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Q96Q27

- ASB2_HUMAN

UniProt

Q96Q27 - ASB2_HUMAN

Protein

Ankyrin repeat and SOCS box protein 2

Gene

ASB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.2 Publications

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. ubiquitin-protein transferase activity Source: Ensembl

    GO - Biological processi

    1. intracellular signal transduction Source: InterPro
    2. myoblast differentiation Source: Ensembl
    3. protein polyubiquitination Source: Ensembl
    4. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: Ensembl
    5. signal transduction Source: ProtInc
    6. skeletal muscle cell differentiation Source: Ensembl

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ankyrin repeat and SOCS box protein 2
    Short name:
    ASB-2
    Gene namesi
    Name:ASB2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:16012. ASB2.

    Subcellular locationi

    GO - Cellular componenti

    1. Cul5-RING ubiquitin ligase complex Source: Ensembl

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi548 – 5481L → P: No interaction with Elongin BC complex. 2 Publications
    Mutagenesisi551 – 5522LC → PF: No interaction with CUL5 or RNF7. 1 Publication
    Mutagenesisi552 – 5521C → P: No interaction with Elongin BC complex. 2 Publications
    Mutagenesisi571 – 5744LPLP → AAAA: No interaction with CUL5 or RNF7. 1 Publication

    Organism-specific databases

    PharmGKBiPA25030.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 587587Ankyrin repeat and SOCS box protein 2PRO_0000066925Add
    BLAST

    Proteomic databases

    PaxDbiQ96Q27.
    PRIDEiQ96Q27.

    PTM databases

    PhosphoSiteiQ96Q27.

    Expressioni

    Inductioni

    By all-trans retinoic acid (ATRA).2 Publications

    Gene expression databases

    ArrayExpressiQ96Q27.
    BgeeiQ96Q27.
    CleanExiHS_ASB2.
    GenevestigatoriQ96Q27.

    Organism-specific databases

    HPAiHPA001546.

    Interactioni

    Subunit structurei

    Component of a probable ECS E3 ubiquitin-protein ligase complex which contains CUL5, either RBX1 or RNF7/RBX2, Elongin BC complex (TCEB1 and TCEB2) and ASB2.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CUL5Q930344EBI-2880677,EBI-1057139
    RNF7Q9UBF62EBI-2880677,EBI-398632

    Protein-protein interaction databases

    BioGridi119674. 36 interactions.
    IntActiQ96Q27. 5 interactions.
    MINTiMINT-1187414.
    STRINGi9606.ENSP00000320675.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96Q27.
    SMRiQ96Q27. Positions 10-449.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati56 – 8530ANK 1Add
    BLAST
    Repeati89 – 11931ANK 2Add
    BLAST
    Repeati123 – 15230ANK 3Add
    BLAST
    Repeati156 – 18530ANK 4Add
    BLAST
    Repeati189 – 21830ANK 5Add
    BLAST
    Repeati222 – 25130ANK 6Add
    BLAST
    Repeati255 – 28430ANK 7Add
    BLAST
    Repeati288 – 31730ANK 8Add
    BLAST
    Repeati320 – 34930ANK 9Add
    BLAST
    Repeati362 – 39130ANK 10Add
    BLAST
    Repeati392 – 42130ANK 11Add
    BLAST
    Repeati428 – 45629ANK 12Add
    BLAST
    Domaini533 – 58755SOCS boxPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes.By similarity

    Sequence similaritiesi

    Contains 12 ANK repeats.PROSITE-ProRule annotation
    Contains 1 SOCS box domain.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    HOGENOMiHOG000034086.
    HOVERGENiHBG104037.
    InParanoidiQ96Q27.
    KOiK10324.
    OMAiRPLAHLC.
    OrthoDBiEOG77DJ5P.
    PhylomeDBiQ96Q27.
    TreeFamiTF315127.

    Family and domain databases

    Gene3Di1.25.40.20. 4 hits.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR001496. SOCS_C.
    [Graphical view]
    PfamiPF00023. Ank. 2 hits.
    PF12796. Ank_2. 3 hits.
    PF07525. SOCS_box. 1 hit.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 11 hits.
    SM00969. SOCS_box. 1 hit.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 9 hits.
    PS50225. SOCS. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96Q27-1) [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

    MTRFSYAEYF SLFHSCSAPS RSTAPPESSP ARAPMGLFQG VMQKYSSSLF    50
    KTSQLAPADP LIKAIKDGDE EALKTMIKEG KNLAEPNKEG WLPLHEAAYY 100
    GQVGCLKVLQ RAYPGTIDQR TLQEETAVYL ATCRGHLDCL LSLLQAGAEP 150
    DISNKSRETP LYKACERKNA EAVKILVQHN ADTNHRCNRG WTALHESVSR 200
    NDLEVMQILV SGGAKVESKN AYGITPLFVA AQSGQLEALR FLAKYGADIN 250
    TQASDNASAL YEACKNEHEE VVEFLLSQGA DANKTNKDGL LPLHIASKKG 300
    NYRIVQMLLP VTSRTRIRRS GVSPLHLAAE RNHDEVLEAL LSARFDVNTP 350
    LAPERARLYE DRRSSALYFA VVNNNVYATE LLLQHGADPN RDVISPLLVA 400
    IRHGCLRTMQ LLLDHGANID AYIATHPTAF PATIMFAMKC LSLLKFLMDL 450
    GCDGEPCFSC LYGNGPHPPA PQPSSRFNDA PAADKEPSVV QFCEFVSAPE 500
    VSRWAGPIID VLLDYVGNVQ LCSRLKEHID SFEDWAVIKE KAEPPRPLAH 550
    LCRLRVRKAI GKYRIKLLDT LPLPGRLIRY LKYENTQ 587
    Length:587
    Mass (Da):65,084
    Last modified:December 1, 2001 - v1
    Checksum:i866A2B6010C4C1F9
    GO
    Isoform 2 (identifier: Q96Q27-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-20: MTRFSYAEYFSLFHSCSAPS → MATQISTRGS...RQPAHFYPWT

    Show »
    Length:635
    Mass (Da):70,212
    Checksum:iB91E4EB394531076
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti224 – 2241Missing in AAD45345. (PubMed:11111040)Curated
    Sequence conflicti460 – 4601Missing in AAD45345. (PubMed:11111040)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti160 – 1601P → S.
    Corresponds to variant rs2295213 [ dbSNP | Ensembl ].
    VAR_022089

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2020MTRFS…CSAPS → MATQISTRGSQCTIGQEEYS LYSSLSEDELVQMAIEQSLA DKTRGPTTAEATASACTNRQ PAHFYPWT in isoform 2. 2 PublicationsVSP_043042Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB056723 mRNA. Translation: BAB64532.1.
    AJ251238 mRNA. Translation: CAC17765.1.
    AB488462 mRNA. Translation: BAI77868.1.
    AK303686 mRNA. Translation: BAG64678.1.
    AK315628 mRNA. Translation: BAG37996.1.
    AL079302 Genomic DNA. No translation available.
    AL132642 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW81540.1.
    CH471061 Genomic DNA. Translation: EAW81542.1.
    BC032354 mRNA. Translation: AAH32354.1.
    AL137735 mRNA. Translation: CAB70899.1.
    AF159164 mRNA. Translation: AAD45345.1.
    CCDSiCCDS55940.1. [Q96Q27-2]
    CCDS9915.1. [Q96Q27-1]
    PIRiT46507.
    RefSeqiNP_001189358.1. NM_001202429.1. [Q96Q27-2]
    NP_057234.2. NM_016150.4. [Q96Q27-1]
    XP_005267815.1. XM_005267758.1. [Q96Q27-2]
    XP_006725228.1. XM_006725165.1. [Q96Q27-2]
    UniGeneiHs.510327.

    Genome annotation databases

    EnsembliENST00000315988; ENSP00000320675; ENSG00000100628. [Q96Q27-1]
    ENST00000555019; ENSP00000451575; ENSG00000100628. [Q96Q27-2]
    GeneIDi51676.
    KEGGihsa:51676.
    UCSCiuc001ycc.2. human. [Q96Q27-1]
    uc001ycd.3. human. [Q96Q27-2]

    Polymorphism databases

    DMDMi20531999.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB056723 mRNA. Translation: BAB64532.1 .
    AJ251238 mRNA. Translation: CAC17765.1 .
    AB488462 mRNA. Translation: BAI77868.1 .
    AK303686 mRNA. Translation: BAG64678.1 .
    AK315628 mRNA. Translation: BAG37996.1 .
    AL079302 Genomic DNA. No translation available.
    AL132642 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW81540.1 .
    CH471061 Genomic DNA. Translation: EAW81542.1 .
    BC032354 mRNA. Translation: AAH32354.1 .
    AL137735 mRNA. Translation: CAB70899.1 .
    AF159164 mRNA. Translation: AAD45345.1 .
    CCDSi CCDS55940.1. [Q96Q27-2 ]
    CCDS9915.1. [Q96Q27-1 ]
    PIRi T46507.
    RefSeqi NP_001189358.1. NM_001202429.1. [Q96Q27-2 ]
    NP_057234.2. NM_016150.4. [Q96Q27-1 ]
    XP_005267815.1. XM_005267758.1. [Q96Q27-2 ]
    XP_006725228.1. XM_006725165.1. [Q96Q27-2 ]
    UniGenei Hs.510327.

    3D structure databases

    ProteinModelPortali Q96Q27.
    SMRi Q96Q27. Positions 10-449.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119674. 36 interactions.
    IntActi Q96Q27. 5 interactions.
    MINTi MINT-1187414.
    STRINGi 9606.ENSP00000320675.

    PTM databases

    PhosphoSitei Q96Q27.

    Polymorphism databases

    DMDMi 20531999.

    Proteomic databases

    PaxDbi Q96Q27.
    PRIDEi Q96Q27.

    Protocols and materials databases

    DNASUi 51676.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000315988 ; ENSP00000320675 ; ENSG00000100628 . [Q96Q27-1 ]
    ENST00000555019 ; ENSP00000451575 ; ENSG00000100628 . [Q96Q27-2 ]
    GeneIDi 51676.
    KEGGi hsa:51676.
    UCSCi uc001ycc.2. human. [Q96Q27-1 ]
    uc001ycd.3. human. [Q96Q27-2 ]

    Organism-specific databases

    CTDi 51676.
    GeneCardsi GC14M094400.
    HGNCi HGNC:16012. ASB2.
    HPAi HPA001546.
    MIMi 605759. gene.
    neXtProti NX_Q96Q27.
    PharmGKBi PA25030.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0666.
    HOGENOMi HOG000034086.
    HOVERGENi HBG104037.
    InParanoidi Q96Q27.
    KOi K10324.
    OMAi RPLAHLC.
    OrthoDBi EOG77DJ5P.
    PhylomeDBi Q96Q27.
    TreeFami TF315127.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    GeneWikii ASB2.
    GenomeRNAii 51676.
    NextBioi 55678.
    PROi Q96Q27.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96Q27.
    Bgeei Q96Q27.
    CleanExi HS_ASB2.
    Genevestigatori Q96Q27.

    Family and domain databases

    Gene3Di 1.25.40.20. 4 hits.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR001496. SOCS_C.
    [Graphical view ]
    Pfami PF00023. Ank. 2 hits.
    PF12796. Ank_2. 3 hits.
    PF07525. SOCS_box. 1 hit.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    SMARTi SM00248. ANK. 11 hits.
    SM00969. SOCS_box. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 9 hits.
    PS50225. SOCS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ATRA-regulated Asb-2 gene induced in differentiation of HL-60 leukemia cells."
      Kohroki J., Fujita S., Itoh N., Yamada Y., Imai H., Yumoto N., Nakanishi T., Tanaka K.
      FEBS Lett. 505:223-228(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION.
    2. "ASB-2 inhibits growth and promotes commitment in myeloid leukemia cells."
      Guibal F.C., Moog-Lutz C., Smolewski P., Di Gioia Y., Darzynkiewicz Z., Lutz P.G., Cayre Y.E.
      J. Biol. Chem. 277:218-224(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION.
    3. "Ubiquitin-interacting motif on ankyrin repeat and SOCS box-containing protein (ASB) 2a and its application to purify polyubiquitinated proteins and associated proteins without denaturation."
      Kohroki J., Kuroda S., Takiguchi E., Kawakami T., Nakamura T., Nishiyama T., Masuho Y.
      Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    4. "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] (ISOFORMS 1 AND 2).
      Tissue: Kidney and Stomach.
    5. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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).
      Tissue: Blood.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-587 (ISOFORM 1).
      Tissue: Uterus.
    9. "Cloning and characterization of the genes encoding the ankyrin repeat and SOCS box-containing proteins Asb-1, Asb-2, Asb-3 and Asb-4."
      Kile B.T., Viney E.M., Willson T.A., Brodnicki T.C., Cancilla M.R., Herlihy A.S., Croker B.A., Baca M., Nicola N.A., Hilton D.J., Alexander W.S.
      Gene 258:31-41(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-587 (ISOFORM 1).
    10. "ASB proteins interact with cullin5 and Rbx2 to form E3 ubiquitin ligase complexes."
      Kohroki J., Nishiyama T., Nakamura T., Masuho Y.
      FEBS Lett. 579:6796-6802(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, INTERACTION WITH CUL5 AND RNF7, MUTAGENESIS OF 551-LEU-CYS-552 AND 571-LEU--PRO-574.
    11. "ASB2 is an elongin BC-interacting protein that can assemble with cullin 5 and Rbx1 to reconstitute an E3 ubiquitin ligase complex."
      Heuze M.L., Guibal F.C., Banks C.A., Conaway J.W., Conaway R.C., Cayre Y.E., Benecke A., Lutz P.G.
      J. Biol. Chem. 280:5468-5474(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, INTERACTION WITH TCEB1, MUTAGENESIS OF LEU-548 AND CYS-552.

    Entry informationi

    Entry nameiASB2_HUMAN
    AccessioniPrimary (citable) accession number: Q96Q27
    Secondary accession number(s): B2RDP9
    , B4E166, Q9NSU5, Q9Y567
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2002
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 120 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 14
      Human chromosome 14: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3