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P42357

- HUTH_HUMAN

UniProt

P42357 - HUTH_HUMAN

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Protein

Histidine ammonia-lyase

Gene

HAL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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: UniProtKB-EC

GO - Biological processi

  1. biosynthetic process Source: InterPro
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. histidine catabolic process Source: Reactome
  4. histidine catabolic process to glutamate and formamide Source: UniProtKB-UniPathway
  5. histidine catabolic process to glutamate and formate Source: UniProtKB-UniPathway
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Histidine metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS01466-MONOMER.
ReactomeiREACT_1249. 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:HIS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:4806. HAL.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Histidinemia (HISTID) [MIM:235800]: Autosomal recessive disease characterized by increased histidine and histamine as well as decreased urocanic acid in body fluids.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti206 – 2061R → T in HISTID. 1 Publication
VAR_022915
Natural varianti208 – 2081R → L in HISTID. 1 Publication
VAR_022916
Natural varianti259 – 2591P → L in HISTID. 1 Publication
VAR_022917
Natural varianti322 – 3221R → P in HISTID. 1 Publication
VAR_022918

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi235800. phenotype.
Orphaneti2157. Histidinemia.
PharmGKBiPA29181.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 657657Histidine ammonia-lyasePRO_0000161058Add
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 – 3961PhosphothreonineBy similarity
Modified residuei648 – 6481PhosphoserineBy similarity

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

MaxQBiP42357.
PaxDbiP42357.
PRIDEiP42357.

PTM databases

PhosphoSiteiP42357.

Expressioni

Gene expression databases

BgeeiP42357.
CleanExiHS_HAL.
ExpressionAtlasiP42357. baseline and differential.
GenevestigatoriP42357.

Organism-specific databases

HPAiHPA038547.
HPA038548.

Interactioni

Protein-protein interaction databases

BioGridi109284. 16 interactions.
STRINGi9606.ENSP00000261208.

Structurei

3D structure databases

ProteinModelPortaliP42357.
SMRiP42357. Positions 121-648.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PAL/histidase family.Curated

Phylogenomic databases

eggNOGiCOG2986.
GeneTreeiENSGT00390000009047.
HOGENOMiHOG000237619.
HOVERGENiHBG004509.
InParanoidiP42357.
KOiK01745.
OMAiVHIRDEW.
OrthoDBiEOG73RB9V.
PhylomeDBiP42357.
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P42357-1) [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
MPRYTVHVRG EWLAVPCQDA QLTVGWLGRE AVRRYIKNKP DNGGFTSVDD
60 70 80 90 100
AHFLVRRCKG LGLLDNEDRL EVALENNEFV EVVIEGDAMS PDFIPSQPEG
110 120 130 140 150
VYLYSKYREP EKYIELDGDR LTTEDLVNLG KGRYKIKLTP TAEKRVQKSR
160 170 180 190 200
EVIDSIIKEK TVVYGITTGF GKFARTVIPI NKLQELQVNL VRSHSSGVGK
210 220 230 240 250
PLSPERCRML LALRINVLAK GYSGISLETL KQVIEMFNAS CLPYVPEKGT
260 270 280 290 300
VGASGDLAPL SHLALGLVGE GKMWSPKSGW ADAKYVLEAH GLKPVILKPK
310 320 330 340 350
EGLALINGTQ MITSLGCEAV ERASAIARQA DIVAALTLEV LKGTTKAFDT
360 370 380 390 400
DIHALRPHRG QIEVAFRFRS LLDSDHHPSE IAESHRFCDR VQDAYTLRCC
410 420 430 440 450
PQVHGVVNDT IAFVKNIITT ELNSATDNPM VFANRGETVS GGNFHGEYPA
460 470 480 490 500
KALDYLAIGI HELAAISERR IERLCNPSLS ELPAFLVAEG GLNSGFMIAH
510 520 530 540 550
CTAAALVSEN KALCHPSSVD SLSTSAATED HVSMGGWAAR KALRVIEHVE
560 570 580 590 600
QVLAIELLAA CQGIEFLRPL KTTTPLEKVY DLVRSVVRPW IKDRFMAPDI
610 620 630 640 650
EAAHRLLLEQ KVWEVAAPYI EKYRMEHIPE SRPLSPTAFS LQFLHKKSTK

IPESEDL
Length:657
Mass (Da):72,698
Last modified:November 1, 1995 - v1
Checksum:i6B9FF97C066FB8F1
GO
Isoform 2 (identifier: P42357-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     589-657: PWIKDRFMAPDIEAAHRLLLEQKVWEVAAPYIEKYRMEHIPESRPLSPTAFSLQFLHKKSTKIPESEDL → FGK

Note: No experimental confirmation available.

Show »
Length:591
Mass (Da):64,888
Checksum:iDEBBCF642F5BC7DB
GO
Isoform 3 (identifier: P42357-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-208: Missing.

Note: No experimental confirmation available.

Show »
Length:449
Mass (Da):49,123
Checksum:iDD7DB9B250E4AFDA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti549 – 5491V → M in BAG64570. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti206 – 2061R → T in HISTID. 1 Publication
VAR_022915
Natural varianti208 – 2081R → L in HISTID. 1 Publication
VAR_022916
Natural varianti259 – 2591P → L in HISTID. 1 Publication
VAR_022917
Natural varianti322 – 3221R → P in HISTID. 1 Publication
VAR_022918
Natural varianti439 – 4391V → I.4 Publications
Corresponds to variant rs7297245 [ dbSNP | Ensembl ].
VAR_006042

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 208208Missing in isoform 3. 1 PublicationVSP_046003Add
BLAST
Alternative sequencei589 – 65769PWIKD…ESEDL → FGK in isoform 2. 1 PublicationVSP_044704Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D16626 mRNA. Translation: BAA04047.1.
AB042217 Genomic DNA. Translation: BAB61863.1.
AK298736 mRNA. Translation: BAG60883.1.
AK303544 mRNA. Translation: BAG64570.1.
AC007298 Genomic DNA. No translation available.
AC126174 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97556.1.
BC096097 mRNA. Translation: AAH96097.1.
BC096098 mRNA. Translation: AAH96098.1.
BC096099 mRNA. Translation: AAH96099.1.
CCDSiCCDS58264.1. [P42357-3]
CCDS58265.1. [P42357-2]
CCDS9058.1. [P42357-1]
PIRiS43415.
RefSeqiNP_001245262.1. NM_001258333.1. [P42357-3]
NP_001245263.1. NM_001258334.1. [P42357-2]
NP_002099.1. NM_002108.3. [P42357-1]
UniGeneiHs.190783.
Hs.742210.

Genome annotation databases

EnsembliENST00000261208; ENSP00000261208; ENSG00000084110. [P42357-1]
ENST00000538703; ENSP00000440861; ENSG00000084110. [P42357-2]
ENST00000541929; ENSP00000446364; ENSG00000084110. [P42357-3]
GeneIDi3034.
KEGGihsa:3034.
UCSCiuc001tem.2. human. [P42357-1]

Polymorphism databases

DMDMi1170423.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D16626 mRNA. Translation: BAA04047.1 .
AB042217 Genomic DNA. Translation: BAB61863.1 .
AK298736 mRNA. Translation: BAG60883.1 .
AK303544 mRNA. Translation: BAG64570.1 .
AC007298 Genomic DNA. No translation available.
AC126174 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97556.1 .
BC096097 mRNA. Translation: AAH96097.1 .
BC096098 mRNA. Translation: AAH96098.1 .
BC096099 mRNA. Translation: AAH96099.1 .
CCDSi CCDS58264.1. [P42357-3 ]
CCDS58265.1. [P42357-2 ]
CCDS9058.1. [P42357-1 ]
PIRi S43415.
RefSeqi NP_001245262.1. NM_001258333.1. [P42357-3 ]
NP_001245263.1. NM_001258334.1. [P42357-2 ]
NP_002099.1. NM_002108.3. [P42357-1 ]
UniGenei Hs.190783.
Hs.742210.

3D structure databases

ProteinModelPortali P42357.
SMRi P42357. Positions 121-648.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109284. 16 interactions.
STRINGi 9606.ENSP00000261208.

Chemistry

ChEMBLi CHEMBL4003.
DrugBanki DB00117. L-Histidine.

PTM databases

PhosphoSitei P42357.

Polymorphism databases

DMDMi 1170423.

Proteomic databases

MaxQBi P42357.
PaxDbi P42357.
PRIDEi P42357.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261208 ; ENSP00000261208 ; ENSG00000084110 . [P42357-1 ]
ENST00000538703 ; ENSP00000440861 ; ENSG00000084110 . [P42357-2 ]
ENST00000541929 ; ENSP00000446364 ; ENSG00000084110 . [P42357-3 ]
GeneIDi 3034.
KEGGi hsa:3034.
UCSCi uc001tem.2. human. [P42357-1 ]

Organism-specific databases

CTDi 3034.
GeneCardsi GC12M096366.
HGNCi HGNC:4806. HAL.
HPAi HPA038547.
HPA038548.
MIMi 235800. phenotype.
609457. gene.
neXtProti NX_P42357.
Orphaneti 2157. Histidinemia.
PharmGKBi PA29181.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2986.
GeneTreei ENSGT00390000009047.
HOGENOMi HOG000237619.
HOVERGENi HBG004509.
InParanoidi P42357.
KOi K01745.
OMAi VHIRDEW.
OrthoDBi EOG73RB9V.
PhylomeDBi P42357.
TreeFami TF313824.

Enzyme and pathway databases

UniPathwayi UPA00379 ; UER00549 .
BioCyci MetaCyc:HS01466-MONOMER.
Reactomei REACT_1249. Histidine catabolism.

Miscellaneous databases

GeneWikii Histidine_ammonia-lyase.
GenomeRNAii 3034.
NextBioi 12010.
PROi P42357.
SOURCEi Search...

Gene expression databases

Bgeei P42357.
CleanExi HS_HAL.
ExpressionAtlasi P42357. baseline and differential.
Genevestigatori P42357.

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
InterProi IPR001106. Aromatic_Lyase.
IPR024083. Fumarase/histidase_N.
IPR005921. HutH.
IPR008948. L-Aspartase-like.
IPR022313. Phe/His_NH3-lyase_AS.
[Graphical view ]
Pfami PF00221. Lyase_aromatic. 1 hit.
[Graphical view ]
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR01225. hutH. 1 hit.
PROSITEi PS00488. PAL_HISTIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a cDNA encoding human histidase."
    Suchi M., Harada N., Wada Y., Takagi Y.
    Biochim. Biophys. Acta 1216:293-295(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "Molecular cloning and structural characterization of the human histidase gene (HAL)."
    Suchi M., Sano H., Mizuno H., Wada Y.
    Genomics 29:98-104(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-439.
  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] (ISOFORMS 2 AND 3), VARIANT ILE-439.
    Tissue: Thymus.
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ILE-439.
  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 1), VARIANT ILE-439.
  7. "Molecular characterization of histidinemia: identification of four missense mutations in the histidase gene."
    Kawai Y., Moriyama A., Asai K., Coleman-Campbell C.M., Sumi S., Morishita H., Suchi M.
    Hum. Genet. 116:340-346(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HISTID THR-206; LEU-208; LEU-259 AND PRO-322.

Entry informationi

Entry nameiHUTH_HUMAN
AccessioniPrimary (citable) accession number: P42357
Secondary accession number(s): B4DQC1
, B4E0V8, F5GXF2, F5H1U5, Q4VB92, Q4VB93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 138 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3