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Protein

2-hydroxyacyl-CoA lyase 1

Gene

HACL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes a carbon-carbon cleavage reaction; cleaves a 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde.

Catalytic activityi

2-hydroxyphytanoyl-CoA = pristanal + formyl-CoA.

Cofactori

Protein has several cofactor binding sites:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601Thiamine pyrophosphateBy similarity
Metal bindingi455 – 4551MagnesiumBy similarity
Metal bindingi482 – 4821MagnesiumBy similarity

GO - Molecular functioni

  • carbon-carbon lyase activity Source: UniProtKB
  • cofactor binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • magnesium ion binding Source: InterPro
  • receptor binding Source: UniProtKB
  • thiamine pyrophosphate binding Source: UniProtKB

GO - Biological processi

  • cellular lipid metabolic process Source: Reactome
  • fatty acid alpha-oxidation Source: HGNC
  • protein oligomerization Source: UniProtKB
  • small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS05516-MONOMER.
ReactomeiREACT_17003. Alpha-oxidation of phytanate.
UniPathwayiUPA00199.

Names & Taxonomyi

Protein namesi
Recommended name:
2-hydroxyacyl-CoA lyase 1 (EC:4.1.-.-)
Alternative name(s):
2-hydroxyphytanoyl-CoA lyase
Short name:
2-HPCL
Phytanoyl-CoA 2-hydroxylase 2
Gene namesi
Name:HACL1
Synonyms:HPCL, HPCL2, PHYH2
ORF Names:HSPC279
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:17856. HACL1.

Subcellular locationi

GO - Cellular componenti

  • peroxisomal matrix Source: Reactome
  • peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671172.

Polymorphism and mutation databases

BioMutaiHACL1.
DMDMi20455027.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5785782-hydroxyacyl-CoA lyase 1PRO_0000090816Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei351 – 3511N6-succinyllysineBy similarity
Modified residuei358 – 3581N6-succinyllysineBy similarity
Modified residuei365 – 3651N6-succinyllysineBy similarity

Proteomic databases

MaxQBiQ9UJ83.
PaxDbiQ9UJ83.
PeptideAtlasiQ9UJ83.
PRIDEiQ9UJ83.

PTM databases

PhosphoSiteiQ9UJ83.

Expressioni

Tissue specificityi

Expressed in high levels in liver, also expressed in kidney, heart and skeletal muscle.1 Publication

Gene expression databases

BgeeiQ9UJ83.
CleanExiHS_HACL1.
ExpressionAtlasiQ9UJ83. baseline and differential.
GenevestigatoriQ9UJ83.

Organism-specific databases

HPAiHPA035496.
HPA035497.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-746580,EBI-746580
MAGEB6Q8N7X43EBI-746580,EBI-6447163
ZMYND19Q96E354EBI-746580,EBI-746595

Protein-protein interaction databases

BioGridi117523. 8 interactions.
IntActiQ9UJ83. 4 interactions.
MINTiMINT-1444467.
STRINGi9606.ENSP00000323811.

Structurei

3D structure databases

ProteinModelPortaliQ9UJ83.
SMRiQ9UJ83. Positions 12-563.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni401 – 48686Thiamine pyrophosphate bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi576 – 5783Microbody targeting signal

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

eggNOGiCOG0028.
GeneTreeiENSGT00530000063412.
HOGENOMiHOG000053808.
HOVERGENiHBG027302.
InParanoidiQ9UJ83.
KOiK12261.
OMAiMERCMSP.
OrthoDBiEOG741Z1P.
PhylomeDBiQ9UJ83.
TreeFamiTF105690.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UJ83-1) [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
MPDSNFAERS EEQVSGAKVI AQALKTQDVE YIFGIVGIPV TEIAIAAQQL
60 70 80 90 100
GIKYIGMRNE QAACYAASAI GYLTSRPGVC LVVSGPGLIH ALGGMANANM
110 120 130 140 150
NCWPLLVIGG SSERNQETMG AFQEFPQVEA CRLYTKFSAR PSSIEAIPFV
160 170 180 190 200
IEKAVRSSIY GRPGACYVDI PADFVNLQVN VNSIKYMERC MSPPISMAET
210 220 230 240 250
SAVCTAASVI RNAKQPLLII GKGAAYAHAE ESIKKLVEQY KLPFLPTPMG
260 270 280 290 300
KGVVPDNHPY CVGAARSRAL QFADVIVLFG ARLNWILHFG LPPRYQPDVK
310 320 330 340 350
FIQVDICAEE LGNNVKPAVT LLGNIHAVTK QLLEELDKTP WQYPPESKWW
360 370 380 390 400
KTLREKMKSN EAASKELASK KSLPMNYYTV FYHVQEQLPR DCFVVSEGAN
410 420 430 440 450
TMDIGRTVLQ NYLPRHRLDA GTFGTMGVGL GFAIAAAVVA KDRSPGQWII
460 470 480 490 500
CVEGDSAFGF SGMEVETICR YNLPIILLVV NNNGIYQGFD TDTWKEMLKF
510 520 530 540 550
QDATAVVPPM CLLPNSHYEQ VMTAFGGKGY FVQTPEELQK SLRQSLADTT
560 570
KPSLINIMIE PQATRKAQDF HWLTRSNM
Length:578
Mass (Da):63,729
Last modified:May 2, 2002 - v2
Checksum:iCF4F4B1A97025140
GO
Isoform 2 (identifier: Q9UJ83-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     77-103: Missing.

Note: No experimental confirmation available.

Show »
Length:551
Mass (Da):61,064
Checksum:iE4CCA8D486BE14FB
GO
Isoform 4 (identifier: Q9UJ83-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     128-153: Missing.
     332-365: Missing.

Show »
Length:518
Mass (Da):56,660
Checksum:iC8ED2E77A6246C04
GO
Isoform 3 (identifier: Q9UJ83-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     104-185: Missing.

Note: No experimental confirmation available.

Show »
Length:496
Mass (Da):54,724
Checksum:iBACFA0F55B8007A1
GO

Sequence cautioni

The sequence AAF28957.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti447 – 4471Q → H in CAB60200 (PubMed:10468558).Curated
Sequence conflicti543 – 5431R → E in CAB60200 (PubMed:10468558).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei77 – 10327Missing in isoform 2. 1 PublicationVSP_054191Add
BLAST
Alternative sequencei104 – 18582Missing in isoform 3. 1 PublicationVSP_054192Add
BLAST
Alternative sequencei128 – 15326Missing in isoform 4. CuratedVSP_054749Add
BLAST
Alternative sequencei332 – 36534Missing in isoform 4. CuratedVSP_054750Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ131753 mRNA. Translation: CAB60200.1.
AF161397 mRNA. Translation: AAF28957.1. Different initiation.
AK301546 mRNA. Translation: BAG63043.1.
AK301990 mRNA. Translation: BAG63397.1.
AC027129 Genomic DNA. No translation available.
BC001627 mRNA. Translation: AAH01627.1.
CCDSiCCDS2627.1. [Q9UJ83-1]
CCDS68360.1. [Q9UJ83-2]
CCDS68361.1. [Q9UJ83-3]
CCDS68362.1. [Q9UJ83-4]
RefSeqiNP_001271342.1. NM_001284413.1. [Q9UJ83-2]
NP_001271344.1. NM_001284415.1. [Q9UJ83-4]
NP_001271345.1. NM_001284416.1. [Q9UJ83-3]
NP_036392.2. NM_012260.3. [Q9UJ83-1]
UniGeneiHs.63290.

Genome annotation databases

EnsembliENST00000321169; ENSP00000323811; ENSG00000131373. [Q9UJ83-1]
ENST00000451445; ENSP00000403656; ENSG00000131373. [Q9UJ83-3]
ENST00000456194; ENSP00000390699; ENSG00000131373. [Q9UJ83-2]
ENST00000457447; ENSP00000404883; ENSG00000131373. [Q9UJ83-4]
GeneIDi26061.
KEGGihsa:26061.
UCSCiuc003caf.3. human. [Q9UJ83-1]
uc011avs.2. human.
uc011avu.2. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ131753 mRNA. Translation: CAB60200.1.
AF161397 mRNA. Translation: AAF28957.1. Different initiation.
AK301546 mRNA. Translation: BAG63043.1.
AK301990 mRNA. Translation: BAG63397.1.
AC027129 Genomic DNA. No translation available.
BC001627 mRNA. Translation: AAH01627.1.
CCDSiCCDS2627.1. [Q9UJ83-1]
CCDS68360.1. [Q9UJ83-2]
CCDS68361.1. [Q9UJ83-3]
CCDS68362.1. [Q9UJ83-4]
RefSeqiNP_001271342.1. NM_001284413.1. [Q9UJ83-2]
NP_001271344.1. NM_001284415.1. [Q9UJ83-4]
NP_001271345.1. NM_001284416.1. [Q9UJ83-3]
NP_036392.2. NM_012260.3. [Q9UJ83-1]
UniGeneiHs.63290.

3D structure databases

ProteinModelPortaliQ9UJ83.
SMRiQ9UJ83. Positions 12-563.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117523. 8 interactions.
IntActiQ9UJ83. 4 interactions.
MINTiMINT-1444467.
STRINGi9606.ENSP00000323811.

PTM databases

PhosphoSiteiQ9UJ83.

Polymorphism and mutation databases

BioMutaiHACL1.
DMDMi20455027.

Proteomic databases

MaxQBiQ9UJ83.
PaxDbiQ9UJ83.
PeptideAtlasiQ9UJ83.
PRIDEiQ9UJ83.

Protocols and materials databases

DNASUi26061.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321169; ENSP00000323811; ENSG00000131373. [Q9UJ83-1]
ENST00000451445; ENSP00000403656; ENSG00000131373. [Q9UJ83-3]
ENST00000456194; ENSP00000390699; ENSG00000131373. [Q9UJ83-2]
ENST00000457447; ENSP00000404883; ENSG00000131373. [Q9UJ83-4]
GeneIDi26061.
KEGGihsa:26061.
UCSCiuc003caf.3. human. [Q9UJ83-1]
uc011avs.2. human.
uc011avu.2. human.

Organism-specific databases

CTDi26061.
GeneCardsiGC03M015602.
HGNCiHGNC:17856. HACL1.
HPAiHPA035496.
HPA035497.
MIMi604300. gene.
neXtProtiNX_Q9UJ83.
PharmGKBiPA142671172.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0028.
GeneTreeiENSGT00530000063412.
HOGENOMiHOG000053808.
HOVERGENiHBG027302.
InParanoidiQ9UJ83.
KOiK12261.
OMAiMERCMSP.
OrthoDBiEOG741Z1P.
PhylomeDBiQ9UJ83.
TreeFamiTF105690.

Enzyme and pathway databases

UniPathwayiUPA00199.
BioCyciMetaCyc:HS05516-MONOMER.
ReactomeiREACT_17003. Alpha-oxidation of phytanate.

Miscellaneous databases

ChiTaRSiHACL1. human.
GenomeRNAii26061.
NextBioi35475725.
PROiQ9UJ83.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UJ83.
CleanExiHS_HACL1.
ExpressionAtlasiQ9UJ83. baseline and differential.
GenevestigatoriQ9UJ83.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Purification, molecular cloning, and expression of 2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine hydrophosphate-dependent enzyme that catalyzes the carbon-carbon bond cleavage during alpha-oxidation of 3-methyl-branched fatty acids."
    Foulon V., Antonenkov V.D., Croes K., Waelkens E., Mannaerts G.P., Van Veldhoven P.P., Casteels M.
    Proc. Natl. Acad. Sci. U.S.A. 96:10039-10044(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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.
    , 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).
    Tissue: Mammary gland and Testis.
  4. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    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 1).
    Tissue: Lung.
  6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHACL1_HUMAN
AccessioniPrimary (citable) accession number: Q9UJ83
Secondary accession number(s): B4DWI1
, B4DXI5, E9PEN4, Q9BV42, Q9P0A2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 2, 2002
Last modified: April 29, 2015
This is version 127 of the entry and version 2 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 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. 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.