Q5T8D3 (ACBD5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acyl-CoA-binding domain-containing protein 5

Gene names

Name:	ACBD5
Synonyms:	KIAA1996

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	534 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds medium- and long-chain acyl-CoA esters.
Subcellular location	Peroxisome membrane; Single-pass membrane protein By similarity.
Sequence similarities	Contains 1 ACB (acyl-CoA-binding) domain.
Sequence caution	The sequence AAH30555.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transport
Cellular component	Membrane Peroxisome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Transmembrane Transmembrane helix
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intracellular membrane-bounded organelle Inferred from direct assay. Source: HPA peroxisomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	fatty-acyl-CoA binding Inferred from electronic annotation. Source: InterPro lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q5T8D3-1)

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.

Isoform 2 (identifier: Q5T8D3-2)

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.

Isoform 3 (identifier: Q5T8D3-3)

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.

Isoform 4 (identifier: Q5T8D3-4)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 534

534

Acyl-CoA-binding domain-containing protein 5

PRO_0000287377

Regions

Transmembrane

506 – 526

21

Helical; Potential

Domain

41 – 130

90

ACB

Region

52 – 61

10

Acyl-CoA binding

Region

72 – 76

5

Acyl-CoA binding

Coiled coil

190 – 219

30

Potential

Coiled coil

447 – 476

30

Potential

Compositional bias

13 – 16

4

Poly-Cys

Compositional bias

201 – 204

4

Poly-Glu

Compositional bias

528 – 531

4

Poly-Arg

Sites

Binding site

98

1

Acyl-CoA

Binding site

117

1

Acyl-CoA By similarity

Amino acid modifications

Modified residue

160

1

Phosphothreonine By similarity

Modified residue

193

1

Phosphoserine Ref.9

Modified residue

194

1

Phosphoserine Ref.9

Modified residue

196

1

Phosphoserine Ref.9

Modified residue

200

1

Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10

Modified residue

400

1

Phosphothreonine Ref.8

Modified residue

428

1

Phosphoserine Ref.8

Modified residue

441

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 107

107

Missing in isoform 4.

VSP_025448

Alternative sequence

1 – 33

33

Missing in isoform 2.

VSP_025447

Alternative sequence

1 – 3

3

MFQ → MLFLS in isoform 3.

VSP_025446

Alternative sequence

162 – 172

11

Missing in isoform 2, isoform 3 and isoform 4.

VSP_025449

Natural variant

472

1

T → M.
Corresponds to variant rs7918793 [ dbSNP | Ensembl ].

VAR_032301

Experimental info

Sequence conflict

332

1

P → Q in AAP30852. Ref.1

Sequence conflict

419

1

E → D in AAP30852. Ref.1

Sequence conflict

478

1

A → T in AAP30852. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

534

Helix Strand Turn

Details...

Helix

41 – 58

18

Helix

65 – 79

15

Helix

93 – 104

12

Turn

105 – 107

3

Helix

110 – 127

18

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 8BE9A09967717653	FASTA	534	60,092
	10 20 30 40 50 60 MFQFHAGSWE SWCCCCLIPA DRPWDRGQHW QLEMADTRSV HETRFEAAVK VIQSLPKNGS 70 80 90 100 110 120 FQPTNEMMLK FYSFYKQATE GPCKLSRPGF WDPIGRYKWD AWSSLGDMTK EEAMIAYVEE 130 140 150 160 170 180 MKKIIETMPM TEKVEELLRV IGPFYEIVED KKSGRSSDIT SVRLEKISKC LEDLGNVLTS 190 200 210 220 230 240 TPNAKTVNGK AESSDSGAES EEEEAQEEVK GAEQSDNDKK MMKKSADHKN LEVIVTNGYD 250 260 270 280 290 300 KDGFVQDIQN DIHASSSLNG RSTEEVKPID ENLGQTGKSA VCIHQDINDD HVEDVTGIQH 310 320 330 340 350 360 LTSDSDSEVY CDSMEQFGQE ESLDSFTSNN GPFQYYLGGH SSQPMENSGF REDIQVPPGN 370 380 390 400 410 420 GNIGNMQVVA VEGKGEVKHG GEDGRNNSGA PHREKRGGET DEFSNVRRGR GHRMQHLSEG 430 440 450 460 470 480 TKGRQVGSGG DGERWGSDRG SRGSLNEQIA LVLMRLQEDM QNVLQRLQKL ETLTALQAKS 490 500 510 520 530 STSTLQTAPQ PTSQRPSWWP FEMSPGVLTF AIIWPFIAQW LVYLYYQRRR RKLN
	Isoform 2 [UniParc]. Checksum: 35B7F4B27ECE706B	FASTA	490	54,786
	10 20 30 40 50 60 MADTRSVHET RFEAAVKVIQ SLPKNGSFQP TNEMMLKFYS FYKQATEGPC KLSRPGFWDP 70 80 90 100 110 120 IGRYKWDAWS SLGDMTKEEA MIAYVEEMKK IIETMPMTEK VEELLRVIGP FYEIVEDKKS 130 140 150 160 170 180 GRSSDITSDL GNVLTSTPNA KTVNGKAESS DSGAESEEEE AQEEVKGAEQ SDNDKKMMKK 190 200 210 220 230 240 SADHKNLEVI VTNGYDKDGF VQDIQNDIHA SSSLNGRSTE EVKPIDENLG QTGKSAVCIH 250 260 270 280 290 300 QDINDDHVED VTGIQHLTSD SDSEVYCDSM EQFGQEESLD SFTSNNGPFQ YYLGGHSSQP 310 320 330 340 350 360 MENSGFREDI QVPPGNGNIG NMQVVAVEGK GEVKHGGEDG RNNSGAPHRE KRGGETDEFS 370 380 390 400 410 420 NVRRGRGHRM QHLSEGTKGR QVGSGGDGER WGSDRGSRGS LNEQIALVLM RLQEDMQNVL 430 440 450 460 470 480 QRLQKLETLT ALQAKSSTST LQTAPQPTSQ RPSWWPFEMS PGVLTFAIIW PFIAQWLVYL 490 YYQRRRRKLN
	Isoform 3 [UniParc]. Checksum: 95E2AD87B672D414	FASTA	525	58,978
	10 20 30 40 50 60 MLFLSFHAGS WESWCCCCLI PADRPWDRGQ HWQLEMADTR SVHETRFEAA VKVIQSLPKN 70 80 90 100 110 120 GSFQPTNEMM LKFYSFYKQA TEGPCKLSRP GFWDPIGRYK WDAWSSLGDM TKEEAMIAYV 130 140 150 160 170 180 EEMKKIIETM PMTEKVEELL RVIGPFYEIV EDKKSGRSSD ITSDLGNVLT STPNAKTVNG 190 200 210 220 230 240 KAESSDSGAE SEEEEAQEEV KGAEQSDNDK KMMKKSADHK NLEVIVTNGY DKDGFVQDIQ 250 260 270 280 290 300 NDIHASSSLN GRSTEEVKPI DENLGQTGKS AVCIHQDIND DHVEDVTGIQ HLTSDSDSEV 310 320 330 340 350 360 YCDSMEQFGQ EESLDSFTSN NGPFQYYLGG HSSQPMENSG FREDIQVPPG NGNIGNMQVV 370 380 390 400 410 420 AVEGKGEVKH GGEDGRNNSG APHREKRGGE TDEFSNVRRG RGHRMQHLSE GTKGRQVGSG 430 440 450 460 470 480 GDGERWGSDR GSRGSLNEQI ALVLMRLQED MQNVLQRLQK LETLTALQAK SSTSTLQTAP 490 500 510 520 QPTSQRPSWW PFEMSPGVLT FAIIWPFIAQ WLVYLYYQRR RRKLN
	Isoform 4 [UniParc]. Checksum: 2FD7CD93EAA41CC9	FASTA	416	46,268
	10 20 30 40 50 60 MTKEEAMIAY VEEMKKIIET MPMTEKVEEL LRVIGPFYEI VEDKKSGRSS DITSDLGNVL 70 80 90 100 110 120 TSTPNAKTVN GKAESSDSGA ESEEEEAQEE VKGAEQSDND KKMMKKSADH KNLEVIVTNG 130 140 150 160 170 180 YDKDGFVQDI QNDIHASSSL NGRSTEEVKP IDENLGQTGK SAVCIHQDIN DDHVEDVTGI 190 200 210 220 230 240 QHLTSDSDSE VYCDSMEQFG QEESLDSFTS NNGPFQYYLG GHSSQPMENS GFREDIQVPP 250 260 270 280 290 300 GNGNIGNMQV VAVEGKGEVK HGGEDGRNNS GAPHREKRGG ETDEFSNVRR GRGHRMQHLS 310 320 330 340 350 360 EGTKGRQVGS GGDGERWGSD RGSRGSLNEQ IALVLMRLQE DMQNVLQRLQ KLETLTALQA 370 380 390 400 410 KSSTSTLQTA PQPTSQRPSW WPFEMSPGVL TFAIIWPFIA QWLVYLYYQR RRRKLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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.
[3]	"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].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Blood.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 252-534. Tissue: Testis.
[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(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] 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), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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, MASS SPECTROMETRY. Tissue: Liver.
[11]	"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), MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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 COENZYME A AND STEARIC ACID.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00186681.
IPI00550377.
IPI00640010.
IPI00644427.

PIR

T42665.

RefSeq

NP_001035938.1. NM_001042473.2.
NP_663736.2. NM_145698.3.

UniGene

Hs.530597.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FLV	X-ray	1.70	A/B	41-136	[»]

ProteinModelPortal

Q5T8D3.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q5T8D3. 1 interaction.

STRING

9606.ENSP00000379568.

PTM databases

PhosphoSite

Q5T8D3.

Polymorphism databases

DMDM

74745508.

Proteomic databases

PaxDb

Q5T8D3.

PRIDE

Q5T8D3.

Protocols and materials databases

DNASU

91452.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000375888; ENSP00000365049; ENSG00000107897.
ENST00000375901; ENSP00000365066; ENSG00000107897.
ENST00000375905; ENSP00000365070; ENSG00000107897.
ENST00000396271; ENSP00000379568; ENSG00000107897.
ENST00000412279; ENSP00000393398; ENSG00000107897.

GeneID

91452.

KEGG

hsa:91452.

UCSC

uc001ito.3. human.
uc001itp.3. human.
uc001itr.1. human.
uc010qdp.2. human.

Organism-specific databases

CTD

91452.

GeneCards

GC10M027484.

HGNC

HGNC:23338. ACBD5.

HPA

HPA011861.
HPA012145.

neXtProt

NX_Q5T8D3.

PharmGKB

PA134892991.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG4281.

HOVERGEN

HBG106445.

OMA

GRGHRMQ.

Gene expression databases

ArrayExpress

Q5T8D3.

Bgee

Q5T8D3.

CleanEx

HS_ACBD5.

Genevestigator

Q5T8D3.

Family and domain databases

Gene3D

1.20.80.10. 1 hit.

InterPro

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]

Pfam

PF00887. ACBP. 1 hit.
[Graphical view]

PIRSF

PIRSF002412. MA_DBI. 1 hit.

PRINTS

PR00689. ACOABINDINGP.

SUPFAM

SSF47027. ACBP. 1 hit.

PROSITE

PS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ACBD5. human.

EvolutionaryTrace

Q5T8D3.

GenomeRNAi

91452.

NextBio

77259.

Entry information

Entry name

ACBD5_HUMAN

Accession

Primary (citable) accession number: Q5T8D3
Secondary accession number(s): B3KQ56 , D3DRW0, Q5T8D4, Q5T8E1, Q5T8E2, Q86UV1, Q8N6E3, Q9UFB5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	December 21, 2004
Last modified:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.