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Protein

Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial

Gene

SUCLG2

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

Functioni

Catalyzes the GTP-dependent ligation of succinate and CoA to form succinyl-CoA.By similarity

Catalytic activityi

GTP + succinate + CoA = GDP + phosphate + succinyl-CoA.

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. GDP binding Source: Ensembl
  3. GTP binding Source: UniProtKB-KW
  4. succinate-CoA ligase (GDP-forming) activity Source: UniProtKB

GO - Biological processi

  1. cellular metabolic process Source: Reactome
  2. small molecule metabolic process Source: Reactome
  3. succinate metabolic process Source: Ensembl
  4. succinyl-CoA metabolic process Source: UniProtKB
  5. tricarboxylic acid cycle Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS10493-MONOMER.
BRENDAi6.2.1.4. 2681.
ReactomeiREACT_1785. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial (EC:6.2.1.4)
Alternative name(s):
GTP-specific succinyl-CoA synthetase subunit beta
Succinyl-CoA synthetase beta-G chain
Short name:
SCS-betaG
Gene namesi
Name:SUCLG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:11450. SUCLG2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrion Source: HPA
  3. plasma membrane Source: HPA
  4. succinate-CoA ligase complex (GDP-forming) Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36247.

Chemistry

DrugBankiDB00139. Succinic acid.

Polymorphism and mutation databases

BioMutaiSUCLG2.
DMDMi52788292.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3737MitochondrionBy similarityAdd
BLAST
Chaini38 – 432395Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrialPRO_0000033356Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei73 – 731N6-acetyllysineBy similarity
Modified residuei78 – 781N6-succinyllysineBy similarity
Modified residuei132 – 1321N6-acetyllysineBy similarity
Modified residuei139 – 1391N6-acetyllysineBy similarity
Modified residuei200 – 2001N6-acetyllysineBy similarity
Modified residuei218 – 2181N6-acetyllysineBy similarity
Modified residuei227 – 2271N6-acetyllysine1 Publication
Modified residuei271 – 2711N6-acetyllysineBy similarity
Modified residuei291 – 2911N6-acetyllysine1 Publication
Modified residuei338 – 3381N6-succinyllysineBy similarity
Modified residuei347 – 3471N6-acetyllysineBy similarity
Modified residuei386 – 3861N6-acetyllysineBy similarity
Modified residuei423 – 4231N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ96I99.
PaxDbiQ96I99.
PRIDEiQ96I99.

2D gel databases

REPRODUCTION-2DPAGEIPI00096066.

PTM databases

PhosphoSiteiQ96I99.

Expressioni

Tissue specificityi

Mainly expressed in liver, kidney, heart, spleen and skeletal muscle. Also found in intestine and colon, and in low amounts in lung, brain, prostate, testis and ovary.1 Publication

Gene expression databases

BgeeiQ96I99.
CleanExiHS_SUCLG2.
ExpressionAtlasiQ96I99. baseline and differential.
GenevestigatoriQ96I99.

Organism-specific databases

HPAiHPA046705.
HPA051998.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.

Protein-protein interaction databases

BioGridi114329. 25 interactions.
IntActiQ96I99. 5 interactions.
STRINGi9606.ENSP00000307432.

Structurei

3D structure databases

ProteinModelPortaliQ96I99.
SMRiQ96I99. Positions 38-429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 274229ATP-graspAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0045.
GeneTreeiENSGT00390000010170.
HOGENOMiHOG000007059.
HOVERGENiHBG055555.
InParanoidiQ96I99.
KOiK01900.
OMAiTNVHEAQ.
OrthoDBiEOG7CZK66.
PhylomeDBiQ96I99.
TreeFamiTF300624.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
InterProiIPR013650. ATP-grasp_succ-CoA_synth-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005811. CoA_ligase.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR005809. Succ_CoA_synthase_bsu.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PANTHERiPTHR11815. PTHR11815. 1 hit.
PfamiPF08442. ATP-grasp_2. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF001554. SucCS_beta. 1 hit.
SUPFAMiSSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01016. sucCoAbeta. 1 hit.
PROSITEiPS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

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

Isoform 1 (identifier: Q96I99-1) [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
MASPVAAQAG KLLRALALRP RFLAAGSQAV QLTSRRWLNL QEYQSKKLMS
60 70 80 90 100
DNGVRVQRFF VADTANEALE AAKRLNAKEI VLKAQILAGG RGKGVFNSGL
110 120 130 140 150
KGGVHLTKDP NVVGQLAKQM IGYNLATKQT PKEGVKVNKV MVAEALDISR
160 170 180 190 200
ETYLAILMDR SCNGPVLVGS PQGGVDIEEV AASNPELIFK EQIDIFEGIK
210 220 230 240 250
DSQAQRMAEN LGFVGPLKSQ AADQITKLYN LFLKIDATQV EVNPFGETPE
260 270 280 290 300
GQVVCFDAKI NFDDNAEFRQ KDIFAMDDKS ENEPIENEAA KYDLKYIGLD
310 320 330 340 350
GNIACFVNGA GLAMATCDII FLNGGKPANF LDLGGGVKEA QVYQAFKLLT
360 370 380 390 400
ADPKVEAILV NIFGGIVNCA IIANGITKAC RELELKVPLV VRLEGTNVQE
410 420 430
AQKILNNSGL PITSAIDLED AAKKAVASVA KK
Length:432
Mass (Da):46,511
Last modified:September 27, 2004 - v2
Checksum:i56A977A3E50713A1
GO
Isoform 2 (identifier: Q96I99-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     397-432: NVQEAQKILN...KKAVASVAKK → FMEKKGSYMH...SKCAISIFLC

Note: No experimental confirmation available.

Show »
Length:440
Mass (Da):47,732
Checksum:iFFBA486CDA19334B
GO

Sequence cautioni

The sequence AAH07716.3 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH47024.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH47024.1 differs from that shown. Reason: Erroneous termination at position 31. Translated as Gln.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti174 – 1752GV → RS in AAC64397 (PubMed:9765291).Curated
Sequence conflicti220 – 2201Q → K in AAH68602 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti347 – 3471K → R.
Corresponds to variant rs9843840 [ dbSNP | Ensembl ].
VAR_052499
Natural varianti381 – 3811R → W.
Corresponds to variant rs7623258 [ dbSNP | Ensembl ].
VAR_052500

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei397 – 43236NVQEA…SVAKK → FMEKKGSYMHIKQETGNSNE NITGIQENVAHQNLSKCAIS IFLC in isoform 2. 1 PublicationVSP_042013Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK310527 mRNA. No translation available.
AC099783 Genomic DNA. No translation available.
AC112213 Genomic DNA. No translation available.
AC113169 Genomic DNA. No translation available.
AC114401 Genomic DNA. No translation available.
BC007716 mRNA. Translation: AAH07716.3. Different initiation.
BC019868 mRNA. Translation: AAH19868.1.
BC047024 mRNA. Translation: AAH47024.1. Sequence problems.
BC068602 mRNA. Translation: AAH68602.1.
AF058954 mRNA. Translation: AAC64397.1.
AF131748 mRNA. Translation: AAD20032.1.
CCDSiCCDS43104.1. [Q96I99-1]
CCDS54605.1. [Q96I99-2]
RefSeqiNP_001171070.1. NM_001177599.1. [Q96I99-2]
NP_003839.2. NM_003848.3. [Q96I99-1]
UniGeneiHs.644919.

Genome annotation databases

EnsembliENST00000307227; ENSP00000307432; ENSG00000172340. [Q96I99-1]
ENST00000493112; ENSP00000419325; ENSG00000172340. [Q96I99-2]
GeneIDi8801.
KEGGihsa:8801.
UCSCiuc003dna.4. human. [Q96I99-1]
uc021xae.1. human. [Q96I99-2]

Polymorphism and mutation databases

BioMutaiSUCLG2.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK310527 mRNA. No translation available.
AC099783 Genomic DNA. No translation available.
AC112213 Genomic DNA. No translation available.
AC113169 Genomic DNA. No translation available.
AC114401 Genomic DNA. No translation available.
BC007716 mRNA. Translation: AAH07716.3. Different initiation.
BC019868 mRNA. Translation: AAH19868.1.
BC047024 mRNA. Translation: AAH47024.1. Sequence problems.
BC068602 mRNA. Translation: AAH68602.1.
AF058954 mRNA. Translation: AAC64397.1.
AF131748 mRNA. Translation: AAD20032.1.
CCDSiCCDS43104.1. [Q96I99-1]
CCDS54605.1. [Q96I99-2]
RefSeqiNP_001171070.1. NM_001177599.1. [Q96I99-2]
NP_003839.2. NM_003848.3. [Q96I99-1]
UniGeneiHs.644919.

3D structure databases

ProteinModelPortaliQ96I99.
SMRiQ96I99. Positions 38-429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114329. 25 interactions.
IntActiQ96I99. 5 interactions.
STRINGi9606.ENSP00000307432.

Chemistry

DrugBankiDB00139. Succinic acid.

PTM databases

PhosphoSiteiQ96I99.

Polymorphism and mutation databases

BioMutaiSUCLG2.
DMDMi52788292.

2D gel databases

REPRODUCTION-2DPAGEIPI00096066.

Proteomic databases

MaxQBiQ96I99.
PaxDbiQ96I99.
PRIDEiQ96I99.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307227; ENSP00000307432; ENSG00000172340. [Q96I99-1]
ENST00000493112; ENSP00000419325; ENSG00000172340. [Q96I99-2]
GeneIDi8801.
KEGGihsa:8801.
UCSCiuc003dna.4. human. [Q96I99-1]
uc021xae.1. human. [Q96I99-2]

Organism-specific databases

CTDi8801.
GeneCardsiGC03M067507.
HGNCiHGNC:11450. SUCLG2.
HPAiHPA046705.
HPA051998.
MIMi603922. gene.
neXtProtiNX_Q96I99.
PharmGKBiPA36247.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0045.
GeneTreeiENSGT00390000010170.
HOGENOMiHOG000007059.
HOVERGENiHBG055555.
InParanoidiQ96I99.
KOiK01900.
OMAiTNVHEAQ.
OrthoDBiEOG7CZK66.
PhylomeDBiQ96I99.
TreeFamiTF300624.

Enzyme and pathway databases

UniPathwayiUPA00223.
BioCyciMetaCyc:HS10493-MONOMER.
BRENDAi6.2.1.4. 2681.
ReactomeiREACT_1785. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSiSUCLG2. human.
GenomeRNAii8801.
NextBioi33012.
PROiQ96I99.
SOURCEiSearch...

Gene expression databases

BgeeiQ96I99.
CleanExiHS_SUCLG2.
ExpressionAtlasiQ96I99. baseline and differential.
GenevestigatoriQ96I99.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
InterProiIPR013650. ATP-grasp_succ-CoA_synth-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005811. CoA_ligase.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR005809. Succ_CoA_synthase_bsu.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PANTHERiPTHR11815. PTHR11815. 1 hit.
PfamiPF08442. ATP-grasp_2. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF001554. SucCS_beta. 1 hit.
SUPFAMiSSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01016. sucCoAbeta. 1 hit.
PROSITEiPS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]
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] (ISOFORM 2).
    Tissue: Testis.
  2. "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].
  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 1).
    Tissue: Hippocampus, Mammary gland, Placenta and Uterus.
  4. "Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes."
    Johnson J.D., Mehus J.G., Tews K., Milavetz B.I., Lambeth D.O.
    J. Biol. Chem. 273:27580-27586(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-432 (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Liver.
  5. Mei G., Yu W., Gibbs R.A.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 234-432 (ISOFORM 1).
    Tissue: Brain.
  6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-227 AND LYS-291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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 nameiSUCB2_HUMAN
AccessioniPrimary (citable) accession number: Q96I99
Secondary accession number(s): C9JVT2
, O95195, Q6NUH7, Q86VX8, Q8WUQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: September 27, 2004
Last modified: April 29, 2015
This is version 145 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. 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

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.