
Isoform 2 (identifier: Q86XL3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     631-648: GSNSISVRAFLDEDDMSL → VEMRFHRIDQAGLELLTS
     649-938: Missing.

Note: No experimental confirmation available.

Show »
Length:648
Mass (Da):72,641
Checksum:iA98712EBEE04E982
GO
Isoform 3 (identifier: Q86XL3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-645: Missing.

Show »
Length:293
Mass (Da):31,982
Checksum:i018D51B5FEA0E877
GO

Sequence cautioni

The sequence BAG51259.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti266 – 2661P → Q in AAH43157 (PubMed:15489334).Curated
Sequence conflicti481 – 4811L → V in AAH43157 (PubMed:15489334).Curated
Sequence conflicti647 – 6471S → N in AAH43157 (PubMed:15489334).Curated
Sequence conflicti662 – 6621S → I in BAG52720 (PubMed:14702039).Curated
Sequence conflicti680 – 6801E → K in BAG52720 (PubMed:14702039).Curated
Sequence conflicti863 – 8631L → P in BAG51259 (PubMed:14702039).Curated
Sequence conflicti891 – 8911G → A in BAG52720 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti122 – 1221H → Y.1 Publication
Corresponds to variant rs1132375 [ dbSNP | Ensembl ].
VAR_031097
Natural varianti148 – 1481Q → E.
Corresponds to variant rs7968520 [ dbSNP | Ensembl ].
VAR_031098
Natural varianti720 – 7201R → H.2 Publications
Corresponds to variant rs10781634 [ dbSNP | Ensembl ].
VAR_031099

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 645645Missing in isoform 3. 1 PublicationVSP_044173Add
BLAST
Alternative sequencei631 – 64818GSNSI…DDMSL → VEMRFHRIDQAGLELLTS in isoform 2. 1 PublicationVSP_023574Add
BLAST
Alternative sequencei649 – 938290Missing in isoform 2. 1 PublicationVSP_023575Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK024061 mRNA. Translation: BAG51259.1. Different initiation.
AK093451 mRNA. Translation: BAG52720.1.
AK293028 mRNA. Translation: BAF85717.1.
AC135586 Genomic DNA. No translation available.
AC136467 Genomic DNA. No translation available.
BC001530 mRNA. Translation: AAH01530.2.
BC025347 mRNA. Translation: AAH25347.1.
BC043157 mRNA. Translation: AAH43157.2.
BC062373 mRNA. Translation: AAH62373.1.
BC082962 mRNA. Translation: AAH82962.1.
AB014592 mRNA. Translation: BAA31667.1.
CCDSiCCDS41869.1. [Q86XL3-1]
PIRiT00354.
RefSeqiNP_055929.1. NM_015114.2. [Q86XL3-1]
UniGeneiHs.654628.

Genome annotation databases

EnsembliENST00000357997; ENSP00000350686; ENSG00000176915. [Q86XL3-1]
ENST00000542282; ENSP00000437807; ENSG00000176915. [Q86XL3-3]
ENST00000542657; ENSP00000438551; ENSG00000176915. [Q86XL3-3]
GeneIDi23141.
KEGGihsa:23141.
UCSCiuc001ukx.2. human. [Q86XL3-1]
uc001uky.3. human. [Q86XL3-2]
uc009zyw.1. human. [Q86XL3-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK024061 mRNA. Translation: BAG51259.1. Different initiation.
AK093451 mRNA. Translation: BAG52720.1.
AK293028 mRNA. Translation: BAF85717.1.
AC135586 Genomic DNA. No translation available.
AC136467 Genomic DNA. No translation available.
BC001530 mRNA. Translation: AAH01530.2.
BC025347 mRNA. Translation: AAH25347.1.
BC043157 mRNA. Translation: AAH43157.2.
BC062373 mRNA. Translation: AAH62373.1.
BC082962 mRNA. Translation: AAH82962.1.
AB014592 mRNA. Translation: BAA31667.1.
CCDSiCCDS41869.1. [Q86XL3-1]
PIRiT00354.
RefSeqiNP_055929.1. NM_015114.2. [Q86XL3-1]
UniGeneiHs.654628.

3D structure databases

ProteinModelPortaliQ86XL3.
SMRiQ86XL3. Positions 399-453.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116758. 16 interactions.
IntActiQ86XL3. 8 interactions.
MINTiMINT-1187128.
STRINGi9606.ENSP00000350686.

PTM databases

PhosphoSiteiQ86XL3.

Polymorphism and mutation databases

BioMutaiANKLE2.
DMDMi269849748.

Proteomic databases

MaxQBiQ86XL3.
PaxDbiQ86XL3.
PRIDEiQ86XL3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357997; ENSP00000350686; ENSG00000176915. [Q86XL3-1]
ENST00000542282; ENSP00000437807; ENSG00000176915. [Q86XL3-3]
ENST00000542657; ENSP00000438551; ENSG00000176915. [Q86XL3-3]
GeneIDi23141.
KEGGihsa:23141.
UCSCiuc001ukx.2. human. [Q86XL3-1]
uc001uky.3. human. [Q86XL3-2]
uc009zyw.1. human. [Q86XL3-3]

Organism-specific databases

CTDi23141.
GeneCardsiGC12M133302.
H-InvDBHIX0020726.
HGNCiHGNC:29101. ANKLE2.
HPAiHPA003602.
MIMi616062. gene.
neXtProtiNX_Q86XL3.
PharmGKBiPA162376532.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG83459.
GeneTreeiENSGT00390000016767.
HOGENOMiHOG000234326.
HOVERGENiHBG096073.
InParanoidiQ86XL3.
OMAiKAGFFHN.
OrthoDBiEOG7RBZ81.
PhylomeDBiQ86XL3.
TreeFamiTF317729.

Enzyme and pathway databases

ReactomeiREACT_160242. Initiation of Nuclear Envelope Reformation.

Miscellaneous databases

ChiTaRSiANKLE2. human.
GenomeRNAii23141.
NextBioi44418.
PROiQ86XL3.
SOURCEiSearch...

Gene expression databases

BgeeiQ86XL3.
CleanExiHS_ANKLE2.
ExpressionAtlasiQ86XL3. baseline and differential.
GenevestigatoriQ86XL3.

Family and domain databases

Gene3Di1.10.720.40. 1 hit.
1.25.40.20. 1 hit.
3.40.970.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
IPR011320. RNase_H1_N.
[Graphical view]
PfamiPF13606. Ank_3. 1 hit.
PF03020. LEM. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 2 hits.
SSF63451. SSF63451. 1 hit.
PROSITEiPS50954. LEM. 1 hit.
[Graphical view]
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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 409-938 (ISOFORM 1).
    Tissue: Testis and Uterus.
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 208-938 (ISOFORM 2), VARIANTS TYR-122 AND HIS-720.
    Tissue: Brain and Skin.
  4. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 156-938 (ISOFORM 1), VARIANT HIS-720.
    Tissue: Brain.
  5. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259; SER-268; SER-488; SER-496; SER-512; SER-662; SER-896 AND SER-914, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "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-496 AND SER-662, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-662, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Coordination of kinase and phosphatase activities by Lem4 enables nuclear envelope reassembly during mitosis."
    Asencio C., Davidson I.F., Santarella-Mellwig R., Ly-Hartig T.B., Mall M., Wallenfang M.R., Mattaj I.W., Gorjanacz M.
    Cell 150:122-135(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH BANF1 AND PROTEIN PHOSPHATASE 2A.
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiANKL2_HUMAN
AccessioniPrimary (citable) accession number: Q86XL3
Secondary accession number(s): A8KAG3
, B3KN97, B3KSF8, O75176, Q6P6A5, Q8TAZ9, Q96DH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: November 24, 2009
Last modified: May 27, 2015
This is version 108 of the entry and version 4 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 12
    Human chromosome 12: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.