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Protein

E3 ubiquitin-protein ligase Hakai

Gene

Cbll1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Promotes ubiquitination of several tyrosine-phosphorylated Src substrates, including CDH1, CTTN and DOK1. Targets CDH1 for endocytosis and degradation.2 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri109 – 14941RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri164 – 19027C2H2-typeAdd
BLAST

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • ligase activity Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

  • negative regulation of cell adhesion Source: MGI
  • positive regulation of cell migration Source: MGI
  • positive regulation of endocytosis Source: MGI
  • single organismal cell-cell adhesion Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase Hakai (EC:6.3.2.-)
Alternative name(s):
Casitas B-lineage lymphoma-transforming sequence-like protein 1
E-cadherin binding protein E7
c-Cbl-like protein 1
Gene namesi
Name:Cbll1
Synonyms:Hakai
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:2144842. Cbll1.

Subcellular locationi

  • Nucleus speckle By similarity
  • Nucleusnucleoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491E3 ubiquitin-protein ligase HakaiPRO_0000284050Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei201 – 2011PhosphoserineBy similarity
Modified residuei290 – 2901PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on tyrosine residues.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9JIY2.
MaxQBiQ9JIY2.
PaxDbiQ9JIY2.
PRIDEiQ9JIY2.

PTM databases

iPTMnetiQ9JIY2.
PhosphoSiteiQ9JIY2.

Expressioni

Tissue specificityi

Detected in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis.1 Publication

Gene expression databases

BgeeiQ9JIY2.
CleanExiMM_CBLL1.
ExpressionAtlasiQ9JIY2. baseline and differential.
GenevisibleiQ9JIY2. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with tyrosine-phosphorylated SRC substrates. Component of the WTAP complex composed of WTAP, ZC3H13, CBLL1, KIAA1429, RBM15, BCLAF1 and THRAP3 (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-7644904,EBI-7644904
CDH1P1283021EBI-7644904,EBI-727477From a different organism.
CTTNQ142478EBI-7644904,EBI-351886From a different organism.
CttnQ605984EBI-7644904,EBI-397955
DOK1Q997042EBI-7644904,EBI-1384360From a different organism.

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi222714. 1 interaction.
IntActiQ9JIY2. 26 interactions.
MINTiMINT-4129836.
STRINGi10090.ENSMUSP00000099038.

Structurei

Secondary structure

1
491
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni110 – 1123Combined sources
Beta strandi117 – 1237Combined sources
Turni124 – 1263Combined sources
Beta strandi128 – 1303Combined sources
Helixi131 – 1399Combined sources
Turni146 – 1483Combined sources
Beta strandi153 – 1597Combined sources
Helixi160 – 1623Combined sources
Helixi179 – 18911Combined sources
Turni190 – 1923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MQ1NMR-A106-194[»]
3VK6X-ray1.90A106-206[»]
ProteinModelPortaliQ9JIY2.
SMRiQ9JIY2. Positions 106-201.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni148 – 20659HYB domainAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi207 – 481275Pro-richAdd
BLAST

Domaini

The HYB domain forms a phosphotyrosine-binding pocket upon dimerization, and mediates as well the recognition of its flanking acidic amino acids.1 Publication

Sequence similaritiesi

Contains 1 C2H2-type zinc finger.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri109 – 14941RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri164 – 19027C2H2-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2932. Eukaryota.
ENOG410XQ6S. LUCA.
GeneTreeiENSGT00510000047522.
HOGENOMiHOG000082498.
HOVERGENiHBG057723.
InParanoidiQ9JIY2.
KOiK15685.
OMAiGTPHMVY.
OrthoDBiEOG7GN2NX.
PhylomeDBiQ9JIY2.
TreeFamiTF332910.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9JIY2-1) [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
MDHTDNELQG TNSSGSLGGL DVRRRIPIKL ISKQASKVKP APRTQRTVSR
60 70 80 90 100
MPAKAPQGDE EGFDYNEEQR YDCKGGELFG NQRRFPGHLF WDFKINILGE
110 120 130 140 150
KDDTPVHFCD KCGLPIKVYG RMIPCKHVFC YDCAILHEKK GDKMCPGCSD
160 170 180 190 200
PVQRIEQCTR GSLFMCSIVQ GCKRTYLSQR DLQAHINHRH MRAGKPVTRA
210 220 230 240 250
SLENVHPPIA PPPTDIPDRF IMPPDKHHMS HIPPKQHIMM PPPPLQHVPH
260 270 280 290 300
EHYNQPHEDI RAPPAELSMA PPPPRSVSQE TFRISTRKHS NLITVPIQDD
310 320 330 340 350
SSSGAREPPP PAPAPAHHHP EYQGQPVVSH PHHIMPPQQH YAPPPPPPPP
360 370 380 390 400
ISHPMPHPPQ AAGTPHLVYS QAPPPPMTSA PPPITPPPGH IIAQMPPYMN
410 420 430 440 450
HPPPGPPPPQ HGGPPVTAPP PHHYNPNSLP QFTEDQGTLS PPFTQPGGMS
460 470 480 490
PGIWPAPRGP PPPPRMQGPP SQTPLPGPHH PDQTRYRPYY Q
Length:491
Mass (Da):54,444
Last modified:October 1, 2000 - v1
Checksum:iAD2A3C188781A7DA
GO
Isoform 2 (identifier: Q9JIY2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-61: Missing.

Show »
Length:490
Mass (Da):54,315
Checksum:i633E8854196D4E83
GO
Isoform 3 (identifier: Q9JIY2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-61: Missing.
     311-374: Missing.
     398-409: Missing.

Show »
Length:414
Mass (Da):46,167
Checksum:iF463812DF2ECAA35
GO
Isoform 4 (identifier: Q9JIY2-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     58-61: Missing.
     277-431: Missing.

Show »
Length:332
Mass (Da):37,481
Checksum:i47F62DF8D15B006C
GO

Sequence cautioni

The sequence BAE38522.1 differs from that shown. Reason: Frameshift at position 470. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei58 – 614Missing in isoform 4. 1 PublicationVSP_024415
Alternative sequencei61 – 611Missing in isoform 2 and isoform 3. 2 PublicationsVSP_024416
Alternative sequencei277 – 431155Missing in isoform 4. 1 PublicationVSP_024417Add
BLAST
Alternative sequencei311 – 37464Missing in isoform 3. 1 PublicationVSP_024418Add
BLAST
Alternative sequencei398 – 40912Missing in isoform 3. 1 PublicationVSP_024419Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF167441 mRNA. Translation: AAF89617.1.
AK049141 mRNA. Translation: BAC33568.1.
AK166017 mRNA. Translation: BAE38522.1. Frameshift.
BC019529 mRNA. Translation: AAH19529.1.
CCDSiCCDS56834.1. [Q9JIY2-1]
CCDS56835.1. [Q9JIY2-4]
RefSeqiNP_001240776.1. NM_001253847.1. [Q9JIY2-1]
NP_001240777.1. NM_001253848.1. [Q9JIY2-4]
NP_598809.1. NM_134048.2. [Q9JIY2-2]
UniGeneiMm.273270.

Genome annotation databases

EnsembliENSMUST00000064240; ENSMUSP00000063266; ENSMUSG00000020659. [Q9JIY2-4]
ENSMUST00000101499; ENSMUSP00000099038; ENSMUSG00000020659. [Q9JIY2-1]
GeneIDi104836.
KEGGimmu:104836.
UCSCiuc007nhl.2. mouse. [Q9JIY2-2]
uc007nhm.2. mouse. [Q9JIY2-1]
uc007nhn.2. mouse. [Q9JIY2-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF167441 mRNA. Translation: AAF89617.1.
AK049141 mRNA. Translation: BAC33568.1.
AK166017 mRNA. Translation: BAE38522.1. Frameshift.
BC019529 mRNA. Translation: AAH19529.1.
CCDSiCCDS56834.1. [Q9JIY2-1]
CCDS56835.1. [Q9JIY2-4]
RefSeqiNP_001240776.1. NM_001253847.1. [Q9JIY2-1]
NP_001240777.1. NM_001253848.1. [Q9JIY2-4]
NP_598809.1. NM_134048.2. [Q9JIY2-2]
UniGeneiMm.273270.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MQ1NMR-A106-194[»]
3VK6X-ray1.90A106-206[»]
ProteinModelPortaliQ9JIY2.
SMRiQ9JIY2. Positions 106-201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi222714. 1 interaction.
IntActiQ9JIY2. 26 interactions.
MINTiMINT-4129836.
STRINGi10090.ENSMUSP00000099038.

PTM databases

iPTMnetiQ9JIY2.
PhosphoSiteiQ9JIY2.

Proteomic databases

EPDiQ9JIY2.
MaxQBiQ9JIY2.
PaxDbiQ9JIY2.
PRIDEiQ9JIY2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000064240; ENSMUSP00000063266; ENSMUSG00000020659. [Q9JIY2-4]
ENSMUST00000101499; ENSMUSP00000099038; ENSMUSG00000020659. [Q9JIY2-1]
GeneIDi104836.
KEGGimmu:104836.
UCSCiuc007nhl.2. mouse. [Q9JIY2-2]
uc007nhm.2. mouse. [Q9JIY2-1]
uc007nhn.2. mouse. [Q9JIY2-4]

Organism-specific databases

CTDi79872.
MGIiMGI:2144842. Cbll1.

Phylogenomic databases

eggNOGiKOG2932. Eukaryota.
ENOG410XQ6S. LUCA.
GeneTreeiENSGT00510000047522.
HOGENOMiHOG000082498.
HOVERGENiHBG057723.
InParanoidiQ9JIY2.
KOiK15685.
OMAiGTPHMVY.
OrthoDBiEOG7GN2NX.
PhylomeDBiQ9JIY2.
TreeFamiTF332910.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiCbll1. mouse.
NextBioi357318.
PROiQ9JIY2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JIY2.
CleanExiMM_CBLL1.
ExpressionAtlasiQ9JIY2. baseline and differential.
GenevisibleiQ9JIY2. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex."
    Fujita Y., Krause G., Scheffner M., Zechner D., Molina Leddy H.E., Behrens J., Sommer T., Birchmeier W.
    Nat. Cell Biol. 4:222-231(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CDH1, PHOSPHORYLATION, TISSUE SPECIFICITY.
    Tissue: Embryo.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Embryonic stem cell and Lung.
  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 2).
    Strain: FVB/N.
    Tissue: Colon.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 106-206, FUNCTION, DOMAIN HYB, SUBUNIT.

Entry informationi

Entry nameiHAKAI_MOUSE
AccessioniPrimary (citable) accession number: Q9JIY2
Secondary accession number(s): Q3TMC0, Q8C7W5, Q8VCL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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