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O14639

- ABLM1_HUMAN

UniProt

O14639 - ABLM1_HUMAN

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Protein

Actin-binding LIM protein 1

Gene
ABLIM1, ABLIM, KIAA0059, LIMAB1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 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
Complete GO annotation...

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
Complete GO annotation...

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.

Family & Domainsi

Domains and Repeats

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili590 – 61425 Reviewed predictionAdd
BLAST

Sequence similaritiesi

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.

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. VSP_012099Add
BLAST
Alternative sequencei1 – 8181MPAFL…SVDPF → MLMTLEMTELTDPHHTMGDY K in isoform 2. VSP_012100Add
BLAST
Alternative sequencei347 – 3471R → RLPNIRRSSSDFFYSKSLIR RTGRSPSLQ in isoform 5. VSP_041185
Alternative sequencei348 – 37326Missing in isoform 4. VSP_012101Add
BLAST
Alternative sequencei480 – 51435Missing in isoform 3, isoform 4 and isoform 5. VSP_012102Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti499 – 4991R → L in AAC51676. 1 Publication
Sequence conflicti532 – 5321A → R in AAC51676. 1 Publication
Sequence conflicti563 – 5631K → E in BAA06681. 1 Publication
Sequence conflicti578 – 5781V → I in BAA06681. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 137 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

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