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Protein

Actin-binding LIM protein 3

Gene

ABLIM3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity.1 Publication

GO - Molecular functioni

  1. zinc ion binding Source: InterPro

GO - Biological processi

  1. actin cytoskeleton organization Source: InterPro
  2. axon guidance Source: Reactome
  3. cilium assembly Source: MGI
  4. lamellipodium assembly Source: MGI
  5. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  6. transcription, DNA-templated Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_22351. DCC mediated attractive signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-binding LIM protein 3
Short name:
abLIM-3
Alternative name(s):
Actin-binding LIM protein family member 3
Gene namesi
Name:ABLIM3
Synonyms:KIAA0843
ORF Names:HMFN1661
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:29132. ABLIM3.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. lamellipodium Source: MGI
  3. stress fiber Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134962761.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 683683Actin-binding LIM protein 3PRO_0000075702Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei277 – 2771PhosphoserineBy similarity
Modified residuei280 – 2801PhosphoserineBy similarity
Modified residuei282 – 2821Phosphoserine1 Publication
Modified residuei286 – 2861Phosphoserine1 Publication
Modified residuei372 – 3721Phosphoserine1 Publication
Modified residuei373 – 3731Phosphoserine1 Publication
Modified residuei376 – 3761Phosphotyrosine1 Publication
Modified residuei388 – 3881Phosphoserine1 Publication
Modified residuei493 – 4931Phosphoserine1 Publication
Modified residuei503 – 5031Phosphoserine3 Publications
Modified residuei504 – 5041Phosphoserine3 Publications
Modified residuei543 – 5431Phosphothreonine1 Publication
Modified residuei576 – 5761Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO94929.
PaxDbiO94929.
PRIDEiO94929.

PTM databases

PhosphoSiteiO94929.

Expressioni

Tissue specificityi

Expressed predominantly in heart and brain.1 Publication

Gene expression databases

BgeeiO94929.
CleanExiHS_ABLIM3.
ExpressionAtlasiO94929. baseline and differential.
GenevestigatoriO94929.

Organism-specific databases

HPAiHPA003245.

Interactioni

Subunit structurei

Directly interacts with F-actin and ABRA.1 Publication

Protein-protein interaction databases

BioGridi116552. 7 interactions.
IntActiO94929. 4 interactions.
MINTiMINT-4657493.
STRINGi9606.ENSP00000310309.

Structurei

Secondary structure

1
683
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni152 – 1543Combined sources
Beta strandi159 – 1613Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi169 – 1713Combined sources
Turni173 – 1753Combined sources
Beta strandi179 – 1813Combined sources
Beta strandi190 – 1923Combined sources
Beta strandi195 – 1973Combined sources
Helixi201 – 2055Combined sources
Turni623 – 6264Combined sources
Turni630 – 6334Combined sources
Turni642 – 6443Combined sources
Helixi645 – 6484Combined sources
Helixi653 – 6586Combined sources
Helixi662 – 6654Combined sources
Helixi670 – 67910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UJSNMR-A609-683[»]
2DJ7NMR-A141-207[»]
ProteinModelPortaliO94929.
SMRiO94929. Positions 34-268, 607-683.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO94929.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 8060LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini80 – 14061LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini149 – 20860LIM zinc-binding 3PROSITE-ProRule annotationAdd
BLAST
Domaini208 – 26861LIM zinc-binding 4PROSITE-ProRule annotationAdd
BLAST
Domaini615 – 68369HPPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiNOG302299.
GeneTreeiENSGT00760000119039.
HOGENOMiHOG000285997.
HOVERGENiHBG031499.
InParanoidiO94929.
KOiK07520.
OMAiDPYYASE.
OrthoDBiEOG71CFKF.
PhylomeDBiO94929.
TreeFamiTF318042.

Family and domain databases

Gene3Di1.10.950.10. 1 hit.
2.10.110.10. 4 hits.
InterProiIPR028449. ABLIM3.
IPR003128. Villin_headpiece.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR24213:SF0. PTHR24213:SF0. 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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O94929-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNTSIPYQQN PYNPRGSSNV IQCYRCGDTC KGEVVRVHNN HFHIRCFTCQ
60 70 80 90 100
VCGCGLAQSG FFFKNQEYIC TQDYQQLYGT RCDSCRDFIT GEVISALGRT
110 120 130 140 150
YHPKCFVCSL CRKPFPIGDK VTFSGKECVC QTCSQSMASS KPIKIRGPSH
160 170 180 190 200
CAGCKEEIKH GQSLLALDKQ WHVSCFKCQT CSVILTGEYI SKDGVPYCES
210 220 230 240 250
DYHAQFGIKC ETCDRYISGR VLEAGGKHYH PTCARCVRCH QMFTEGEEMY
260 270 280 290 300
LTGSEVWHPI CKQAARAEKK LKHRRTSETS ISPPGSSIGS PNRVICAKVD
310 320 330 340 350
NEILNYKDLA ALPKVKSIYE VQRPDLISYE PHSRYMSDEM LERCGYGESL
360 370 380 390 400
GTLSPYSQDI YENLDLRQRR ASSPGYIDSP TYSRQGMSPT FSRSPHHYYR
410 420 430 440 450
SGPESGRSSP YHSQLDVRSS TPTSYQAPKH FHIPAGDSNI YRKPPIYKRH
460 470 480 490 500
GDLSTATKSK TSEDISQTSK YSPIYSPDPY YASESEYWTY HGSPKVPRAR
510 520 530 540 550
RFSSGGEEDD FDRSMHKLQS GIGRLILKEE MKARSSSYAD PWTPPRSSTS
560 570 580 590 600
SREALHTAGY EMSLNGSPRS HYLADSDPLI SKSASLPAYR RNGLHRTPSA
610 620 630 640 650
DLFHYDSMNA VNWGMREYKI YPYELLLVTT RGRNRLPKDV DRTRLERHLS
660 670 680
QEEFYQVFGM TISEFDRLAL WKRNELKKQA RLF
Length:683
Mass (Da):77,802
Last modified:December 6, 2004 - v3
Checksum:i0392DBD9065EE08A
GO
Isoform 2 (identifier: O94929-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     297-358: Missing.
     402-450: Missing.
     647-683: RHLSQEEFYQVFGMTISEFDRLALWKRNELKKQARLF → GNFWKSGCL

Note: No experimental confirmation available.

Show »
Length:544
Mass (Da):61,570
Checksum:iE6A19F001BF02176
GO
Isoform 3 (identifier: O94929-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     297-358: Missing.
     402-434: Missing.

Note: No experimental confirmation available.

Show »
Length:588
Mass (Da):67,073
Checksum:i858F0D8EA50B1A57
GO
Isoform 4 (identifier: O94929-4) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.

Show »
Length:169
Mass (Da):19,695
Checksum:i18F1F045422E1552
GO

Sequence cautioni

The sequence BAA74866.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti227 – 2271K → R in BAF82425 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti125 – 1251G → D.
Corresponds to variant rs35907283 [ dbSNP | Ensembl ].
VAR_050143

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 514514Missing in isoform 4. 1 PublicationVSP_012126Add
BLAST
Alternative sequencei297 – 35862Missing in isoform 2 and isoform 3. 3 PublicationsVSP_012127Add
BLAST
Alternative sequencei402 – 45049Missing in isoform 2. 1 PublicationVSP_012128Add
BLAST
Alternative sequencei402 – 43433Missing in isoform 3. 2 PublicationsVSP_012129Add
BLAST
Alternative sequencei647 – 68337RHLSQ…QARLF → GNFWKSGCL in isoform 2. 1 PublicationVSP_012130Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ413174 mRNA. Translation: ABD83327.1.
AB020650 mRNA. Translation: BAA74866.2. Different initiation.
AK289736 mRNA. Translation: BAF82425.1.
AB075881 mRNA. Translation: BAD38663.1.
BC001665 mRNA. Translation: AAH01665.1.
AL833021 mRNA. Translation: CAH56270.1.
CCDSiCCDS4294.1. [O94929-1]
RefSeqiNP_001287944.1. NM_001301015.1. [O94929-1]
NP_001287947.1. NM_001301018.1.
NP_001287956.1. NM_001301027.1.
NP_001287957.1. NM_001301028.1. [O94929-2]
NP_055760.1. NM_014945.3. [O94929-1]
XP_005268449.1. XM_005268392.1.
XP_005268452.1. XM_005268395.1. [O94929-3]
UniGeneiHs.49688.

Genome annotation databases

EnsembliENST00000309868; ENSP00000310309; ENSG00000173210. [O94929-1]
ENST00000326685; ENSP00000315841; ENSG00000173210. [O94929-3]
ENST00000504238; ENSP00000421183; ENSG00000173210. [O94929-2]
ENST00000506113; ENSP00000425394; ENSG00000173210. [O94929-1]
ENST00000517451; ENSP00000430150; ENSG00000173210. [O94929-4]
GeneIDi22885.
KEGGihsa:22885.
UCSCiuc003lpy.2. human. [O94929-1]
uc003lqa.1. human. [O94929-2]
uc003lqd.1. human. [O94929-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ413174 mRNA. Translation: ABD83327.1.
AB020650 mRNA. Translation: BAA74866.2. Different initiation.
AK289736 mRNA. Translation: BAF82425.1.
AB075881 mRNA. Translation: BAD38663.1.
BC001665 mRNA. Translation: AAH01665.1.
AL833021 mRNA. Translation: CAH56270.1.
CCDSiCCDS4294.1. [O94929-1]
RefSeqiNP_001287944.1. NM_001301015.1. [O94929-1]
NP_001287947.1. NM_001301018.1.
NP_001287956.1. NM_001301027.1.
NP_001287957.1. NM_001301028.1. [O94929-2]
NP_055760.1. NM_014945.3. [O94929-1]
XP_005268449.1. XM_005268392.1.
XP_005268452.1. XM_005268395.1. [O94929-3]
UniGeneiHs.49688.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UJSNMR-A609-683[»]
2DJ7NMR-A141-207[»]
ProteinModelPortaliO94929.
SMRiO94929. Positions 34-268, 607-683.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116552. 7 interactions.
IntActiO94929. 4 interactions.
MINTiMINT-4657493.
STRINGi9606.ENSP00000310309.

PTM databases

PhosphoSiteiO94929.

Proteomic databases

MaxQBiO94929.
PaxDbiO94929.
PRIDEiO94929.

Protocols and materials databases

DNASUi22885.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309868; ENSP00000310309; ENSG00000173210. [O94929-1]
ENST00000326685; ENSP00000315841; ENSG00000173210. [O94929-3]
ENST00000504238; ENSP00000421183; ENSG00000173210. [O94929-2]
ENST00000506113; ENSP00000425394; ENSG00000173210. [O94929-1]
ENST00000517451; ENSP00000430150; ENSG00000173210. [O94929-4]
GeneIDi22885.
KEGGihsa:22885.
UCSCiuc003lpy.2. human. [O94929-1]
uc003lqa.1. human. [O94929-2]
uc003lqd.1. human. [O94929-3]

Organism-specific databases

CTDi22885.
GeneCardsiGC05P148501.
HGNCiHGNC:29132. ABLIM3.
HPAiHPA003245.
MIMi611305. gene.
neXtProtiNX_O94929.
PharmGKBiPA134962761.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG302299.
GeneTreeiENSGT00760000119039.
HOGENOMiHOG000285997.
HOVERGENiHBG031499.
InParanoidiO94929.
KOiK07520.
OMAiDPYYASE.
OrthoDBiEOG71CFKF.
PhylomeDBiO94929.
TreeFamiTF318042.

Enzyme and pathway databases

ReactomeiREACT_22351. DCC mediated attractive signaling.

Miscellaneous databases

ChiTaRSiABLIM3. human.
EvolutionaryTraceiO94929.
GeneWikiiABLIM3.
GenomeRNAii22885.
NextBioi43475.
PROiO94929.
SOURCEiSearch...

Gene expression databases

BgeeiO94929.
CleanExiHS_ABLIM3.
ExpressionAtlasiO94929. baseline and differential.
GenevestigatoriO94929.

Family and domain databases

Gene3Di1.10.950.10. 1 hit.
2.10.110.10. 4 hits.
InterProiIPR028449. ABLIM3.
IPR003128. Villin_headpiece.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR24213:SF0. PTHR24213:SF0. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH F-ACTIN AND ABRA.
    Tissue: Heart.
  2. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:355-364(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas."
    Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.
    Oncogene 23:5901-5911(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Hepatoblastoma.
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Colon.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 117-683 (ISOFORM 3).
    Tissue: Stomach.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-504, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  9. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-504, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282; SER-286; SER-372; SER-373; TYR-376; SER-388; SER-493; SER-503; SER-504; THR-543 AND SER-576, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Solution structure of the villin headpiece domain of human actin-binding LIM protein homologue (KIAA0843 protein)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JAN-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 610-683.

Entry informationi

Entry nameiABLM3_HUMAN
AccessioniPrimary (citable) accession number: O94929
Secondary accession number(s): A8K121
, Q19VH3, Q658S1, Q68CI5, Q9BV32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2004
Last sequence update: December 6, 2004
Last modified: March 3, 2015
This is version 130 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.