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Protein

Histidine ammonia-lyase

Gene

Hal

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-histidine = urocanate + NH3.PROSITE-ProRule annotation

Pathwayi

GO - Molecular functioni

  1. histidine ammonia-lyase activity Source: MGI

GO - Biological processi

  1. biosynthetic process Source: InterPro
  2. histidine catabolic process Source: MGI
  3. histidine catabolic process to glutamate and formamide Source: UniProtKB-UniPathway
  4. histidine catabolic process to glutamate and formate Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Histidine metabolism

Enzyme and pathway databases

ReactomeiREACT_292978. Histidine catabolism.
UniPathwayiUPA00379; UER00549.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine ammonia-lyase (EC:4.3.1.3)
Short name:
Histidase
Gene namesi
Name:Hal
Synonyms:Hsd, Huth
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:96010. Hal.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Defects in Hal are the cause of histidinemia (His).

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 657657Histidine ammonia-lyasePRO_0000161059Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki253 ↔ 2555-imidazolinone (Ala-Gly)By similarity
Modified residuei254 – 25412,3-didehydroalanine (Ser)PROSITE-ProRule annotation
Modified residuei396 – 3961Phosphothreonine1 Publication
Modified residuei648 – 6481Phosphoserine1 Publication

Post-translational modificationi

Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP35492.
PaxDbiP35492.
PRIDEiP35492.

PTM databases

PhosphoSiteiP35492.

Expressioni

Gene expression databases

BgeeiP35492.
CleanExiMM_HAL.
ExpressionAtlasiP35492. baseline and differential.
GenevestigatoriP35492.

Interactioni

Protein-protein interaction databases

BioGridi200203. 1 interaction.
MINTiMINT-1856476.

Structurei

3D structure databases

ProteinModelPortaliP35492.
SMRiP35492. Positions 114-607.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PAL/histidase family.Curated

Phylogenomic databases

eggNOGiCOG2986.
GeneTreeiENSGT00390000009047.
HOVERGENiHBG004509.
InParanoidiP35492.
KOiK01745.
OMAiCFLVRRC.
OrthoDBiEOG73RB9V.
PhylomeDBiP35492.
TreeFamiTF313824.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR001106. Aromatic_Lyase.
IPR024083. Fumarase/histidase_N.
IPR005921. HutH.
IPR008948. L-Aspartase-like.
IPR022313. Phe/His_NH3-lyase_AS.
[Graphical view]
PfamiPF00221. Lyase_aromatic. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR01225. hutH. 1 hit.
PROSITEiPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35492-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRYTVHVRG EWLAVPCQDG KLTVGWLGRE AVRRYMKNKP DNGGFTSVDE
60 70 80 90 100
VQFLVHRCKG LGLLDNEDEL EVALEDNEFV EVVIEGDVMS PDFIPSQPEG
110 120 130 140 150
VFLYSKYREP EKYIALDGDS LSTEDLVNLG KGRYKIKLTS IAEKKVQQSR
160 170 180 190 200
EVIDSIIKER TVVYGITTGF GKFARTVIPA NKLQELQVNL VRSHSSGVGK
210 220 230 240 250
PLSPERCRML LALRINVLAK GYSGISLETL KQVIEAFNAS CLSYVPEKGT
260 270 280 290 300
VGASGDLAPL SHLALGLIGE GKMWSPKSGW ADAKYVLEAH GLKPIVLKPK
310 320 330 340 350
EGLALINGTQ MITSLGCEAL ERASAIARQA DIVAALTLEV LKGTTKAFDT
360 370 380 390 400
DIHAVRPHRG QIEVAFRFRS LLDSDHHPSE IAESHRFCDR VQDAYTLRCC
410 420 430 440 450
PQVHGVVNDT IAFVKDIITT ELNSATDNPM VFASRGETIS GGNFHGEYPA
460 470 480 490 500
KALDYLAIGV HELAAISERR IERLCNPSLS ELPAFLVAEG GLNSGFMIAH
510 520 530 540 550
CTAAALVSES KALCHPSSVD SLSTSAATED HVSMGGWAAR KALRVVEHVE
560 570 580 590 600
QVLAIELLAA CQGIEFLRPL KTTTPLEKVY DLVRSVVRPW IKDRFMAPDI
610 620 630 640 650
EAAHRLLLDQ KVWEVAAPYI EKYRMEHIPE SRPLSPTAFS LESLRKNSAT

IPESDDL
Length:657
Mass (Da):72,258
Last modified:June 1, 1994 - v1
Checksum:i03402C348686C22D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti322 – 3221R → Q in His; reduced stability. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07645 mRNA. Translation: AAA37777.1.
AK014518 mRNA. Translation: BAB29407.1.
BC057637 mRNA. Translation: AAH57637.1.
CCDSiCCDS36036.1.
PIRiA46128.
RefSeqiNP_034531.1. NM_010401.3.
UniGeneiMm.13000.

Genome annotation databases

EnsembliENSMUST00000129421; ENSMUSP00000123336; ENSMUSG00000020017.
GeneIDi15109.
KEGGimmu:15109.
UCSCiuc007gus.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07645 mRNA. Translation: AAA37777.1.
AK014518 mRNA. Translation: BAB29407.1.
BC057637 mRNA. Translation: AAH57637.1.
CCDSiCCDS36036.1.
PIRiA46128.
RefSeqiNP_034531.1. NM_010401.3.
UniGeneiMm.13000.

3D structure databases

ProteinModelPortaliP35492.
SMRiP35492. Positions 114-607.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200203. 1 interaction.
MINTiMINT-1856476.

PTM databases

PhosphoSiteiP35492.

Proteomic databases

MaxQBiP35492.
PaxDbiP35492.
PRIDEiP35492.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000129421; ENSMUSP00000123336; ENSMUSG00000020017.
GeneIDi15109.
KEGGimmu:15109.
UCSCiuc007gus.1. mouse.

Organism-specific databases

CTDi3034.
MGIiMGI:96010. Hal.

Phylogenomic databases

eggNOGiCOG2986.
GeneTreeiENSGT00390000009047.
HOVERGENiHBG004509.
InParanoidiP35492.
KOiK01745.
OMAiCFLVRRC.
OrthoDBiEOG73RB9V.
PhylomeDBiP35492.
TreeFamiTF313824.

Enzyme and pathway databases

UniPathwayiUPA00379; UER00549.
ReactomeiREACT_292978. Histidine catabolism.

Miscellaneous databases

NextBioi287506.
PROiP35492.
SOURCEiSearch...

Gene expression databases

BgeeiP35492.
CleanExiMM_HAL.
ExpressionAtlasiP35492. baseline and differential.
GenevestigatoriP35492.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR001106. Aromatic_Lyase.
IPR024083. Fumarase/histidase_N.
IPR005921. HutH.
IPR008948. L-Aspartase-like.
IPR022313. Phe/His_NH3-lyase_AS.
[Graphical view]
PfamiPF00221. Lyase_aromatic. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR01225. hutH. 1 hit.
PROSITEiPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the mutation in murine histidinemia (his) and genetic mapping of the murine histidase locus (Hal) on chromosome 10."
    Taylor R.G., Grieco D., Clarke G.A., McInnes R.R., Taylor B.A.
    Genomics 16:231-240(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS GLN-322.
    Strain: C57BL/6J.
    Tissue: Liver.
  2. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Skin.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-396 AND SER-648, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHUTH_MOUSE
AccessioniPrimary (citable) accession number: P35492
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 1, 2015
This is version 123 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.