Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q96I99

- SUCB2_HUMAN

UniProt

Q96I99 - SUCB2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

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

Gene

SUCLG2

Organism
Homo sapiens (Human)
Status
Reviewed - 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.
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: 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.

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. 4 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.
OMAiEQMIGYN.
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. Align

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

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:
EMBL
GenBank
DDBJ
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 databases

DMDMi52788292.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS43104.1. [Q96I99-1 ]
CCDS54605.1. [Q96I99-2 ]
RefSeqi NP_001171070.1. NM_001177599.1. [Q96I99-2 ]
NP_003839.2. NM_003848.3. [Q96I99-1 ]
UniGenei Hs.644919.

3D structure databases

ProteinModelPortali Q96I99.
SMRi Q96I99. Positions 38-429.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114329. 25 interactions.
IntActi Q96I99. 4 interactions.
STRINGi 9606.ENSP00000307432.

Chemistry

DrugBanki DB00139. Succinic acid.

PTM databases

PhosphoSitei Q96I99.

Polymorphism databases

DMDMi 52788292.

2D gel databases

REPRODUCTION-2DPAGE IPI00096066.

Proteomic databases

MaxQBi Q96I99.
PaxDbi Q96I99.
PRIDEi Q96I99.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000307227 ; ENSP00000307432 ; ENSG00000172340 . [Q96I99-1 ]
ENST00000493112 ; ENSP00000419325 ; ENSG00000172340 . [Q96I99-2 ]
GeneIDi 8801.
KEGGi hsa:8801.
UCSCi uc003dna.4. human. [Q96I99-1 ]
uc021xae.1. human. [Q96I99-2 ]

Organism-specific databases

CTDi 8801.
GeneCardsi GC03M067507.
HGNCi HGNC:11450. SUCLG2.
HPAi HPA046705.
HPA051998.
MIMi 603922. gene.
neXtProti NX_Q96I99.
PharmGKBi PA36247.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0045.
GeneTreei ENSGT00390000010170.
HOGENOMi HOG000007059.
HOVERGENi HBG055555.
InParanoidi Q96I99.
KOi K01900.
OMAi EQMIGYN.
OrthoDBi EOG7CZK66.
PhylomeDBi Q96I99.
TreeFami TF300624.

Enzyme and pathway databases

UniPathwayi UPA00223 .
BioCyci MetaCyc:HS10493-MONOMER.
Reactomei REACT_1785. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSi SUCLG2. human.
GenomeRNAii 8801.
NextBioi 33012.
PROi Q96I99.
SOURCEi Search...

Gene expression databases

Bgeei Q96I99.
CleanExi HS_SUCLG2.
ExpressionAtlasi Q96I99. baseline and differential.
Genevestigatori Q96I99.

Family and domain databases

Gene3Di 3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
InterProi IPR013650. 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 ]
PANTHERi PTHR11815. PTHR11815. 1 hit.
Pfami PF08442. ATP-grasp_2. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view ]
PIRSFi PIRSF001554. SucCS_beta. 1 hit.
SUPFAMi SSF52210. SSF52210. 1 hit.
TIGRFAMsi TIGR01016. sucCoAbeta. 1 hit.
PROSITEi PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].

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: October 29, 2014
This is version 141 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