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Q5T8D3

- ACBD5_HUMAN

UniProt

Q5T8D3 - ACBD5_HUMAN

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Protein

Acyl-CoA-binding domain-containing protein 5

Gene

ACBD5

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

Functioni

Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy but is dispensable for aggrephagy and nonselective autophagy. Binds medium- and long-chain acyl-CoA esters.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei98 – 981Acyl-CoA
Binding sitei117 – 1171Acyl-CoABy similarity

GO - Molecular functioni

  1. fatty-acyl-CoA binding Source: InterPro
  2. lipid binding Source: UniProtKB-KW

GO - Biological processi

  1. peroxisome degradation Source: UniProtKB
  2. transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Autophagy, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA-binding domain-containing protein 5
Gene namesi
Name:ACBD5
Synonyms:KIAA1996
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:23338. ACBD5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei506 – 52621HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. intracellular membrane-bounded organelle Source: HPA
  3. membrane Source: UniProtKB
  4. nucleus Source: HPA
  5. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134892991.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 534534Acyl-CoA-binding domain-containing protein 5PRO_0000287377Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei193 – 1931Phosphoserine1 Publication
Modified residuei194 – 1941Phosphoserine1 Publication
Modified residuei196 – 1961Phosphoserine1 Publication
Modified residuei200 – 2001Phosphoserine4 Publications
Modified residuei400 – 4001Phosphothreonine1 Publication
Modified residuei428 – 4281Phosphoserine1 Publication
Modified residuei469 – 4691N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ5T8D3.
PaxDbiQ5T8D3.
PRIDEiQ5T8D3.

PTM databases

PhosphoSiteiQ5T8D3.

Expressioni

Gene expression databases

BgeeiQ5T8D3.
CleanExiHS_ACBD5.
ExpressionAtlasiQ5T8D3. baseline and differential.
GenevestigatoriQ5T8D3.

Organism-specific databases

HPAiHPA011861.
HPA012145.

Interactioni

Protein-protein interaction databases

BioGridi124836. 3 interactions.
IntActiQ5T8D3. 1 interaction.
MINTiMINT-3040525.
STRINGi9606.ENSP00000379568.

Structurei

Secondary structure

1
534
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi41 – 5818Combined sources
Helixi65 – 7915Combined sources
Helixi93 – 10412Combined sources
Turni105 – 1073Combined sources
Helixi110 – 12718Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FLVX-ray1.70A/B41-136[»]
ProteinModelPortaliQ5T8D3.
SMRiQ5T8D3. Positions 39-130.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5T8D3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 13090ACBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni52 – 6110Acyl-CoA binding
Regioni72 – 765Acyl-CoA binding

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili190 – 21930Sequence AnalysisAdd
BLAST
Coiled coili447 – 47630Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 164Poly-Cys
Compositional biasi201 – 2044Poly-Glu
Compositional biasi528 – 5314Poly-Arg

Sequence similaritiesi

Belongs to the ATG37 family.Curated
Contains 1 ACB (acyl-CoA-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG4281.
GeneTreeiENSGT00730000110900.
HOVERGENiHBG106445.
InParanoidiQ5T8D3.
OMAiGRGHRMQ.
OrthoDBiEOG7TJ3JP.
PhylomeDBiQ5T8D3.
TreeFamiTF319446.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
InterProiIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR016347. M-assoc_diazepam-bd-inh.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
[Graphical view]
PIRSFiPIRSF002412. MA_DBI. 1 hit.
PRINTSiPR00689. ACOABINDINGP.
SUPFAMiSSF47027. SSF47027. 1 hit.
PROSITEiPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5T8D3-1) [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
MFQFHAGSWE SWCCCCLIPA DRPWDRGQHW QLEMADTRSV HETRFEAAVK
60 70 80 90 100
VIQSLPKNGS FQPTNEMMLK FYSFYKQATE GPCKLSRPGF WDPIGRYKWD
110 120 130 140 150
AWSSLGDMTK EEAMIAYVEE MKKIIETMPM TEKVEELLRV IGPFYEIVED
160 170 180 190 200
KKSGRSSDIT SVRLEKISKC LEDLGNVLTS TPNAKTVNGK AESSDSGAES
210 220 230 240 250
EEEEAQEEVK GAEQSDNDKK MMKKSADHKN LEVIVTNGYD KDGFVQDIQN
260 270 280 290 300
DIHASSSLNG RSTEEVKPID ENLGQTGKSA VCIHQDINDD HVEDVTGIQH
310 320 330 340 350
LTSDSDSEVY CDSMEQFGQE ESLDSFTSNN GPFQYYLGGH SSQPMENSGF
360 370 380 390 400
REDIQVPPGN GNIGNMQVVA VEGKGEVKHG GEDGRNNSGA PHREKRGGET
410 420 430 440 450
DEFSNVRRGR GHRMQHLSEG TKGRQVGSGG DGERWGSDRG SRGSLNEQIA
460 470 480 490 500
LVLMRLQEDM QNVLQRLQKL ETLTALQAKS STSTLQTAPQ PTSQRPSWWP
510 520 530
FEMSPGVLTF AIIWPFIAQW LVYLYYQRRR RKLN
Length:534
Mass (Da):60,092
Last modified:December 21, 2004 - v1
Checksum:i8BE9A09967717653
GO
Isoform 2 (identifier: Q5T8D3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     162-172: Missing.

Note: Contains a phosphothreonine at position 137.

Show »
Length:490
Mass (Da):54,786
Checksum:i35B7F4B27ECE706B
GO
Isoform 3 (identifier: Q5T8D3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MFQ → MLFLS
     162-172: Missing.

Note: Contains a phosphothreonine at position 172.

Show »
Length:525
Mass (Da):58,978
Checksum:i95E2AD87B672D414
GO
Isoform 4 (identifier: Q5T8D3-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-107: Missing.
     162-172: Missing.

Note: Contains a phosphothreonine at position 63.

Show »
Length:416
Mass (Da):46,268
Checksum:i2FD7CD93EAA41CC9
GO

Sequence cautioni

The sequence AAH30555.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti332 – 3321P → Q in AAP30852. 1 PublicationCurated
Sequence conflicti419 – 4191E → D in AAP30852. 1 PublicationCurated
Sequence conflicti478 – 4781A → T in AAP30852. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti472 – 4721T → M.
Corresponds to variant rs7918793 [ dbSNP | Ensembl ].
VAR_032301

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 107107Missing in isoform 4. 1 PublicationVSP_025448Add
BLAST
Alternative sequencei1 – 3333Missing in isoform 2. 1 PublicationVSP_025447Add
BLAST
Alternative sequencei1 – 33MFQ → MLFLS in isoform 3. 1 PublicationVSP_025446
Alternative sequencei162 – 17211Missing in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_025449Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF505653 mRNA. Translation: AAP30852.1.
AK057469 mRNA. Translation: BAG51918.1.
AL160291 Genomic DNA. Translation: CAI16911.1.
AL160291 Genomic DNA. Translation: CAI16912.1.
AL160291 Genomic DNA. Translation: CAI16913.1.
AL160291 Genomic DNA. Translation: CAI16914.1.
AL160291 Genomic DNA. Translation: CAI16915.1.
CH471072 Genomic DNA. Translation: EAW86062.1.
CH471072 Genomic DNA. Translation: EAW86061.1.
CH471072 Genomic DNA. Translation: EAW86063.1.
BC030555 mRNA. Translation: AAH30555.1. Different initiation.
AL133064 mRNA. Translation: CAB61388.1.
CCDSiCCDS44368.1. [Q5T8D3-3]
CCDS7154.1. [Q5T8D3-2]
PIRiT42665.
RefSeqiNP_001035938.1. NM_001042473.3. [Q5T8D3-2]
NP_001288180.1. NM_001301251.1. [Q5T8D3-4]
NP_001288181.1. NM_001301252.1. [Q5T8D3-4]
NP_001288182.1. NM_001301253.1. [Q5T8D3-4]
NP_663736.2. NM_145698.4. [Q5T8D3-3]
UniGeneiHs.530597.

Genome annotation databases

EnsembliENST00000375888; ENSP00000365049; ENSG00000107897. [Q5T8D3-1]
ENST00000375901; ENSP00000365066; ENSG00000107897. [Q5T8D3-4]
ENST00000375905; ENSP00000365070; ENSG00000107897. [Q5T8D3-2]
ENST00000396271; ENSP00000379568; ENSG00000107897. [Q5T8D3-3]
GeneIDi91452.
KEGGihsa:91452.
UCSCiuc001ito.3. human. [Q5T8D3-2]
uc001itp.3. human. [Q5T8D3-4]
uc001itr.2. human. [Q5T8D3-1]
uc010qdp.2. human. [Q5T8D3-3]

Polymorphism databases

DMDMi74745508.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF505653 mRNA. Translation: AAP30852.1 .
AK057469 mRNA. Translation: BAG51918.1 .
AL160291 Genomic DNA. Translation: CAI16911.1 .
AL160291 Genomic DNA. Translation: CAI16912.1 .
AL160291 Genomic DNA. Translation: CAI16913.1 .
AL160291 Genomic DNA. Translation: CAI16914.1 .
AL160291 Genomic DNA. Translation: CAI16915.1 .
CH471072 Genomic DNA. Translation: EAW86062.1 .
CH471072 Genomic DNA. Translation: EAW86061.1 .
CH471072 Genomic DNA. Translation: EAW86063.1 .
BC030555 mRNA. Translation: AAH30555.1 . Different initiation.
AL133064 mRNA. Translation: CAB61388.1 .
CCDSi CCDS44368.1. [Q5T8D3-3 ]
CCDS7154.1. [Q5T8D3-2 ]
PIRi T42665.
RefSeqi NP_001035938.1. NM_001042473.3. [Q5T8D3-2 ]
NP_001288180.1. NM_001301251.1. [Q5T8D3-4 ]
NP_001288181.1. NM_001301252.1. [Q5T8D3-4 ]
NP_001288182.1. NM_001301253.1. [Q5T8D3-4 ]
NP_663736.2. NM_145698.4. [Q5T8D3-3 ]
UniGenei Hs.530597.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3FLV X-ray 1.70 A/B 41-136 [» ]
ProteinModelPortali Q5T8D3.
SMRi Q5T8D3. Positions 39-130.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124836. 3 interactions.
IntActi Q5T8D3. 1 interaction.
MINTi MINT-3040525.
STRINGi 9606.ENSP00000379568.

PTM databases

PhosphoSitei Q5T8D3.

Polymorphism databases

DMDMi 74745508.

Proteomic databases

MaxQBi Q5T8D3.
PaxDbi Q5T8D3.
PRIDEi Q5T8D3.

Protocols and materials databases

DNASUi 91452.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375888 ; ENSP00000365049 ; ENSG00000107897 . [Q5T8D3-1 ]
ENST00000375901 ; ENSP00000365066 ; ENSG00000107897 . [Q5T8D3-4 ]
ENST00000375905 ; ENSP00000365070 ; ENSG00000107897 . [Q5T8D3-2 ]
ENST00000396271 ; ENSP00000379568 ; ENSG00000107897 . [Q5T8D3-3 ]
GeneIDi 91452.
KEGGi hsa:91452.
UCSCi uc001ito.3. human. [Q5T8D3-2 ]
uc001itp.3. human. [Q5T8D3-4 ]
uc001itr.2. human. [Q5T8D3-1 ]
uc010qdp.2. human. [Q5T8D3-3 ]

Organism-specific databases

CTDi 91452.
GeneCardsi GC10M027484.
HGNCi HGNC:23338. ACBD5.
HPAi HPA011861.
HPA012145.
neXtProti NX_Q5T8D3.
PharmGKBi PA134892991.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4281.
GeneTreei ENSGT00730000110900.
HOVERGENi HBG106445.
InParanoidi Q5T8D3.
OMAi GRGHRMQ.
OrthoDBi EOG7TJ3JP.
PhylomeDBi Q5T8D3.
TreeFami TF319446.

Miscellaneous databases

ChiTaRSi ACBD5. human.
EvolutionaryTracei Q5T8D3.
GenomeRNAii 91452.
NextBioi 77259.
PROi Q5T8D3.

Gene expression databases

Bgeei Q5T8D3.
CleanExi HS_ACBD5.
ExpressionAtlasi Q5T8D3. baseline and differential.
Genevestigatori Q5T8D3.

Family and domain databases

Gene3Di 1.20.80.10. 1 hit.
InterProi IPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR016347. M-assoc_diazepam-bd-inh.
[Graphical view ]
Pfami PF00887. ACBP. 1 hit.
[Graphical view ]
PIRSFi PIRSF002412. MA_DBI. 1 hit.
PRINTSi PR00689. ACOABINDINGP.
SUPFAMi SSF47027. SSF47027. 1 hit.
PROSITEi PS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Functional research of a new human gene related to endozepine."
    Ye X., Mao Y., Xie Y.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
  2. "Peroxisomal Atg37 binds Atg30 or palmitoyl-CoA to regulate phagophore formation during pexophagy."
    Nazarko T.Y., Ozeki K., Till A., Ramakrishnan G., Lotfi P., Yan M., Subramani S.
    J. Cell Biol. 204:541-557(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 3).
    Tissue: Blood.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 252-534.
    Tissue: Testis.
  8. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; THR-400 AND SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193; SER-194; SER-196 AND SER-200, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-137 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "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 THR-137 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "The crystal structure of human acyl-coenzyme A binding domain containing 5."
    Structural genomics consortium (SGC)
    Submitted (JUL-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 41-136 IN COMPLEX WITH THE ACYL-COA ANALOGS COENZYME A AND STEARIC ACID.

Entry informationi

Entry nameiACBD5_HUMAN
AccessioniPrimary (citable) accession number: Q5T8D3
Secondary accession number(s): B3KQ56
, D3DRW0, Q5T8D4, Q5T8E1, Q5T8E2, Q86UV1, Q8N6E3, Q9UFB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: December 21, 2004
Last modified: November 26, 2014
This is version 91 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

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