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Protein

Succinate--hydroxymethylglutarate CoA-transferase

Gene

SUGCT

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

Functioni

Catalyzes the succinyl-CoA-dependent conversion of glutarate to glutaryl-CoA. Can use different dicarboxylic acids as CoA acceptors, the preferred ones are glutarate, succinate, adipate, and 3-hydroxymethylglutarate.1 Publication

Catalytic activityi

Succinyl-CoA + 3-hydroxy-3-methylglutarate = succinate + (S)-3-hydroxy-3-methylglutaryl-CoA.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei212 – 2121NucleophileBy similarity

GO - Molecular functioni

  • succinate-hydroxymethylglutarate CoA-transferase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000175600-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate--hydroxymethylglutarate CoA-transferase (EC:2.8.3.13)
Alternative name(s):
Dermal papilla-derived protein 13
SuccinylCoA:glutarate-CoA transferase
Gene namesi
Name:SUGCT
Synonyms:C7orf10, DERP13
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:16001. SUGCT.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Glutaric aciduria 3 (GA3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA metabolic disorder due to peroxisomal glutaryl-CoA oxidase deficiency and characterized by the excretion of abnormal quantities of glutaric acid but low 3-hydroxyglutaric acid.
See also OMIM:231690
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti336 – 3361R → W in GA3; inactive enzyme; healthy individuals who have abnormal quantities of glutaric acid but low 3-hydroxyglutaric acid. 2 Publications
Corresponds to variant rs137852860 [ dbSNP | Ensembl ].
VAR_054852

Keywords - Diseasei

Disease mutation, Glutaricaciduria

Organism-specific databases

MalaCardsiSUGCT.
MIMi231690. phenotype.
Orphaneti35706. Glutaric acidemia type 3.
PharmGKBiPA25942.

Polymorphism and mutation databases

BioMutaiC7orf10.
DMDMi71152390.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3838MitochondrionSequence analysisAdd
BLAST
Chaini39 – 445407Succinate--hydroxymethylglutarate CoA-transferasePRO_0000194726Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei401 – 4011N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9HAC7.
PRIDEiQ9HAC7.

PTM databases

iPTMnetiQ9HAC7.
PhosphoSiteiQ9HAC7.

Expressioni

Tissue specificityi

Highly expressed in kidney. Intermediate expression in liver, skeletal muscle and pancreas. Little to no expression detected in other tissues examined.1 Publication

Gene expression databases

BgeeiQ9HAC7.
CleanExiHS_C7orf10.
ExpressionAtlasiQ9HAC7. baseline and differential.
GenevisibleiQ9HAC7. HS.

Organism-specific databases

HPAiHPA026698.
HPA026704.
HPA026705.

Interactioni

Protein-protein interaction databases

BioGridi122883. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9HAC7.
SMRiQ9HAC7. Positions 42-438.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CaiB/BaiF CoA-transferase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00530000063418.
HOGENOMiHOG000219745.
HOVERGENiHBG102620.
InParanoidiQ9HAC7.
KOiK18703.
OMAiTIQIRIE.
OrthoDBiEOG7WDN2T.
PhylomeDBiQ9HAC7.
TreeFamiTF314188.

Family and domain databases

Gene3Di3.40.50.10540. 2 hits.
InterProiIPR003673. CoA-Trfase_fam_III.
IPR023606. CoA-Trfase_III_dom.
[Graphical view]
PfamiPF02515. CoA_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF89796. SSF89796. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

Isoform 1 (identifier: Q9HAC7-1) [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
MPSETHAMLA TLARVAALRR TCLFSGRGGG RGLWTGRPQS DMNNIKPLEG
60 70 80 90 100
VKILDLTRVL AGPFATMNLG DLGAEVIKVE RPGAGDDTRT WGPPFVGTES
110 120 130 140 150
TYYLSVNRNK KSIAVNIKDP KGVKIIKELA AVCDVFVENY VPGKLSAMGL
160 170 180 190 200
GYEDIDEIAP HIIYCSITGY GQTGPISQRA GYDAVASAVS GLMHITGPEN
210 220 230 240 250
GDPVRPGVAM TDLATGLYAY GAIMAGLIQK YKTGKGLFID CNLLSSQVAC
260 270 280 290 300
LSHIAANYLI GQKEAKRWGT AHGSIVPYQA FKTKDGYIVV GAGNNQQFAT
310 320 330 340 350
VCKILDLPEL IDNSKYKTNH LRVHNRKELI KILSERFEEE LTSKWLYLFE
360 370 380 390 400
GSGVPYGPIN NMKNVFAEPQ VLHNGLVMEM EHPTVGKISV PGPAVRYSKF
410 420 430 440
KMSEARPPPL LGQHTTHILK EVLRYDDRAI GELLSAGVVD QHETH
Length:445
Mass (Da):48,462
Last modified:July 19, 2005 - v2
Checksum:iD1FE42D75787692A
GO
Isoform 2 (identifier: Q9HAC7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     126-162: Missing.
     370-370: Q → QNAVSGFQSLLHSLAHGPFLHLQGSAR

Note: No experimental confirmation available.
Show »
Length:434
Mass (Da):47,186
Checksum:i7154D3E23618A883
GO
Isoform 3 (identifier: Q9HAC7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     370-370: Q → QNAVSGFQSLLHSLAHGPFLHLQGSAR

Show »
Length:471
Mass (Da):51,189
Checksum:iF55613A9604F5D55
GO
Isoform 4 (identifier: Q9HAC7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     200-247: Missing.

Note: No experimental confirmation available.
Show »
Length:397
Mass (Da):43,446
Checksum:i067AC010C8F7DD46
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti99 – 991E → G in BAB87807 (Ref. 7) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti336 – 3361R → W in GA3; inactive enzyme; healthy individuals who have abnormal quantities of glutaric acid but low 3-hydroxyglutaric acid. 2 Publications
Corresponds to variant rs137852860 [ dbSNP | Ensembl ].
VAR_054852

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei126 – 16237Missing in isoform 2. 1 PublicationVSP_014721Add
BLAST
Alternative sequencei200 – 24748Missing in isoform 4. 1 PublicationVSP_043291Add
BLAST
Alternative sequencei370 – 3701Q → QNAVSGFQSLLHSLAHGPFL HLQGSAR in isoform 2 and isoform 3. 2 PublicationsVSP_014722

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK021870 mRNA. Translation: BAB13922.1.
AK299133 mRNA. Translation: BAG61185.1.
AC004988 Genomic DNA. No translation available.
AC005030 Genomic DNA. No translation available.
AC005160 Genomic DNA. No translation available.
AC006023 Genomic DNA. No translation available.
AC025536 Genomic DNA. No translation available.
AC026866 Genomic DNA. No translation available.
AC079149 Genomic DNA. No translation available.
AC092030 Genomic DNA. No translation available.
CH236951 Genomic DNA. Translation: EAL24000.1.
CH471073 Genomic DNA. Translation: EAW94136.1.
BC098117 mRNA. Translation: AAH98117.1.
BC098261 mRNA. Translation: AAH98261.1.
BC098310 mRNA. Translation: AAH98310.1.
BC098318 mRNA. Translation: AAH98318.1.
AF397013 mRNA. Translation: AAL76418.1.
AB014767 mRNA. Translation: BAB87807.1.
CCDSiCCDS55104.1. [Q9HAC7-3]
CCDS55105.1. [Q9HAC7-1]
CCDS55106.1. [Q9HAC7-4]
RefSeqiNP_001180240.1. NM_001193311.1. [Q9HAC7-3]
NP_001180241.1. NM_001193312.1. [Q9HAC7-4]
NP_001180242.1. NM_001193313.1. [Q9HAC7-1]
NP_079004.1. NM_024728.2. [Q9HAC7-2]
UniGeneiHs.586313.

Genome annotation databases

EnsembliENST00000335693; ENSP00000338475; ENSG00000175600. [Q9HAC7-1]
ENST00000401647; ENSP00000385222; ENSG00000175600. [Q9HAC7-4]
ENST00000628514; ENSP00000486291; ENSG00000175600. [Q9HAC7-3]
GeneIDi79783.
KEGGihsa:79783.
UCSCiuc003thn.3. human. [Q9HAC7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK021870 mRNA. Translation: BAB13922.1.
AK299133 mRNA. Translation: BAG61185.1.
AC004988 Genomic DNA. No translation available.
AC005030 Genomic DNA. No translation available.
AC005160 Genomic DNA. No translation available.
AC006023 Genomic DNA. No translation available.
AC025536 Genomic DNA. No translation available.
AC026866 Genomic DNA. No translation available.
AC079149 Genomic DNA. No translation available.
AC092030 Genomic DNA. No translation available.
CH236951 Genomic DNA. Translation: EAL24000.1.
CH471073 Genomic DNA. Translation: EAW94136.1.
BC098117 mRNA. Translation: AAH98117.1.
BC098261 mRNA. Translation: AAH98261.1.
BC098310 mRNA. Translation: AAH98310.1.
BC098318 mRNA. Translation: AAH98318.1.
AF397013 mRNA. Translation: AAL76418.1.
AB014767 mRNA. Translation: BAB87807.1.
CCDSiCCDS55104.1. [Q9HAC7-3]
CCDS55105.1. [Q9HAC7-1]
CCDS55106.1. [Q9HAC7-4]
RefSeqiNP_001180240.1. NM_001193311.1. [Q9HAC7-3]
NP_001180241.1. NM_001193312.1. [Q9HAC7-4]
NP_001180242.1. NM_001193313.1. [Q9HAC7-1]
NP_079004.1. NM_024728.2. [Q9HAC7-2]
UniGeneiHs.586313.

3D structure databases

ProteinModelPortaliQ9HAC7.
SMRiQ9HAC7. Positions 42-438.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122883. 3 interactions.

PTM databases

iPTMnetiQ9HAC7.
PhosphoSiteiQ9HAC7.

Polymorphism and mutation databases

BioMutaiC7orf10.
DMDMi71152390.

Proteomic databases

MaxQBiQ9HAC7.
PRIDEiQ9HAC7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335693; ENSP00000338475; ENSG00000175600. [Q9HAC7-1]
ENST00000401647; ENSP00000385222; ENSG00000175600. [Q9HAC7-4]
ENST00000628514; ENSP00000486291; ENSG00000175600. [Q9HAC7-3]
GeneIDi79783.
KEGGihsa:79783.
UCSCiuc003thn.3. human. [Q9HAC7-1]

Organism-specific databases

CTDi79783.
GeneCardsiSUGCT.
HGNCiHGNC:16001. SUGCT.
HPAiHPA026698.
HPA026704.
HPA026705.
MalaCardsiSUGCT.
MIMi231690. phenotype.
609187. gene.
neXtProtiNX_Q9HAC7.
Orphaneti35706. Glutaric acidemia type 3.
PharmGKBiPA25942.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00530000063418.
HOGENOMiHOG000219745.
HOVERGENiHBG102620.
InParanoidiQ9HAC7.
KOiK18703.
OMAiTIQIRIE.
OrthoDBiEOG7WDN2T.
PhylomeDBiQ9HAC7.
TreeFamiTF314188.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000175600-MONOMER.

Miscellaneous databases

GenomeRNAii79783.
PROiQ9HAC7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HAC7.
CleanExiHS_C7orf10.
ExpressionAtlasiQ9HAC7. baseline and differential.
GenevisibleiQ9HAC7. HS.

Family and domain databases

Gene3Di3.40.50.10540. 2 hits.
InterProiIPR003673. CoA-Trfase_fam_III.
IPR023606. CoA-Trfase_III_dom.
[Graphical view]
PfamiPF02515. CoA_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF89796. SSF89796. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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 1 AND 2).
  2. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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] (ISOFORMS 1; 3 AND 4).
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-78, TISSUE SPECIFICITY.
  7. "Molecular cloning of a dermal papiila derived gene."
    Ikeda A., Yamashita M., Yoshimoto M.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-445 (ISOFORM 1).
    Tissue: Hair follicle dermal papilla.
  8. "C7orf10 encodes succinate-hydroxymethylglutarate CoA-transferase, the enzyme that converts glutarate to glutaryl-CoA."
    Marlaire S., Van Schaftingen E., Veiga-da-Cunha M.
    J. Inherit. Metab. Dis. 37:13-19(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT GA3 TRP-336.
  9. "Genetic mapping of glutaric aciduria, type 3, to chromosome 7 and identification of mutations in C7orf10."
    Sherman E.A., Strauss K.A., Tortorelli S., Bennett M.J., Knerr I., Morton D.H., Puffenberger E.G.
    Am. J. Hum. Genet. 83:604-609(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GA3 TRP-336.

Entry informationi

Entry nameiSUCHY_HUMAN
AccessioniPrimary (citable) accession number: Q9HAC7
Secondary accession number(s): A4D1W5
, B4DR73, Q4KMW4, Q4KMW8, Q4KMZ0, Q8TE00, Q8TEY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: June 8, 2016
This is version 115 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 7
    Human chromosome 7: 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. 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.