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Protein

Protein-cysteine N-palmitoyltransferase HHAT

Gene

Hhat

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes N-terminal palmitoylation of SHH; which is required for SHH signaling during limb development. May bind GTP.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei385 – 3851Sequence analysis

GO - Molecular functioni

  • GTP binding Source: UniProtKB-KW
  • palmitoyltransferase activity Source: MGI

GO - Biological processi

  • multicellular organism development Source: UniProtKB-KW
  • positive regulation of protein targeting to mitochondrion Source: MGI
  • protein palmitoylation Source: MGI
  • smoothened signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Developmental protein, Transferase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-5358346. Hedgehog ligand biogenesis.

Protein family/group databases

TCDBi2.A.50.1.3. the glycerol uptake (gup) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-cysteine N-palmitoyltransferase HHAT (EC:2.3.1.-)
Alternative name(s):
Hedgehog acyltransferase
Skinny hedgehog protein
Gene namesi
Name:Hhat
Synonyms:Skn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2444681. Hhat.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 55CytoplasmicSequence analysis
Transmembranei6 – 2217HelicalSequence analysisAdd
BLAST
Topological domaini23 – 6745LumenalSequence analysisAdd
BLAST
Transmembranei68 – 8417HelicalSequence analysisAdd
BLAST
Topological domaini85 – 9410CytoplasmicSequence analysis
Intramembranei95 – 11925Sequence analysisAdd
BLAST
Topological domaini120 – 13112CytoplasmicSequence analysisAdd
BLAST
Transmembranei132 – 14817HelicalSequence analysisAdd
BLAST
Topological domaini149 – 16214LumenalSequence analysisAdd
BLAST
Transmembranei163 – 18321HelicalSequence analysisAdd
BLAST
Topological domaini184 – 20825CytoplasmicSequence analysisAdd
BLAST
Intramembranei209 – 22315Sequence analysisAdd
BLAST
Topological domaini224 – 24926CytoplasmicSequence analysisAdd
BLAST
Transmembranei250 – 27728HelicalSequence analysisAdd
BLAST
Topological domaini278 – 28710LumenalSequence analysis
Transmembranei288 – 31629HelicalSequence analysisAdd
BLAST
Topological domaini317 – 36953CytoplasmicSequence analysisAdd
BLAST
Transmembranei370 – 38617HelicalSequence analysisAdd
BLAST
Topological domaini387 – 3893LumenalSequence analysis
Transmembranei390 – 40516HelicalSequence analysisAdd
BLAST
Topological domaini406 – 43328CytoplasmicSequence analysisAdd
BLAST
Transmembranei434 – 45421HelicalSequence analysisAdd
BLAST
Topological domaini455 – 46814LumenalSequence analysisAdd
BLAST
Transmembranei469 – 48719HelicalSequence analysisAdd
BLAST
Topological domaini488 – 49912CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are characterized by a smaller size and holoprosencephaly at E10.5, shortening of limbs at E13.5, and severe short-limb dwarfism at birth. They die soon after birth.1 Publication

Chemistry

ChEMBLiCHEMBL1255153.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Protein-cysteine N-palmitoyltransferase HHATPRO_0000213135Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi188 – 1881S-palmitoyl cysteineBy similarity
Lipidationi248 – 2481S-palmitoyl cysteineBy similarity
Lipidationi330 – 3301S-palmitoyl cysteineBy similarity
Lipidationi416 – 4161S-palmitoyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiQ8BMT9.
PRIDEiQ8BMT9.

PTM databases

PhosphoSiteiQ8BMT9.

Expressioni

Developmental stagei

Broadly expressed from E7. At E10.5, strongly expressed in anterior ectoderm, pharyngeal arches, and distal part of the limb.1 Publication

Gene expression databases

BgeeiQ8BMT9.
CleanExiMM_HHAT.
ExpressionAtlasiQ8BMT9. baseline and differential.
GenevisibleiQ8BMT9. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000046686.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni454 – 4618GTP-bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3860. Eukaryota.
COG1696. LUCA.
GeneTreeiENSGT00530000063629.
HOGENOMiHOG000015758.
HOVERGENiHBG106485.
InParanoidiQ8BMT9.
OrthoDBiEOG7JT6W2.
PhylomeDBiQ8BMT9.
TreeFamiTF315826.

Family and domain databases

InterProiIPR032981. HHAT.
IPR004299. MBOAT_fam.
[Graphical view]
PANTHERiPTHR13285:SF20. PTHR13285:SF20. 1 hit.
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BMT9-1) [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
MLPGWELTLC LLVSLGFHFR SFYEVYKVSR EHEEELDQEF ELEMDTLFGG
60 70 80 90 100
LKKDPTDFEW NFWMEWGKRR LVWLFIGHMA VSQLATLLTK KHRPWIVMVY
110 120 130 140 150
GMWACWCVLG APGVVMVLLH STIAFCVAQF RSVLLSWLCS LLLLSTLRLQ
160 170 180 190 200
SVEEVKRRWY KTENEYYLLQ FTLTVRCLYY TSFSLELCRQ PPSAQPTPSA
210 220 230 240 250
QGASHSYPWL LTYVFYYPVF HNGPILNFPE FFRQMQQPEL NSLQHSLCIV
260 270 280 290 300
AKGLGRLLCW WWLAELMVHL MYMHALYSSA PLLESVSCWT LGGLALAQVL
310 320 330 340 350
FFYVKYLVLF GVPALLMRLD GLTPPPLPRC VSTMFSFTGM WRYFDVGLHN
360 370 380 390 400
FLIRYVYIPL GGSQHGLLGT LLSTATTFAF VSYWHGSYED LWCWAALNWL
410 420 430 440 450
GVTVESGVRR LLETPCVRET LARHLSPQAH HRLHALLAAC STSMLILFNL
460 470 480 490
VFLGGIQVGK TYWNRIFLQG WPWVTLSVLG FLYCYSHVDI AWAQTYTVL
Length:499
Mass (Da):57,864
Last modified:March 1, 2003 - v1
Checksum:i37A3B98D607CE06C
GO
Isoform 2 (identifier: Q8BMT9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     470-473: GWPW → AAFR
     474-499: Missing.

Note: No experimental confirmation available.
Show »
Length:473
Mass (Da):54,837
Checksum:i5157633CAE39270B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti489 – 4891D → G in BAE42837 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei470 – 4734GWPW → AAFR in isoform 2. 1 PublicationVSP_016690
Alternative sequencei474 – 49926Missing in isoform 2. 1 PublicationVSP_016691Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028230 mRNA. Translation: BAC25829.1.
AK172126 mRNA. Translation: BAE42837.1.
AL365317, AC105325, AC115917 Genomic DNA. Translation: CAO82115.1.
BC008159 mRNA. Translation: AAH08159.1.
CCDSiCCDS15628.1. [Q8BMT9-1]
RefSeqiNP_659130.2. NM_144881.4. [Q8BMT9-1]
UniGeneiMm.145857.

Genome annotation databases

EnsembliENSMUST00000044190; ENSMUSP00000046686; ENSMUSG00000037375. [Q8BMT9-1]
ENSMUST00000128619; ENSMUSP00000120479; ENSMUSG00000037375. [Q8BMT9-2]
GeneIDi226861.
KEGGimmu:226861.
UCSCiuc007edp.2. mouse. [Q8BMT9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028230 mRNA. Translation: BAC25829.1.
AK172126 mRNA. Translation: BAE42837.1.
AL365317, AC105325, AC115917 Genomic DNA. Translation: CAO82115.1.
BC008159 mRNA. Translation: AAH08159.1.
CCDSiCCDS15628.1. [Q8BMT9-1]
RefSeqiNP_659130.2. NM_144881.4. [Q8BMT9-1]
UniGeneiMm.145857.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000046686.

Chemistry

ChEMBLiCHEMBL1255153.

Protein family/group databases

TCDBi2.A.50.1.3. the glycerol uptake (gup) family.

PTM databases

PhosphoSiteiQ8BMT9.

Proteomic databases

PaxDbiQ8BMT9.
PRIDEiQ8BMT9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000044190; ENSMUSP00000046686; ENSMUSG00000037375. [Q8BMT9-1]
ENSMUST00000128619; ENSMUSP00000120479; ENSMUSG00000037375. [Q8BMT9-2]
GeneIDi226861.
KEGGimmu:226861.
UCSCiuc007edp.2. mouse. [Q8BMT9-1]

Organism-specific databases

CTDi55733.
MGIiMGI:2444681. Hhat.

Phylogenomic databases

eggNOGiKOG3860. Eukaryota.
COG1696. LUCA.
GeneTreeiENSGT00530000063629.
HOGENOMiHOG000015758.
HOVERGENiHBG106485.
InParanoidiQ8BMT9.
OrthoDBiEOG7JT6W2.
PhylomeDBiQ8BMT9.
TreeFamiTF315826.

Enzyme and pathway databases

ReactomeiR-MMU-5358346. Hedgehog ligand biogenesis.

Miscellaneous databases

PROiQ8BMT9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BMT9.
CleanExiMM_HHAT.
ExpressionAtlasiQ8BMT9. baseline and differential.
GenevisibleiQ8BMT9. MM.

Family and domain databases

InterProiIPR032981. HHAT.
IPR004299. MBOAT_fam.
[Graphical view]
PANTHERiPTHR13285:SF20. PTHR13285:SF20. 1 hit.
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J and NOD.
    Tissue: Embryo and Spleen.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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 2).
    Strain: FVB/N.
    Tissue: Mammary gland.
  4. "Palmitoylation is required for the production of a soluble multimeric Hedgehog protein complex and long-range signaling in vertebrates."
    Chen M.-H., Li Y.-J., Kawakami T., Xu S.-M., Chuang P.-T.
    Genes Dev. 18:641-659(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  5. "Mammalian Gup1, a homolog of Saccharomyces cerevisiae glycerol uptake/transporter 1, acts as a negative regulator for N-terminal palmitoylation of Sonic hedgehog."
    Abe Y., Kita Y., Niikura T.
    FEBS J. 275:318-331(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiHHAT_MOUSE
AccessioniPrimary (citable) accession number: Q8BMT9
Secondary accession number(s): B1ANS0, Q3TA33, Q922G3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.