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Protein

E3 ubiquitin-protein ligase Hakai

Gene

CBLL1

Organism
Homo sapiens (Human)
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 (By similarity).By similarity

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

GO - Biological processi

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
RING finger protein 188
c-Cbl-like protein 1
Gene namesi
Name:CBLL1
Synonyms:HAKAI, RNF188
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:21225. CBLL1.

Subcellular locationi

GO - Cellular componenti

  • nuclear speck Source: UniProtKB-SubCell
  • ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134960329.

Polymorphism and mutation databases

DMDMi74762414.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491E3 ubiquitin-protein ligase HakaiPRO_0000284048Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei201 – 2011PhosphoserineCombined sources
Modified residuei290 – 2901PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ75N03.
MaxQBiQ75N03.
PaxDbiQ75N03.
PRIDEiQ75N03.

PTM databases

iPTMnetiQ75N03.
PhosphoSiteiQ75N03.

Expressioni

Gene expression databases

BgeeiQ75N03.
CleanExiHS_CBLL1.
ExpressionAtlasiQ75N03. baseline and differential.
GenevisibleiQ75N03. HS.

Organism-specific databases

HPAiHPA021773.
HPA026699.

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 (PubMed:24100041).1 Publication

Protein-protein interaction databases

BioGridi122960. 14 interactions.
IntActiQ75N03. 5 interactions.
MINTiMINT-3298121.
STRINGi9606.ENSP00000401277.

Structurei

3D structure databases

ProteinModelPortaliQ75N03.
SMRiQ75N03. Positions 106-201.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni148 – 20659HYB domainBy similarityAdd
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.By similarity

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.
InParanoidiQ75N03.
KOiK15685.
OMAiGTPHMVY.
OrthoDBiEOG7GN2NX.
PhylomeDBiQ75N03.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q75N03-1) [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 ISKQANKAKP APRTQRTINR
60 70 80 90 100
MPAKAPPGDE EGFDYNEEER YDCKGGELFA NQRRFPGHLF WDFQINILGE
110 120 130 140 150
KDDTPVHFCD KCGLPIKIYG RMIPCKHVFC YDCAILHEKK GDKMCPGCSD
160 170 180 190 200
PVQRIEQCTR GSLFMCSIVQ GCKRTYLSQR DLQAHINHRH MRAGKPVTRA
210 220 230 240 250
SLENVHPPIA PPPTEIPERF IMPPDKHHMS HIPPKQHIMM PPPPLQHVPH
260 270 280 290 300
EHYNQPHEDI RAPPAELSMA PPPPRSVSQE TFRISTRKHS NLITVPIQDD
310 320 330 340 350
SNSGAREPPP 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 PPPPRLQGPP SQTPLPGPHH PDQTRYRPYY Q
Length:491
Mass (Da):54,519
Last modified:July 5, 2004 - v1
Checksum:i1A733A8CC28F3AA0
GO
Isoform 2 (identifier: Q75N03-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     60-60: Missing.

Note: No experimental confirmation available.
Show »
Length:490
Mass (Da):54,390
Checksum:i142CD58C5CF50D7E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti439 – 4391L → P in BAB15544 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei60 – 601Missing in isoform 2. 1 PublicationVSP_054879

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK026762 mRNA. Translation: BAB15544.1.
AC002467 Genomic DNA. Translation: AAS07390.1.
BC027460 mRNA. Translation: AAH27460.2.
BC130529 mRNA. Translation: AAI30530.1.
BC130531 mRNA. Translation: AAI30532.1.
BC144176 mRNA. Translation: AAI44177.1.
CCDSiCCDS5747.1. [Q75N03-1]
CCDS64754.1. [Q75N03-2]
RefSeqiNP_001271220.1. NM_001284291.1. [Q75N03-2]
NP_079090.2. NM_024814.3. [Q75N03-1]
UniGeneiHs.592271.

Genome annotation databases

EnsembliENST00000222597; ENSP00000222597; ENSG00000105879. [Q75N03-2]
ENST00000440859; ENSP00000401277; ENSG00000105879. [Q75N03-1]
GeneIDi79872.
KEGGihsa:79872.
UCSCiuc003veq.4. human. [Q75N03-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK026762 mRNA. Translation: BAB15544.1.
AC002467 Genomic DNA. Translation: AAS07390.1.
BC027460 mRNA. Translation: AAH27460.2.
BC130529 mRNA. Translation: AAI30530.1.
BC130531 mRNA. Translation: AAI30532.1.
BC144176 mRNA. Translation: AAI44177.1.
CCDSiCCDS5747.1. [Q75N03-1]
CCDS64754.1. [Q75N03-2]
RefSeqiNP_001271220.1. NM_001284291.1. [Q75N03-2]
NP_079090.2. NM_024814.3. [Q75N03-1]
UniGeneiHs.592271.

3D structure databases

ProteinModelPortaliQ75N03.
SMRiQ75N03. Positions 106-201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122960. 14 interactions.
IntActiQ75N03. 5 interactions.
MINTiMINT-3298121.
STRINGi9606.ENSP00000401277.

PTM databases

iPTMnetiQ75N03.
PhosphoSiteiQ75N03.

Polymorphism and mutation databases

DMDMi74762414.

Proteomic databases

EPDiQ75N03.
MaxQBiQ75N03.
PaxDbiQ75N03.
PRIDEiQ75N03.

Protocols and materials databases

DNASUi79872.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000222597; ENSP00000222597; ENSG00000105879. [Q75N03-2]
ENST00000440859; ENSP00000401277; ENSG00000105879. [Q75N03-1]
GeneIDi79872.
KEGGihsa:79872.
UCSCiuc003veq.4. human. [Q75N03-1]

Organism-specific databases

CTDi79872.
GeneCardsiCBLL1.
HGNCiHGNC:21225. CBLL1.
HPAiHPA021773.
HPA026699.
MIMi606872. gene.
neXtProtiNX_Q75N03.
PharmGKBiPA134960329.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2932. Eukaryota.
ENOG410XQ6S. LUCA.
GeneTreeiENSGT00510000047522.
HOGENOMiHOG000082498.
HOVERGENiHBG057723.
InParanoidiQ75N03.
KOiK15685.
OMAiGTPHMVY.
OrthoDBiEOG7GN2NX.
PhylomeDBiQ75N03.
TreeFamiTF332910.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

GeneWikiiCBLL1.
GenomeRNAii79872.
PROiQ75N03.
SOURCEiSearch...

Gene expression databases

BgeeiQ75N03.
CleanExiHS_CBLL1.
ExpressionAtlasiQ75N03. baseline and differential.
GenevisibleiQ75N03. HS.

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. "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 1).
    Tissue: Lung.
  2. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [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] (ISOFORMS 1 AND 2).
    Tissue: Testis.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "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-290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  6. "Identification of Wilms' tumor 1-associating protein complex and its role in alternative splicing and the cell cycle."
    Horiuchi K., Kawamura T., Iwanari H., Ohashi R., Naito M., Kodama T., Hamakubo T.
    J. Biol. Chem. 288:33292-33302(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE WTAP COMPLEX, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiHAKAI_HUMAN
AccessioniPrimary (citable) accession number: Q75N03
Secondary accession number(s): B7ZM03, Q8TAJ4, Q9H5S6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: July 5, 2004
Last modified: June 8, 2016
This is version 111 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.