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Q96Q27

- ASB2_HUMAN

UniProt

Q96Q27 - ASB2_HUMAN

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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

Functioni

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
Isoform 1: Enhances adhesion of hematopoietic cells to fibronectin through targeting of filamins FLNA and FLNB for proteasomal degradation, it is transiantly expressed during hematopoietic cell differentiation.2 Publications
Isoform 2: Involved in myogenic differentiation and targets filamin FLNB for proteasomal degradation but not filamin FLNA.1 Publication

Pathwayi

GO - Molecular functioni

  1. 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
Complete GO annotation...

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
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

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

BgeeiQ96Q27.
CleanExiHS_ASB2.
ExpressionAtlasiQ96Q27. baseline and differential.
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 58-449.
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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi8 – 169Required for interaction with FLNA1 Publication

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
Both the N-terminus and ANK repeats 1 to 10 are necessary for interaction with filamins.1 Publication

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.
GeneTreeiENSGT00530000063050.
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

Also known as: ASB2alpha, hematopoietic-type1 Publication

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
MTRFSYAEYF SLFHSCSAPS RSTAPPESSP ARAPMGLFQG VMQKYSSSLF
60 70 80 90 100
KTSQLAPADP LIKAIKDGDE EALKTMIKEG KNLAEPNKEG WLPLHEAAYY
110 120 130 140 150
GQVGCLKVLQ RAYPGTIDQR TLQEETAVYL ATCRGHLDCL LSLLQAGAEP
160 170 180 190 200
DISNKSRETP LYKACERKNA EAVKILVQHN ADTNHRCNRG WTALHESVSR
210 220 230 240 250
NDLEVMQILV SGGAKVESKN AYGITPLFVA AQSGQLEALR FLAKYGADIN
260 270 280 290 300
TQASDNASAL YEACKNEHEE VVEFLLSQGA DANKTNKDGL LPLHIASKKG
310 320 330 340 350
NYRIVQMLLP VTSRTRIRRS GVSPLHLAAE RNHDEVLEAL LSARFDVNTP
360 370 380 390 400
LAPERARLYE DRRSSALYFA VVNNNVYATE LLLQHGADPN RDVISPLLVA
410 420 430 440 450
IRHGCLRTMQ LLLDHGANID AYIATHPTAF PATIMFAMKC LSLLKFLMDL
460 470 480 490 500
GCDGEPCFSC LYGNGPHPPA PQPSSRFNDA PAADKEPSVV QFCEFVSAPE
510 520 530 540 550
VSRWAGPIID VLLDYVGNVQ LCSRLKEHID SFEDWAVIKE KAEPPRPLAH
560 570 580
LCRLRVRKAI GKYRIKLLDT LPLPGRLIRY LKYENTQ
Length:587
Mass (Da):65,084
Last modified:December 1, 2001 - v1
Checksum:i866A2B6010C4C1F9
GO
Isoform 2 (identifier: Q96Q27-2) [UniParc]FASTAAdd to Basket

Also known as: ASB2beta, muscle-type1 Publication

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

Note: Contains a ubiquitin-interacting motif (UIM) at positions 26-41.

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:
EMBLi
GenBanki
DDBJi
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]
ENST00000612647; ENSP00000480388; ENSG00000278693. [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:
EMBLi
GenBanki
DDBJi
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 58-449.
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 ]
ENST00000612647 ; ENSP00000480388 ; ENSG00000278693 . [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.
GeneTreei ENSGT00530000063050.
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

Bgeei Q96Q27.
CleanExi HS_ASB2.
ExpressionAtlasi Q96Q27. baseline and differential.
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

« Hide 'large scale' publications
  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.
  12. "The E3 ubiquitin ligase specificity subunit ASB2beta is a novel regulator of muscle differentiation that targets filamin B to proteasomal degradation."
    Bello N.F., Lamsoul I., Heuze M.L., Metais A., Moreaux G., Calderwood D.A., Duprez D., Moog-Lutz C., Lutz P.G.
    Cell Death Differ. 16:921-932(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 2), ALTERNATIVE SPLICING.
  13. "Functional and structural insights into ASB2alpha, a novel regulator of integrin-dependent adhesion of hematopoietic cells."
    Lamsoul I., Burande C.F., Razinia Z., Houles T.C., Menoret D., Baldassarre M., Erard M., Moog-Lutz C., Calderwood D.A., Lutz P.G.
    J. Biol. Chem. 286:30571-30581(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ALTERNATIVE SPLICING.
  14. "ASB2alpha, an E3 ubiquitin ligase specificity subunit, regulates cell spreading and triggers proteasomal degradation of filamins by targeting the filamin calponin homology 1 domain."
    Razinia Z., Baldassarre M., Cantelli G., Calderwood D.A.
    J. Biol. Chem. 288:32093-32105(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 1).

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: November 26, 2014
This is version 122 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