wanglab/gogpt-training-data huggingface dataset:
Protein: Serine O-succinyltransferase (SST) (EC 2.3.1.-) (Q5AT15)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Transfers a succinyl group from succinyl-CoA to L-serine, forming succinyl-L-serine. Has also weak serine acetyl transferase activity and homoserine succinyl transferase activity.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q10341}.
Interaction partners:
- cystathionine gamma-lyase
- Cystathionine beta-synthase
- Saccharopine dehydrogenase [NAD
- Cysteine synthase 1
- Homocysteine synthase
Sequence:
MSPLNGVARSFPRPFQAVTRRPFRVVQPAIACPSNSRSFNHSRSLRSTGSQSPAPSPRDSSNPALSFPCLDAQEAKSALLSARSLGSGPEPSYTAGHHERFHSDEPLLLDWGGLLPEFDIAYETWGQLNEKKDNVILLHTGLSASSHAHSTEANPKPGWWEKFIGPGKTLDTDKYFVICTNVLGGCYGSTGPSTVDPSDGKKYATRFPILTIEDMVRAQFRLLDHLGVRKLYASVGSSMGGMQSLAAGVLFPERVGKIVSISGCARSHPYSIAMRHTQRQVLMMDPNWARGFYYDSIPPHSGMKLAREIATVTYRSGPEWEKRFGRKRADPSKQPALCPDFLIETYLDHAGEKFCLEYDANSLLYISKAMDLFDLGLTQQLATKKQRAEAQAKISSGTNTVNDASCSLTLPEQPYQEQPSASTSAEQSASASETGSAPNDLVAGLAPLKDHQVLVIGVASDILFPAWQQREIAETLIQAGNKTVEHIELGNDVSLFGHDTFLLDVKNVGGAVRKFLD
Protein: chitinase (EC 3.2.1.14) (Q4WWU6)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
Sequence:
MVSASNLLYSIAAFAAFDCAYSLLDTSSSSTVAVYWGQNSGNTGQQRLSYYCDTYVQQVFQLAFVTRISGAAGLPELDFANQESQCTVYSGTNLLNCPQIGEDIKLCQQKGKTILISIGGAASPELGFASEAAAIEAANKMWQIFGPVDADNTAYRPFGDAAIDGFDFDFETSVTNIVPFANQLRRLMDTSAGRRYYLTVAPQCVFPDVADQEMLNGAVAFDAIWVQFYNNYCGVNAFSFGTMQQDAFNFDLWDAWAKSQSKNKQVKVFIGLPGNVVAAGTGYVGAEQLREIVAWSKAFSSFGGIMIWDASSMDANQGYLESVKKTLIG
Protein: Phosphotransferase (EC 2.7.1.-) (Q9GQI2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
FKQSSRRPEFASVLQRNEEVFETRYISEIEDDSFPEFASTRKIVKNLFGLEKASVEDCQTLRYICECVAKRAATLIAIGVSGLVNRTSNRRVIVGMDGSVYRYHPKFDAYMRQTLQKLVKADKEWDIMLSEDGSGRGAAL
Protein: Mannitol-1-phosphate 5-dehydrogenase (M1PDH) (MPD) (MPDH) (EC 1.1.1.17) (Q4X1A4)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway. Has a strong preference for NADH over NADPH.
Interaction partners:
- ATP-dependent 6-phosphofructokinase
- Phosphotransferase
- Hexokinase-1
- Phosphotransferase
- Mannose-6-phosphate isomerase
- Mannose-6-phosphate isomerase
- Phosphotransferase
- Phosphotransferase
- 6-phosphofructo-2-kinase 1
- fructose-2,6-bisphosphate 2-phosphatase
Sequence:
MGKKAIQFGGGNIGRGFVAEFLHEAGYEVVFIDVVDKIIDALKSTPSYEVTEVSEEGEKTKTITNYRAINSKTNEEDVVKEIGTADVVTCAVGPNVLKFIAPVIAKGIDARTASKPVAVIACENAIGATDTLRGFIEQNTDKDRLSSMSERARFANSAIDRIVPNQPPNAGLNVRIEKFYEWTVEQTPFGEFGHPDIPAIHWVDDLKPYIERKLFTVNTGHATTAYYGHMRGKKMIADALADAEIRQIVHKVLEQTAKLITTKHEITEQEQNEYVDTIVKRMSNPFLEDNVERVGRAPLRKLSRNERFIGPASQLAEKGLPFDALLGSIEMALRFQNVPGDEESAELAKILKEMSAEEATGKLTGLEKHHPLYEPVQNVIAKVQKDSK
Protein: ABSCISIC ACID-INSENSITIVE 5-like protein 7 (ABA-responsive element-binding protein 2) (Abscisic acid responsive elements-binding factor 4) (ABRE-binding factor 4) (bZIP transcription factor 38) (AtbZIP38) (Q9M7Q2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as transcriptional activator in the ABA-inducible expression of LTI65/RD29B (AC Q04980). Binds specifically to the ABA-responsive element (ABRE) of the LTI65/RD29B (AC Q04980) gene promoter. Binds to the promoter of FREE1 and activates its transcription.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- NAC domain-containing protein 96
- Serine/threonine-protein kinase SRK2D
- Dehydration-responsive element-binding protein 1A
- Calcium-dependent protein kinase 32
- Serine/threonine-protein kinase SRK2I
- Serine/threonine-protein kinase SRK2E
- Dehydration-responsive element-binding protein 2C
- Dehydration-responsive element-binding protein 2A
- Basic leucine zipper 8
- Low-temperature-induced 78 kDa protein
Sequence:
MGTHINFNNLGGGGHPGGEGSSNQMKPTGSVMPLARQSSVYSLTFDELQNTLGGPGKDFGSMNMDELLKSIWTAEEAQAMAMTSAPAATAVAQPGAGIPPPGGNLQRQGSLTLPRTISQKTVDEVWKCLITKDGNMEGSSGGGGESNVPPGRQQTLGEMTLEEFLFRAGVVREDNCVQQMGQVNGNNNNGFYGNSTAAGGLGFGFGQPNQNSITFNGTNDSMILNQPPGLGLKMGGTMQQQQQQQQLLQQQQQQMQQLNQPHPQQRLPQTIFPKQANVAFSAPVNITNKGFAGAANNSINNNNGLASYGGTGVTVAATSPGTSSAENNSLSPVPYVLNRGRRSNTGLEKVIERRQRRMIKNRESAARSRARKQAYTLELEAEIEKLKKTNQELQKKQAEMVEMQKNELKETSKRPWGSKRQCLRRTLTGPW
Protein: Calcitonin receptor (CT-R) (P79222)
Organism: Oryctolagus cuniculus (Rabbit)
Function: This is a receptor for calcitonin. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. The calcitonin receptor is thought to couple to the heterotrimeric guanosine triphosphate-binding protein that is sensitive to cholera toxin. Isoform 2 has altered ligand binding and abolished coupling to phospholipase C.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P30988}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P30988}.
Interaction partners:
- Receptor activity-modifying protein 2
- Pro-adrenomedullin
- Calcitonin related polypeptide beta
- Islet amyloid polypeptide
- Receptor activity-modifying protein 1
- Calcitonin
- Calcitonin gene-related peptide type 1 receptor
- RHD domain-containing protein
- Cathepsin K
- Guanine nucleotide-binding protein G
Sequence:
MKFTLTWRCFALFLLLHQPTPVNPASSNDTHPTVEPEPFLYVIGRKKLMDAQYKCYDRMEQLPPYQGEGPYCNRTWDGWMCWDDTPAGVLGFQYCPDYFPDFDPTEKVTKYCDETGVWFKHPGNNQTWSNYTMCNAFTPEKLQNAYVLYYLAIVGHSLSIFTLVISLGIFKCFRSLGCQRVTLHKNMFLTYILNSMIIIIHLVEVVPNGELVRRDPVSCKVLHFFHQYMMSCNYFWMLCEGIYLHTLIVVAVFAKQQHLRWYYLLGWGFPLVPTTIHAITRAIYFNDNCWMSVETHLLYIIHGPVMAALVVNFFFLLNIVRVLVTKMRETLEAESHMYLKAVKATMILVPLLGIQFVVFPWRPSNKILGKIYDYLMHSLIHFQGFFVATIYCFCNNEVQTTVKRQWVQFKIQWNQRWGRRPAHRSVSRTAASAEEGGIPVYIYHQEPRNDPAHSLGEEGAEIIPLNIIEQESSA
Protein: GPI ethanolamine phosphate transferase 1 (EC 2.-.-.-) (Morphogenesis checkpoint-dependent protein 4) (Supersecretion of u-PA protein 21) (P36051)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. Ethanolamine phosphate on the alpha-1,4-linked mannose is essential for further mannosylation by GPI10 and is necessary for an efficient recognition of GPI lipids and GPI proteins by the GPI transamidase, for the efficient transport of GPI anchored proteins from endoplasmic reticulum to Golgi and for the physiological incorporation of ceramides into GPI anchors by lipid remodeling. Also involved in non-mitochondrial ATP movements across membrane and participates in Golgi and endoplasmic reticulum function, Also required for the incorporation of BGL2 into the cell wall.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:35015055}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane; Multi-pass membrane protein. Vacuole membrane; Multi-pass membrane protein.
Interaction partners:
- GPI mannosyltransferase 3
- GPI mannosyltransferase 2
- GPI-anchored wall transfer protein 1
- Glycosylphosphatidylinositol anchor biosynthesis protein 11
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit
- GPI-anchor transamidase
- GPI mannosyltransferase 1
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI15
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit
Sequence:
MWNKTRTTLLAVGVLFHLFYLWSIFDIYFISPLVHGMSPYQSTPTPPAKRLFLIVGDGLRADTTFDKVTHPVSGKTEFLAPFIRSLVMNNATYGISHTRMPTESRPGHVAMIAGFYEDVSAVTKGWKSNPVNFDSFFNQSTHTYSFGSPDILPMFKDGASDPNKVDTWMYDHTFEDFTQSSIELDAFVFRHLDQLFHNSTLNSTLDYEIRQDGNVFFLHLLGCDTAGHSYRPYSAEYYDNVKYIDDQIPILIDKVNKFFADDKTAFIFTADHGMSAFGSHGDGHPNNTRTPLVAWGAGLNKPVHNPFPVSDNYTENWELSSIKRNDVKQADIASLMSYLIGVNYPKNSVGELPIAYIDGKESDKLAALYNNARSILEQYLVKQDEVIDSQFFYKEYFKFVEKSHSHYLEEIETLIQRISEGENYLEQEAITLTEELMQITLEGLHYLTTYNWRFIRTIVTFGFVGWIFFSFIIFLKSFILENVIDDQKASPLSHAVFGSIGILLNWILFYQHSPFNFYMYLLFPLYFWSYIFTNRSVLRSGIKEFFKGTSPWKRVLITISIISVYEGIVYGFFHRWTFTLITNILAFYPFICGVRELSVNILWIITSVLLSTFTLFDAVKIEDLNQIHLAGLLIILSAFYALYKIHSRINSYTRAIFAIQISLVAAMLAVTHRSVISLQLRQGLPRESQVAGWIIFFVSLFVMPILHYRKPNNDYKVRLLIIYLTFAPSFIILTISFESLFYFLFTSYMVQWIEIENKIKEMKTQKDENWLQVLRVSVIGFFLLQVAFFGTGNVASISSFSLESVCRLLPIFDPFLMGALLMLKLIIPYGLLSTCLGILNLKLNFKDYTISSLIISMSDILSLNFFYLLRTEGSWLDIGITISNYCLAILSSLFMLILEVLGHVLLKNVIIQDKTKKTQ
Protein: Serine/threonine-protein kinase SAPK6 (EC 2.7.11.1) (Osmotic stress/abscisic acid-activated protein kinase 6) (stress-activated protein kinase 6) (OsSAPK6) (Q6ZI44)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May play a role in signal transduction of hyperosmotic response (Probable). Can phosphorylate ABI5 in vitro. Can phosphorylate BZIP46 in vitro.
Interaction partners:
- Probable protein phosphatase 2C 6
- Probable protein phosphatase 2C 30
- Probable protein phosphatase 2C 8
- bZIP transcription factor 46
- Probable protein phosphatase 2C 68
- bZIP transcription factor 23
- bZIP transcription factor ABI5 homolog
- bZIP transcription factor TRAB1
- protein-serine/threonine phosphatase
- Os09g0456200 protein
Sequence:
MEKYELLKDIGSGNFGVARLMRNRETKELVAMKYIPRGLKIDENVAREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAAGGELFDRICSAGRFSEDESRYFFQQLICGVSYCHFMQICHRDLKLENTLLDGSPAPRLKICDFGYSKSSLLHSKPKSTVGTPAYIAPEVLSRREYDGKMADVWSCGVTLYVMLVGAYPFEDPDDPKNFRKTIGRIVSIQYKIPEYVHISQDCRQLLSRIFVANPAKRITIREIRNHPWFMKNLPRELTEAAQAKYYKKDNSARTFSDQTVDEIMKIVQEAKTPPPSSTPVAGFGWTEEEEQEDGKNPDDDEGDRDEEEGEEGDSEDEYTKQVKQAHASCDLQKS
Protein: Proteasome subunit beta type-1 (20S proteasome beta subunit F-1) (Proteasome component 5) (Proteasome subunit beta type-6) (TAS-F22/FAFP98) (TAS-G39.20) (P42742)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Non-catalytic component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit alpha type-4-A
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-6-B
- Proteasome subunit alpha type-5-B
- Proteasome subunit beta type-3-B
- Proteasome subunit beta type-6
- Proteasome subunit alpha type-1-B
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-3-A
Sequence:
MTKQHANWSPYDNNGGTCVAIAGSDYCVIAADTRMSTGYSILSRDYSKIHKLADRAVLSSSGFQADVKALQKVLKSRHLIYQHQHNKQMSCPAMAQLLSNTLYFKRFFPYYAFNVLGGLDEEGKGCVFTYDAVGSYERVGYGAQGSGSTLIMPFLDNQLKSPSPLLLPKQDSNTPLSEAEAVDLVKTVFASATERDIYTGDKLEIMILKADGIKTELMDLRKD
Protein: PH domain-containing protein (Q8MPR9)
Organism: Caenorhabditis elegans
Interaction partners:
- MYND-type domain-containing protein
- Golgi pH regulator
- Golgi pH regulator
Sequence:
MLERRKERKLTITSPNEDMRIVEPPAHKQRRASLSVAYHRLLSFSSSPIKKQKKEYRDEKKRVNDELLSALRDPTVVVMADTLKIRGALKRWNRYYCVLKPGLLILYKHKKADRGDWVGTVLLNHCELIERPSKKDGFCFKLFHPMDMSIWGNRGPLGQSFGSFTLNPLNTSFLICRAPSDQAGRCWMDALELSFKCTGLLKKTMNELDDKNGDSSMNDGQRDESRMSRDSDGDDTRELAVSETDAEKHFQEIDDVQDEDHEDGKMSETSDTIREAFTESAWIPSPKEVFGPDGSLTEEVGEENKSLIWTLLKQIRPGMDLSKVVLPTFILEPRSFLEKLADYYYHADLISEAVAEPDPFQRIVKVTKFFLSGFYKKPKGLKKPYNPILGETFRCKWEHPDGSTTFYMAEQVSHHPPVSSLFITNRKAGFNISGTILAKSKYYGNSLSAILAGKLRLTLLNLGETYIVNLPYANCKGIMIGTMTMELGGEVNIECEKTGYRTTLDFKLKPMLGGAYNQIEGSIKYGSDRLASIEGAWDGVIRIKGPDGKKELWNPTPEVIKTRLPRYEINMDEQGEWESAKLWRHVTEAISNEDQYKATEEKTALENDQRARAKSGIPHETKFFKKQHGDDYVYIHADYRPWDNNNDIQQIENNYVVKTISRHSKRKTGNSEQLGSDNTSEASESDEEVIEPKIKKKEIVPAKSKPITPEVADERIKEMERKFELAIRRMEAANERQSSRTLNAIQSTLLFVFVVTSVVQSIFMFFMLRK
Protein: PAT complex subunit CCDC47 (Coiled-coil domain-containing protein 47) (Q23382)
Organism: Caenorhabditis elegans
Subcellular location: Rough endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00034697}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00034697}.
Interaction partners:
- Calcium load-activated calcium channel homolog
- Nicalin
- Translocon Sec61/SecY plug domain-containing protein
- Protein transport protein Sec61 subunit beta
- Developmentally-regulated GTP-binding protein 1
- Protein transport protein Sec61 subunit gamma
- Prion-like
- Large ribosomal subunit protein uL18
- Uncharacterized protein
- Large ribosomal subunit protein eL38
Sequence:
MKIVWIFLIFFIGFAISTDDNEFAEFEDEFVGSSATQAPEIQREGEPPVLKQKDDFEEEDFGVVEEEPEEAEKVREADSDDAAPAQPLKFADVPAHFRSNWASYQVEGIVVLIILIYMTNYLIGKTTNASIAQTIFDMCRPTLEEQFAVVGDDGTTDLDKMIPSLKHDTDSTFSAWCTGRVNVNSLFLQMKMVKRQDVVSRIMEMFTPSGDKMTIKASLETTNDTDPLIFAVGEKKIASKYFKEMLDLNSFASERKQAAQQFNLPASWQVYADQNEVVFSILDPGVVSLLKKHEDAIEFIHISDQFTGPKPAEGESYTRLPEAQRYMFVSLNLQYLGQDEESVMEILNLVFYLIDKARKMKLSKDAKVKAERRRKEFEDAFLKQTHQFRQEAAQARREEKTRERKQKLMDESDPERQKRLEAKELKREAKAKSPKMKQLKVK
Protein: Phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) (AIR carboxylase) (AIRC) (O74197)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome H complete sequence
- Adenylosuccinate lyase
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Amidophosphoribosyltransferase
- Phosphoribosylformylglycinamidine synthase
- Candida glabrata strain CBS138 chromosome A complete sequence
- Phosphoribosylglycinamide formyltransferase
- Orotidine 5'-phosphate decarboxylase
- Imidazoleglycerol-phosphate dehydratase
- 3-isopropylmalate dehydrogenase
Sequence:
MDSRTVGILGGGQLGRMIVEAANRLNIKTLILDAPNSPAKQITNASDHVDGSFANKEDIEALAAKCDVMTVEIEHVDVNALKEVQKQFPKLEIYPTPETIGLIQDKYVQKQHLVKNRIPVVPSITVENSKESLIKTGSSLGYPFVLKSRTLAYDGRGNFVVKSEEDIEKGLEFLANRPLYAEKWASFKKELSVMIIRSLDGRVYSYPIVETIHKNNVCHLCYVPARVPDSVQHKAKLMAENAIKSFPGCGIFGVEMFLLDDDSIVLNEIAPRPHNSGHYTINACVVSQFEAHLRAILDLPMPKNFTSLSTNSTNAIMLNLLGDPETKDKELQICERALNTPGASVYLYGKESKPNRKVGHINIVCSSMKECDKRLQFIMGLKTDPIKHSVMEILNAEEVRKPLVGVIMGSDSDLPVMSAACKMLEQFEVPFEVTIVSAHRTPYRMNKYASEAVSRGIKVIIAGAGGAAHLPGMVAAMTPVPVIGVPVKGSTLDGVDSLHSIVQMPRGVPVATVAINNSTNAGILAVRMLGIHNYDYVKKMEEFLNKQEEEVLQKAAKLESIGYEKYLESK
Protein: Guanylate-binding protein 6 (EC 3.6.5.-) (GTP-binding protein 6) (GBP-6) (Guanine nucleotide-binding protein 6) (Macrophage activation 2 like protein) (A0A0G2JDV3)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions (By similarity). Confers protection to several pathogens, including the bacterial pathogens Listeria monocytogenes and Mycobacterium bovis BCG as well as the protozoan pathogen Toxoplasma gondii.
Subcellular location: Cytoplasmic vesicle {ECO:0000269|PubMed:18025219}.
Interaction partners:
- Interferon-inducible GTPase 1
- Immunity-related GTPase family M protein 2
- Immunity-related GTPase family M protein 3
- Interferon-induced protein 44
- Immunity-related GTPase family M protein 1
- Interferon-induced protein with tetratricopeptide repeats 2
- Antiviral innate immune response effector IFIT1
- Interferon-induced protein with tetratricopeptide repeats 3
- GTP-binding protein
- Signal transducer and activator of transcription 1
Sequence:
MTQPQMAPICLVENHNEQLSVNQEAIEILDKISQPVVVVAIVGLYRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLDTEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMITINHQALEQLQYVTELTELIRAKSSPNPAGIKNSTEFVSFFPDFVWTVRDFMLELKLNGEDITSDDYLENALKLIPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKLDSITEDQLDPKFQEVTKAFVSYIFTYAKIKTLKEGIKVTGNRLGILVTTYVNAINSGAVPCLDDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVHAACEKEAMAVFMEHSFKDENQQFLKKLVELIGENKELFLSKNEEASNKYCQEELDRLSKDFMENISTFFVPCGHKLYMDKREKIEHDYWQVPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGEKAIAEERAQKVAAEKEQELLRQKQKEQQEYMEAQEKSHKENLEQLRRKLEQEREQDIKDHDMMLKKLMKDQKAFLEEGFKKKAEEMNKEIQQLRDVIKDKKRNTDRIKEALLNGFSTVLFHYLVRYLKHL
Protein: MMS19 nucleotide excision repair protein (H0Y746)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000256|RuleBase:RU367072}. Nucleus {ECO:0000256|RuleBase:RU367072}.
Interaction partners:
Sequence:
XWSYEDKDQRPLNGFKDQLCSLVFMALTDPSTQLQLVGIRTLTVLGAQPDLLSYEDLELAVGHLYRLSFLKEDSQSCRVAALEASGTLAALYPVAFSSHLVPKLAEELRVGESNLTNGDEPTQCSRHLCCLQALSAVSTHPSIVKETLPLLLQHLWQVNRGNMVAQSSDVIAVCQSLRQMAEKCQQDPESCWYFHQTAIPCLLALAVQASMPEKEPSVLRKVLLEDEVLAAMVSVIGTATTHLSPELAAQSVTHIVPLFLDGNVSFLPENSFPSRFQPFQDGSSGQRRLIALLMAFVCSLPRNVEIPQLNQLMRELLELSCCHSCPFSSTAAAKCFAGLLNKHPAGQQLDEFLQLAVDKVEAGLGSGPCRSQAFTLLLWVTKALVLRYHPLSSCLTARLMGLLSDPELGPAAADGFSLLMSDCTDVLTRAGHAEVRIMFRQRFFTDNVPALVQGFHAAPQDVKPNYLKGLSHVLNRLPKPVLLPELPTALSCPDCVVQLSTLSCLQPLLLEAPQVMSLHVDTLVTKFLNLSSSPSMAVRIAALQCMHALTRLPTPVLLPYKPQVIRALAKPLDDKKRLVRKEAVSARGEWFLLGSPGS
Protein: Nucleotide exchange factor SIL1 (A0A0G2KDW7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
- FAU ubiquitin-like and ribosomal protein S30 fusion b
- FAU ubiquitin-like and ribosomal protein S30 fusion a ubiquitously expressed
- Immunoglobulin binding protein
- Hypoxia up-regulated protein 1
- Small ribosomal subunit protein uS10m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL12m
- Mitochondrial ribosomal protein S9.
- Large ribosomal subunit protein uL15m
- Elongation factor Tu
Sequence:
MLTSRVMANKWRVRFGLTVTFWLLSLHLIFAHDVKSPTALLIKEDSDDLNNAKETHLEDEDPEDLEVFRPTDKWQTLRPGQAVPAGSHVRLNLQTGQREVKMGEEEGFKYWKDGNRQGMMNMDSHSFTAEELKKALKKFKKGADDPVDQQEEDAVRAKFRPMDELKKDMEALDMLVETDIQVMRRLLDQFNNTNSTTEEKVAALLDLEYLVHQVDNAQNLVSMGGMSLVIRSLNSTDVRLQECAAFVLGSAVSSNPSVQVEAVEGGALQKLLTLLATQRPMTVKKKVLFAVASLLRHFPFAQSHFLKLGGVQVLSELFQTPGAEAMRVRIITVLYDMIIEKELISQVGLDIIPDSSHQERLRQYAEVSLLPVLVEQGWCRLVPELLESPEHDWREKALRTLLAMMAQCQTQFKQNAGLTASLSELQKQYQELVLTEQDVGEEDGYFGEILTLVDSMVVKMRQV
Protein: Malate synthase 2 (EC 2.3.3.9) (Degradation of allantoin protein 7) (P21826)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Allantoin metabolism-specific malate synthase involved in the recycling the glyoxylate generated during allantoin degradation by the ureidoglycollate (UG) hydrolase reaction.
Subcellular location: Peroxisome matrix {ECO:0000269|PubMed:27678487}. Note=Imported in peroxisome via recognition by the peroxisomal targeting signal receptor PEX9. {ECO:0000269|PubMed:27678487}.
Interaction partners:
- Mitochondrial 2-methylisocitrate lyase ICL2
- Isocitrate lyase
- Citrate synthase, peroxisomal
- Acetyl-coenzyme A synthetase 1
- Citrate synthase, mitochondrial
- Citrate synthase 3, mitochondrial
- NAD-dependent malic enzyme, mitochondrial
- Malate dehydrogenase, cytoplasmic
- Malate dehydrogenase, peroxisomal
- Fumarate hydratase, mitochondrial
Sequence:
MVKISLDNTALYADIDTTPQFEPSKTTVADILTKDALEFIVLLHRTFNSTRKQLLANRSNLQSKLDSGEYRFDFLPETEQIRNDPTWQGAIPAPGLINRSSEITGPPLRNMLVNALNAEVTTYMTDFEDSSSPTWENMIYGQVNLYDAIRNQIDFKTPRKEYRLKDDISRLPTLIVRPRGWHMVEKHLYIDDEPISASIFDFGLYFYHNAKELVKIGKGPYFYLPKMEHHMEVKLWNDIFCVAQDFIGMPRGTIRATVLIETLPAAFQMEEIIYQIREHSSGLNCGRWDYIFSTIKKLRNLPEHVLPNRDLVTMTSPFMDAYVKRLINTCHRRGVHAMGGMAAQIPIKDDPKANEAAMNKVRNDKIREMKNGHDGSWVAHPALAPICNEVFSNMGTANQIYFVPDVHVTSSDLLNTKIQDAQVTTEGIRVNLDIGLQYMEAWLRGSGCVPINHLMEDAATAEVSRCQLYQWVKHGVVLSDTGDKVTPELTAKILNEETAKLASASPLGEKNKFALAAKYFLPEVTGKIFSDFLTTLLYDEIIKPSAKPVDLSKL
Protein: Crossover junction endonuclease EME1 (EC 3.1.22.-) (MMS4 homolog) (hMMS4) (Q96AY2)
Organism: Homo sapiens (Human)
Function: Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14617801}. Note=Recruited to regions of DNA damage in S-phase cells.
Interaction partners:
- Structure-specific endonuclease subunit MUS81
- Structure-specific endonuclease subunit SLX4
- Structure-specific endonuclease subunit SLX1
- Structure-specific endonuclease subunit EME2
- DNA repair endonuclease XPF
- DNA excision repair protein ERCC-1
- Flap endonuclease GEN homolog 1
- Exonuclease 1
- DNA repair protein RAD51 homolog 1
- Breast cancer type 1 susceptibility protein
Sequence:
MALKKSSPSLDSGDSDSEELPTFAFLKKEPSSTKRRQPEREEKIVVVDISDCEASCPPAPELFSPPVPEIAETVTQTQPVRLLSSESEDEEEFIPLAQRLTCKFLTHKQLSPEDSSSPVKSVLDHQNNEGASCDWKKPFPKIPEVPLHDTPERSAADNKDLILDPCCQLPAYLSTCPGQSSSLAVTKTNSDILPPQKKTKPSQKVQGRGSHGCRQQRQARQKESTLRRQERKNAALVTRMKAQRPEECLKHIIVVLDPVLLQMEGGGQLLGALQTMECRCVIEAQAVPCSVTWRRRAGPSEDREDWVEEPTVLVLLRAEAFVSMIDNGKQGSLDSTMKGKETLQGFVTDITAKTAGKALSLVIVDQEKCFSAQNPPRRGKQGANKQTKKQQQRQPEASIGSMVSRVDAEEALVDLQLHTEAQAQIVQSWKELADFTCAFTKAVAEAPFKKLRDETTFSFCLESDWAGGVKVDLAGRGLALVWRRQIQQLNRVSLEMASAVVNAYPSPQLLVQAYQQCFSDKERQNLLADIQVRRGEGVTSTSRRIGPELSRRIYLQMTTLQPHLSLDSAD
Protein: Vascular cell adhesion protein 1 (V-CAM 1) (VCAM-1) (CD antigen CD106) [Cleaved into: Soluble Vascular Cell Adhesion Molecule-1] (P29534)
Organism: Rattus norvegicus (Rat)
Function: Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with integrin alpha-4/beta-1 (ITGA4/ITGB1) on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/ITGA4/ITGB1 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation.
Subcellular location: [Vascular cell adhesion protein 1]: Cell membrane {ECO:0000250|UniProtKB:P19320}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P19320}.; SUBCELLULAR LOCATION: [Soluble Vascular Cell Adhesion Molecule-1]: Secreted {ECO:0000250|UniProtKB:P19320}.
Interaction partners:
- Integrin alpha-4
- Integrin beta-1
- Integrin beta
- Integrin alpha-D
- Intercellular adhesion molecule 1
- CD44 antigen
- Integrin alpha-9
- Moesin
- Ezrin
- NADPH oxidase 2
Sequence:
MPVKMVAIFGASTVLWILFAVSQAFKIEISPEYKTLAQIGDSMLLTCSTTGCESPSFSWRTQIDSPLNGKVKTEGAKSVLTMDPVSFENEHSYLCTATCNSGKLERGIQVDIYSFPKDPEIQFSGPLEVGKPVMVKCLAPDVYPIDRLEIELFKGDRLMKKQDFVDEMAKKSLETKSLEVIFTPVIEDIEKALVCRAKLYIDQTDSIPKERETVRELQVYTSPKNTEISVHPSTRLHEGAAVTMTCASEGLPAPEIFWSKKLDNGVLQLLSGNATLTLIAMRMEDSGIYVCEGVNLVGRDKTEVELIVQEKPFTVDISPGSQVAAQVGDSVVLTCAAVGCDSPSFSWRTQTDSPLNGEVRDEGATSTLTLSPVGVEDEHSYLCTVTCQRRKLEKTIQVEVYSFPEDPEIEISGPLVHGRPVTVNCTVPNVYPFDHLEIELLKGETTLLNKFLREEIGTKSLETKSLEMTFIPTAEDTGKALVCLAKLHSSQMESEPKQRQSTQTLYVNVAPKEPTIWVSPSPVPEEGSPVNLTCSSDGFPTPKILWSRQLKNGELQPLSQNTTLSFMATKMEDSGIYVCEGINEAGISKKSVELIIQGSSKDIQLTVFPSKSVKEGDTVIISCTCGSVPEIWIILKKKAKTGDMVLKSVNGSYTIRKAQLQDAGVYECESKTEVGSQLRSLTLDVKGKENNKDYFSPELLALYFASSLVIPAIGMIIYFARKANMKGSYSLVEAQKSKV
Protein: Lanosterol 14-alpha demethylase (LDM) (EC 1.14.14.154) (Cytochrome P450 family member 51) (CYP51) (Sterol 14-alpha demethylase) (Q1JPY5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q64654}; Single-pass membrane protein {ECO:0000255}. Membrane {ECO:0000305|PubMed:24361620}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Terpene cyclase/mutase family member
- Transmembrane 7 superfamily member 2.
- Squalene synthase
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- 24-dehydrocholesterol reductase.
- NAD
- Lamin B receptor.
- Hydroxymethylglutaryl-CoA synthase
- Phosphoethanolamine methyltransferase.
- 7-dehydrocholesterol reductase
Sequence:
MTILEVGSQLIESAVLQMSLTSVLLTASVFTLTLGYFSKLLFTQHSSEHTKYPPHIPSSLPFLGQAVAFGRSPIEFLEKAYEQYGPVVSFTMVGKTFTYLLGSDAAALMFNSKNEDLNAEDVYARLTTPVFGKGVAYDVPNPLFLEQKKMLKTGLNIAQFKQHVEIIEEETKDYFRRWGESGERNLFDALSELIILTASRCLHGCEIRSLLDERVAQLYADLDGGFTHAAWLLPGWLPLPSFRRRDRAHLEIKKIFYNVIKKRREDTEKHDDILQTLIDATYKDGRPLSDDEIAGMLIGLLLAGQHTSSTTSAWMGFFLARDRALQERCYSEQKSVCGEELPPLHYDQLKDLSLLDRCLKETLRLRPPIMTMMRMAKTPQKVGEYTIPPGHQVCVSPTVNHRLQDTWAERLDFDPDRYLHDNPAAGEKFAYIPFGAGRHRCIGENFAYVQIKTIWSTLLRMFDFELVDGHFPPVNYTTMIHTPHNPIIRYTRRNTQPQQ