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Q9P035 (HACD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3

EC=4.2.1.134
Alternative name(s):
3-hydroxyacyl-CoA dehydratase 3
Short name=HACD3
Butyrate-induced protein 1
Short name=B-ind1
Short name=hB-ind1
Protein tyrosine phosphatase-like protein PTPLAD1
Protein-tyrosine phosphatase-like A domain-containing protein 1
Gene names
Name:PTPLAD1
Synonyms:BIND1, HACD3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for the dehydration step in very long-chain fatty acid (VLCFA) synthesis. Involved in Rac1-signaling pathways leading to the modulation of gene expression. Ref.1 Ref.8

Catalytic activity

A very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain trans-2,3-dehydroacyl-CoA + H2O. Ref.8

Subunit structure

Interacts with the condensation enzymes of the ELOVL family. Interacts with RAC1. Ref.1 Ref.8

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.8.

Tissue specificity

Highly expressed in testis, kidney, brain, liver and weakly in skeletal muscle, spleen and heart. No expression detected in leukocytes. Ref.1 Ref.8

Induction

By AKAP12 and histone deacetylase inhibitors such as sodium butyrate. Ref.6

Sequence similarities

Belongs to the very long-chain fatty acids dehydratase HACD family.

Contains 1 CS domain.

Sequence caution

The sequence AAF29085.1 differs from that shown. Reason: Frameshift at position 356.

The sequence BAC11249.1 differs from that shown. Reason: Frameshift at position 359.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q034632EBI-359013,EBI-8803426From a different organism.
Q99IB82EBI-359013,EBI-6927873From a different organism.
Q9WMX23EBI-359013,EBI-6863748From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 362362Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3
PRO_0000313724

Regions

Topological domain1 – 149149Cytoplasmic Potential
Transmembrane150 – 17021Helical; Potential
Topological domain171 – 18515Lumenal Potential
Transmembrane186 – 20722Helical; Potential
Topological domain208 – 21710Cytoplasmic Potential
Transmembrane218 – 23518Helical; Potential
Topological domain236 – 2416Lumenal Potential
Transmembrane242 – 25615Helical; Potential
Topological domain257 – 27923Cytoplasmic Potential
Transmembrane280 – 29819Helical; Potential
Topological domain299 – 32224Lumenal Potential
Transmembrane323 – 34321Helical; Potential
Topological domain344 – 36219Cytoplasmic Potential
Domain5 – 9490CS
Coiled coil111 – 13626 Potential
Compositional bias350 – 3534Poly-Arg
Compositional bias357 – 3604Poly-Lys

Sites

Active site2861 By similarity
Active site2931 By similarity

Amino acid modifications

Modified residue1141Phosphoserine Ref.7 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17

Natural variations

Natural variant561E → K.
Corresponds to variant rs11632737 [ dbSNP | Ensembl ].
VAR_037712
Natural variant2691M → L.
Corresponds to variant rs2279854 [ dbSNP | Ensembl ].
VAR_037713

Experimental info

Sequence conflict601E → K in BAB55101. Ref.3
Sequence conflict2451F → I in BAC11277. Ref.3
Sequence conflict2821W → G in AAH35508. Ref.4
Sequence conflict2921A → V in AAF29085. Ref.2
Sequence conflict352 – 36211RRYGQKKKKIH → LKMRAGAVAHACDPSALGG in CAB69070. Ref.1
Sequence conflict3611I → K in AAH35508. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9P035 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: 1B3591E88DD85D16

FASTA36243,160
        10         20         30         40         50         60 
MENQVLTPHV YWAQRHRELY LRVELSDVQN PAISITENVL HFKAQGHGAK GDNVYEFHLE 

        70         80         90        100        110        120 
FLDLVKPEPV YKLTQRQVNI TVQKKVSQWW ERLTKQEKRP LFLAPDFDRW LDESDAEMEL 

       130        140        150        160        170        180 
RAKEEERLNK LRLESEGSPE TLTNLRKGYL FMYNLVQFLG FSWIFVNLTV RFCILGKESF 

       190        200        210        220        230        240 
YDTFHTVADM MYFCQMLAVV ETINAAIGVT TSPVLPSLIQ LLGRNFILFI IFGTMEEMQN 

       250        260        270        280        290        300 
KAVVFFVFYL WSAIEIFRYS FYMLTCIDMD WKVLTWLRYT LWIPLYPLGC LAEAVSVIQS 

       310        320        330        340        350        360 
IPIFNETGRF SFTLPYPVKI KVRFSFFLQI YLIMIFLGLY INFRHLYKQR RRRYGQKKKK 


IH 

« Hide

References

« Hide 'large scale' references
[1]"B-ind1, a novel mediator of Rac1 signaling cloned from sodium butyrate-treated fibroblasts."
Courilleau D., Chastre E., Sabbah M., Redeuilh G., Atfi A., Mester J.
J. Biol. Chem. 275:17344-17348(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RAC1, TISSUE SPECIFICITY.
[2]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Umbilical cord blood.
[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. expand/collapse author list , 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].
[4]"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].
Tissue: B-cell, Duodenum, Eye and Urinary bladder.
[5]"Human B-ind1 gene promoter: cloning and regulation by histone deacetylase inhibitors."
Sabbah M., Saucier C., Redeuilh G.
Gene 374:128-133(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
[6]"SSeCKS/Gravin/AKAP12 attenuates expression of proliferative and angiogenic genes during suppression of v-Src-induced oncogenesis."
Liu Y., Gao L., Gelman I.H.
BMC Cancer 6:105-105(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY AKAP12.
[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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases involved in very long-chain fatty acid synthesis."
Ikeda M., Kanao Y., Yamanaka M., Sakuraba H., Mizutani Y., Igarashi Y., Kihara A.
FEBS Lett. 582:2435-2440(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INTERACTION WITH ELOVL FAMILY.
[9]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ271091 mRNA. Translation: CAB69070.1.
AF161470 mRNA. Translation: AAF29085.1. Frameshift.
AK027421 mRNA. Translation: BAB55101.1.
AK074857 mRNA. Translation: BAC11249.1. Frameshift.
AK074898 mRNA. Translation: BAC11277.1.
BC019873 mRNA. Translation: AAH19873.1.
BC035508 mRNA. Translation: AAH35508.1.
BC047685 mRNA. Translation: AAH47685.1.
BC058912 mRNA. Translation: AAH58912.1.
DQ251107 Genomic DNA. Translation: ABB83547.1.
CCDSCCDS45282.1.
RefSeqNP_057479.2. NM_016395.2.
UniGeneHs.512973.

3D structure databases

ProteinModelPortalQ9P035.
SMRQ9P035. Positions 5-158.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119570. 27 interactions.
IntActQ9P035. 20 interactions.
MINTMINT-1135933.

PTM databases

PhosphoSiteQ9P035.

Polymorphism databases

DMDM166199462.

Proteomic databases

MaxQBQ9P035.
PaxDbQ9P035.
PRIDEQ9P035.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261875; ENSP00000261875; ENSG00000074696.
GeneID51495.
KEGGhsa:51495.
UCSCuc002apc.3. human.

Organism-specific databases

CTD51495.
GeneCardsGC15P065822.
H-InvDBHIX0012353.
HGNCHGNC:24175. PTPLAD1.
HPAHPA014837.
neXtProtNX_Q9P035.
PharmGKBPA142671113.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5198.
HOVERGENHBG108301.
InParanoidQ9P035.
OrthoDBEOG7BP82H.
PhylomeDBQ9P035.
TreeFamTF313326.

Gene expression databases

ArrayExpressQ9P035.
BgeeQ9P035.
CleanExHS_PTPLAD1.
GenevestigatorQ9P035.

Family and domain databases

Gene3D2.60.40.790. 1 hit.
InterProIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR007482. Tyr_Pase-like_PTPLA.
[Graphical view]
PANTHERPTHR11035. PTHR11035. 1 hit.
PfamPF04969. CS. 1 hit.
PF04387. PTPLA. 1 hit.
[Graphical view]
SUPFAMSSF49764. SSF49764. 1 hit.
PROSITEPS51203. CS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPLAD1. human.
GeneWikiPTPLAD1.
GenomeRNAi51495.
NextBio55161.
PROQ9P035.

Entry information

Entry nameHACD3_HUMAN
AccessionPrimary (citable) accession number: Q9P035
Secondary accession number(s): A0PJA1 expand/collapse secondary AC list , Q280Z3, Q6PD63, Q8IUI5, Q8NC86, Q8NCB1, Q96T12, Q9NQA7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: July 9, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM