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O14639

- ABLM1_HUMAN

UniProt

O14639 - ABLM1_HUMAN

Protein

Actin-binding LIM protein 1

Gene

ABLIM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (23 Sep 2008)
      Previous versions | rss
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    Functioni

    May act as scaffold protein By similarity. May play a role in the development of the retina. Has been suggested to play a role in axon guidance.By similarity1 Publication

    GO - Molecular functioni

    1. actin binding Source: ProtInc
    2. protein binding Source: IntAct
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. cytoskeleton organization Source: InterPro
    3. organ morphogenesis Source: ProtInc
    4. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    5. visual perception Source: ProtInc

    Keywords - Ligandi

    Actin-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_22351. DCC mediated attractive signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Actin-binding LIM protein 1
    Short name:
    abLIM-1
    Alternative name(s):
    Actin-binding LIM protein family member 1
    Actin-binding double zinc finger protein
    LIMAB1
    Limatin
    Gene namesi
    Name:ABLIM1
    Synonyms:ABLIM, KIAA0059, LIMAB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:78. ABLIM1.

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity
    Note: Associated with the cytoskeleton.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35023.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 778778Actin-binding LIM protein 1PRO_0000075697Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei367 – 3671Phosphoserine1 Publication
    Modified residuei373 – 3731Phosphotyrosine1 Publication
    Modified residuei396 – 3961Phosphotyrosine1 Publication
    Modified residuei426 – 4261Phosphoserine1 Publication
    Modified residuei431 – 4311Phosphoserine2 Publications
    Modified residuei433 – 4331Phosphothreonine1 Publication
    Modified residuei435 – 4351Phosphoserine4 Publications
    Modified residuei439 – 4391Phosphotyrosine1 Publication
    Modified residuei455 – 4551Phosphoserine1 Publication
    Modified residuei458 – 4581Phosphoserine1 Publication
    Modified residuei587 – 5871Phosphoserine1 Publication
    Modified residuei640 – 6401Phosphoserine2 Publications
    Modified residuei655 – 6551Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO14639.
    PaxDbiO14639.
    PRIDEiO14639.

    PTM databases

    PhosphoSiteiO14639.

    Expressioni

    Tissue specificityi

    Detected in liver, heart, skeletal muscle, brain and retina, where it is concentrated in the inner segment and in the outer plexiform layers.1 Publication

    Gene expression databases

    ArrayExpressiO14639.
    BgeeiO14639.
    CleanExiHS_ABLIM1.
    GenevestigatoriO14639.

    Organism-specific databases

    HPAiHPA038951.
    HPA038952.

    Interactioni

    Subunit structurei

    Binds F-actin. Interacts with ABRA.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LDOC1O957512EBI-487024,EBI-740738

    Protein-protein interaction databases

    BioGridi110171. 21 interactions.
    IntActiO14639. 17 interactions.
    MINTiMINT-1447354.
    STRINGi9606.ENSP00000338190.

    Structurei

    3D structure databases

    ProteinModelPortaliO14639.
    SMRiO14639. Positions 89-344, 714-778.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini97 – 15660LIM zinc-binding 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini156 – 21661LIM zinc-binding 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini224 – 28360LIM zinc-binding 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini283 – 34361LIM zinc-binding 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini710 – 77869HPPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili590 – 61425Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 HP (headpiece) domain.PROSITE-ProRule annotation
    Contains 4 LIM zinc-binding domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, LIM domain, Repeat

    Phylogenomic databases

    eggNOGiNOG302299.
    HOVERGENiHBG031499.
    KOiK07520.
    OMAiHHPSEKP.
    PhylomeDBiO14639.
    TreeFamiTF318042.

    Family and domain databases

    Gene3Di1.10.950.10. 1 hit.
    2.10.110.10. 4 hits.
    InterProiIPR028448. ABLIM1.
    IPR003128. Villin_headpiece.
    IPR001781. Znf_LIM.
    [Graphical view]
    PANTHERiPTHR24213:SF18. PTHR24213:SF18. 1 hit.
    PfamiPF00412. LIM. 4 hits.
    PF02209. VHP. 1 hit.
    [Graphical view]
    SMARTiSM00132. LIM. 4 hits.
    SM00153. VHP. 1 hit.
    [Graphical view]
    SUPFAMiSSF47050. SSF47050. 1 hit.
    PROSITEiPS51089. HP. 1 hit.
    PS00478. LIM_DOMAIN_1. 4 hits.
    PS50023. LIM_DOMAIN_2. 4 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O14639-1) [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

    MPAFLGLKCL GKLCSSEKSK VTSSERTSAR GSNRKRLIVE DRRVSGTSFT    50
    AHRRATITHL LYLCPKDYCP RGRVCNSVDP FVAHPQDPHH PSEKPVIHCH 100
    KCGEPCKGEV LRVQTKHFHI KCFTCKVCGC DLAQGGFFIK NGEYLCTLDY 150
    QRMYGTRCHG CGEFVEGEVV TALGKTYHPN CFACTICKRP FPPGDRVTFN 200
    GRDCLCQLCA QPMSSSPKET TFSSNCAGCG RDIKNGQALL ALDKQWHLGC 250
    FKCKSCGKVL TGEYISKDGA PYCEKDYQGL FGVKCEACHQ FITGKVLEAG 300
    DKHYHPSCAR CSRCNQMFTE GEEMYLQGST VWHPDCKQST KTEEKLRPTR 350
    TSSESIYSRP GSSIPGSPGH TIYAKVDNEI LDYKDLAAIP KVKAIYDIER 400
    PDLITYEPFY TSGYDDKQER QSLGESPRTL SPTPSAEGYQ DVRDRMIHRS 450
    TSQGSINSPV YSRHSYTPTT SRSPQHFHRP GNEPSSGRNS PLPYRPDSRP 500
    LTPTYAQAPK HFHVPDQGIN IYRKPPIYKQ HAALAAQSKS SEDIIKFSKF 550
    PAAQAPDPSE TPKIETDHWP GPPSFAVVGP DMKRRSSGRE EDDEELLRRR 600
    QLQEEQLMKL NSGLGQLILK EEMEKESRER SSLLASRYDS PINSASHIPS 650
    SKTASLPGYG RNGLHRPVST DFAQYNSYGD VSGGVRDYQT LPDGHMPAMR 700
    MDRGVSMPNM LEPKIFPYEM LMVTNRGRNK ILREVDRTRL ERHLAPEVFR 750
    EIFGMSIQEF DRLPLWRRND MKKKAKLF 778
    Length:778
    Mass (Da):87,688
    Last modified:September 23, 2008 - v3
    Checksum:iEBC2F14BE558752B
    GO
    Isoform 2 (identifier: O14639-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-81: MPAFLGLKCL...GRVCNSVDPF → MLMTLEMTELTDPHHTMGDYK

    Show »
    Length:718
    Mass (Da):81,121
    Checksum:iA9CAEEBA95BDF15E
    GO
    Isoform 3 (identifier: O14639-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-316: Missing.
         480-514: Missing.

    Show »
    Length:427
    Mass (Da):48,804
    Checksum:i1721FB3EC1D99994
    GO
    Isoform 4 (identifier: O14639-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-316: Missing.
         348-373: Missing.
         480-514: Missing.

    Show »
    Length:401
    Mass (Da):46,087
    Checksum:i0B2AC94C24A5D72F
    GO
    Isoform 5 (identifier: O14639-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-316: Missing.
         347-347: R → RLPNIRRSSSDFFYSKSLIRRTGRSPSLQ
         480-514: Missing.

    Show »
    Length:455
    Mass (Da):52,056
    Checksum:iCA7E610D14878674
    GO

    Sequence cautioni

    The sequence BAA06681.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti499 – 4991R → L in AAC51676. (PubMed:9245787)Curated
    Sequence conflicti532 – 5321A → R in AAC51676. (PubMed:9245787)Curated
    Sequence conflicti563 – 5631K → E in BAA06681. (PubMed:7584044)Curated
    Sequence conflicti578 – 5781V → I in BAA06681. (PubMed:7584044)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti434 – 4341P → T.
    Corresponds to variant rs11593544 [ dbSNP | Ensembl ].
    VAR_050141
    Natural varianti637 – 6371R → G.
    Corresponds to variant rs7091419 [ dbSNP | Ensembl ].
    VAR_050142

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 316316Missing in isoform 3, isoform 4 and isoform 5. 3 PublicationsVSP_012099Add
    BLAST
    Alternative sequencei1 – 8181MPAFL…SVDPF → MLMTLEMTELTDPHHTMGDY K in isoform 2. 1 PublicationVSP_012100Add
    BLAST
    Alternative sequencei347 – 3471R → RLPNIRRSSSDFFYSKSLIR RTGRSPSLQ in isoform 5. 1 PublicationVSP_041185
    Alternative sequencei348 – 37326Missing in isoform 4. 1 PublicationVSP_012101Add
    BLAST
    Alternative sequencei480 – 51435Missing in isoform 3, isoform 4 and isoform 5. 3 PublicationsVSP_012102Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF005654 mRNA. Translation: AAC51676.1.
    D31883 mRNA. Translation: BAA06681.2. Different initiation.
    AK098277 mRNA. Translation: BAG53605.1.
    CR749819 mRNA. Translation: CAH18679.1.
    AL133384 Genomic DNA. Translation: CAI40135.1.
    AL133384 Genomic DNA. Translation: CAI40136.1.
    AL133384, AL354873 Genomic DNA. Translation: CAI40140.1.
    AL133384, AL354873 Genomic DNA. Translation: CAI40141.1.
    AL354873, AL133384 Genomic DNA. Translation: CAI10908.1.
    AL354873, AL133384 Genomic DNA. Translation: CAI10910.1.
    AL590109 Genomic DNA. No translation available.
    BC002448 mRNA. Translation: AAH02448.1.
    CCDSiCCDS31288.1. [O14639-2]
    CCDS31289.1. [O14639-5]
    CCDS7590.1. [O14639-1]
    RefSeqiNP_001003407.1. NM_001003407.1. [O14639-2]
    NP_001003408.1. NM_001003408.1.
    NP_002304.3. NM_002313.5. [O14639-1]
    NP_006711.3. NM_006720.3. [O14639-5]
    XP_005269885.1. XM_005269828.2. [O14639-3]
    UniGeneiHs.438236.
    Hs.538331.
    Hs.593868.

    Genome annotation databases

    EnsembliENST00000277895; ENSP00000277895; ENSG00000099204. [O14639-1]
    ENST00000369252; ENSP00000358256; ENSG00000099204. [O14639-2]
    ENST00000369253; ENSP00000358257; ENSG00000099204. [O14639-4]
    ENST00000392952; ENSP00000376679; ENSG00000099204. [O14639-5]
    GeneIDi3983.
    KEGGihsa:3983.
    UCSCiuc021pyu.1. human. [O14639-5]
    uc021pyw.1. human. [O14639-1]
    uc021pyz.1. human. [O14639-2]
    uc021pzc.1. human. [O14639-4]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF005654 mRNA. Translation: AAC51676.1 .
    D31883 mRNA. Translation: BAA06681.2 . Different initiation.
    AK098277 mRNA. Translation: BAG53605.1 .
    CR749819 mRNA. Translation: CAH18679.1 .
    AL133384 Genomic DNA. Translation: CAI40135.1 .
    AL133384 Genomic DNA. Translation: CAI40136.1 .
    AL133384 , AL354873 Genomic DNA. Translation: CAI40140.1 .
    AL133384 , AL354873 Genomic DNA. Translation: CAI40141.1 .
    AL354873 , AL133384 Genomic DNA. Translation: CAI10908.1 .
    AL354873 , AL133384 Genomic DNA. Translation: CAI10910.1 .
    AL590109 Genomic DNA. No translation available.
    BC002448 mRNA. Translation: AAH02448.1 .
    CCDSi CCDS31288.1. [O14639-2 ]
    CCDS31289.1. [O14639-5 ]
    CCDS7590.1. [O14639-1 ]
    RefSeqi NP_001003407.1. NM_001003407.1. [O14639-2 ]
    NP_001003408.1. NM_001003408.1.
    NP_002304.3. NM_002313.5. [O14639-1 ]
    NP_006711.3. NM_006720.3. [O14639-5 ]
    XP_005269885.1. XM_005269828.2. [O14639-3 ]
    UniGenei Hs.438236.
    Hs.538331.
    Hs.593868.

    3D structure databases

    ProteinModelPortali O14639.
    SMRi O14639. Positions 89-344, 714-778.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110171. 21 interactions.
    IntActi O14639. 17 interactions.
    MINTi MINT-1447354.
    STRINGi 9606.ENSP00000338190.

    PTM databases

    PhosphoSitei O14639.

    Proteomic databases

    MaxQBi O14639.
    PaxDbi O14639.
    PRIDEi O14639.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000277895 ; ENSP00000277895 ; ENSG00000099204 . [O14639-1 ]
    ENST00000369252 ; ENSP00000358256 ; ENSG00000099204 . [O14639-2 ]
    ENST00000369253 ; ENSP00000358257 ; ENSG00000099204 . [O14639-4 ]
    ENST00000392952 ; ENSP00000376679 ; ENSG00000099204 . [O14639-5 ]
    GeneIDi 3983.
    KEGGi hsa:3983.
    UCSCi uc021pyu.1. human. [O14639-5 ]
    uc021pyw.1. human. [O14639-1 ]
    uc021pyz.1. human. [O14639-2 ]
    uc021pzc.1. human. [O14639-4 ]

    Organism-specific databases

    CTDi 3983.
    GeneCardsi GC10M116190.
    HGNCi HGNC:78. ABLIM1.
    HPAi HPA038951.
    HPA038952.
    MIMi 602330. gene.
    neXtProti NX_O14639.
    PharmGKBi PA35023.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG302299.
    HOVERGENi HBG031499.
    KOi K07520.
    OMAi HHPSEKP.
    PhylomeDBi O14639.
    TreeFami TF318042.

    Enzyme and pathway databases

    Reactomei REACT_22351. DCC mediated attractive signaling.

    Miscellaneous databases

    ChiTaRSi ABLIM1. human.
    GeneWikii ABLIM1.
    GenomeRNAii 3983.
    NextBioi 15616.
    PROi O14639.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14639.
    Bgeei O14639.
    CleanExi HS_ABLIM1.
    Genevestigatori O14639.

    Family and domain databases

    Gene3Di 1.10.950.10. 1 hit.
    2.10.110.10. 4 hits.
    InterProi IPR028448. ABLIM1.
    IPR003128. Villin_headpiece.
    IPR001781. Znf_LIM.
    [Graphical view ]
    PANTHERi PTHR24213:SF18. PTHR24213:SF18. 1 hit.
    Pfami PF00412. LIM. 4 hits.
    PF02209. VHP. 1 hit.
    [Graphical view ]
    SMARTi SM00132. LIM. 4 hits.
    SM00153. VHP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47050. SSF47050. 1 hit.
    PROSITEi PS51089. HP. 1 hit.
    PS00478. LIM_DOMAIN_1. 4 hits.
    PS50023. LIM_DOMAIN_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of abLIM, a novel actin-binding and double zinc finger protein."
      Roof D.J., Hayes A., Adamian M., Chishti A.H., Li T.
      J. Cell Biol. 138:575-588(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
      Tissue: Retina.
    2. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
      Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
      DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Bone marrow.
    3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    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] (ISOFORM 5).
      Tissue: Uterus.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Retina.
    6. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      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 4).
      Tissue: Kidney.
    8. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Two novel members of the ABLIM protein family, ABLIM-2 and -3, associate with STARS and directly bind F-actin."
      Barrientos T., Frank D., Kuwahara K., Bezprozvannaya S., Pipes G.C.T., Bassel-Duby R., Richardson J.A., Katus H.A., Olson E.N., Frey N.
      J. Biol. Chem. 282:8393-8403(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ABRA.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-435; SER-455; SER-458; SER-587; SER-640 AND SER-655, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-367; TYR-373; SER-426; SER-431; THR-433 AND SER-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "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-435 AND SER-640, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "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-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiABLM1_HUMAN
    AccessioniPrimary (citable) accession number: O14639
    Secondary accession number(s): A6NI16
    , A6NJ06, A8MXA9, Q15039, Q5JVV1, Q5JVV2, Q5T6N3, Q5T6N5, Q68CQ9, Q9BUP1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 138 of the entry and version 3 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 10
      Human chromosome 10: 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