wanglab/gogpt-training-data huggingface dataset:
Protein: Non-structural maintenance of chromosomes element 1 (Non-SMC element 1) (EC 2.3.2.27) (Q07913)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks.
Subcellular location: Nucleus {ECO:0000269|PubMed:11927594}.
Interaction partners:
- Non-structural maintenance of chromosome element 3
- E3 SUMO-protein ligase MMS21
- Structural maintenance of chromosomes protein 5
- Non-structural maintenance of chromosome element 4
- Structural maintenance of chromosomes protein 6
- DNA repair protein KRE29
- Non-structural maintenance of chromosome element 5
- Altered inheritance of mitochondria protein 46, mitochondrial
- Altered inheritance of mitochondria protein 18, mitochondrial
- Cell wall protein SED1
Sequence:
MEVHEEQVSAPVTGDATAKYLLQYILSARGICHENALILALMRLETDASTLNTEWSIQQWVDKLNDYINAINVKLNLLGYKIIRINHGIGRNAVTLKAKQNFESFEDNTAIRAHNNDYAVLQSIVLPESNRFFVYVNLASTEETKLATRFNQNEIEFMKWAIEQFMISGETIVEGPALETSIIVKEVNRILVAATGDSNLAKWRKFSTFTVGSTNLFQFQELTATDIEDLLLRLCELKWFYRTQEGKFGIDLRCIAELEEYLTSMYNLNTCQNCHKLAIQGVRCGNESCREENEETGENSLSQIWHVDCFKHYITHVSKNCDRCGSSLITEGVYVI
Protein: Endothelin-1 receptor (Endothelin receptor type A) (B3DLG5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Endothelin 1.
- Endothelin-3
- END domain-containing protein.
- Endothelin 2
- Endothelin-3a
- Guanine nucleotide-binding protein subunit alpha
- Guanine nucleotide-binding protein
- G-protein alpha 13a, alpha 13a)
- G-protein alpha 12 alpha 12) alpha 12a)
- Guanine nucleotide-binding protein subunit alpha
Sequence:
MAITTLQLFLLMAVLATGGLCLINGTEEAQDALYPNSTTSKTNVHKGFQPPTKKDASVFNMKHPPCRDPTSIKLYFKYINTIISCIVFVVGIVGNATLLKIIYQNKCMRNGPNALIASLALGDLIYITIDIPINVYKLLVTKWPFDDSSFGLFLCKLVPFLQKASVGITVLNLCALSVDRYRAVASWSRVQGVGVPLLTAIEIFSIWVLSIILAVPEAMVFNMITFTYNNQTIRTCMLKPETDFMNFYVYWKDWWLFGFYFCVPLACTAIFYTLMTCEMLHHRDGSLRIALSEHLKQRREVAKAVFCLVLIFALCWFPLHLSRLLKKMVYVPNDERRCDLLNFLLIMDYFGINLATVNSCINPIILYFVSKKFKNCFKSCLCCWCYSNNQVSSSGPVNGTSIQCKNHEPGNLYTDRVRKYSD
Protein: UDP-glucuronosyltransferase 1A10 (UGT1A10) (EC 2.4.1.17) (UDP-glucuronosyltransferase 1-10) (UDPGT 1-10) (UGT1*10) (UGT1-10) (UGT1.10) (UDP-glucuronosyltransferase 1-J) (UGT-1J) (UGT1J) (Q9HAW8)
Organism: Homo sapiens (Human)
Function: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile. Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds. Catalyzes the glucuronidation of endogenous estrogen hormones such as estradiol, estrone and estriol. Also catalyzes the glucuronidation of the isoflavones genistein, daidzein, glycitein, formononetin, biochanin A and prunetin, which are phytoestrogens with anticancer and cardiovascular properties. Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist losartan, caderastan and zolarsatan, drugs which can inhibit the effect of angiotensin II.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:17179145}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- UDP-glucuronosyltransferase 1A1
- UDP-glucuronosyltransferase 1A8
- UDP-glucuronosyltransferase 1A3
- UDP-glucuronosyltransferase 1A9
- UDP-glucuronosyltransferase 1A6
- UDP-glucuronosyltransferase 1A7
- UDP-glucuronosyltransferase 1A4
- Cytochrome P450 3A4)
- UDP-galactose translocator
- Cytochrome P450 1A1
Sequence:
MARAGWTSPVPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMPEVSWQLERSLNCTVKTYSTSYTLEDQNREFMVFAHAQWKAQAQSIFSLLMSSSSGFLDLFFSHCRSLFNDRKLVEYLKESSFDAVFLDPFDTCGLIVAKYFSLPSVVFTRGIFCHHLEEGAQCPAPLSYVPNDLLGFSDAMTFKERVWNHIVHLEDHLFCQYLFRNALEIASEILQTPVTAYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Protein: Cilia-and flagella-associated protein 96 (A7E2U8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:25074808}.
Interaction partners:
- Cilia- and flagella-associated protein 184
Sequence:
MPAEGGKTDMERIGLFSEMEYITVGDKYVSQFNRPFNEAASKNKQMLPGGSKEMSDLQAGYFDPHFVRIFEGEGYINLNQVRRRDMVEAAKKNLGKAFLPSNGEKKPCGLGSYYGTIGGPVPFFSAQSKPREKYKAPGKNLYTNPGKKGTGYGYANITIGKQFSHSADFYDAAKLKYKKANEEHHRLLKGAPFKLNLHPRDYFDANPYFSEESLPPIKKEEKKKTISNTFKPSSPGKKPGGMKAGTFDPYPSHSADPYVAKLANISGKDDKIFHPPSGPKSRPVESIMTLNVRRALNSKNYKTSSVPSY
Protein: Protein sprouty homolog 4 (Spry-4) (Q9C004)
Organism: Homo sapiens (Human)
Function: Suppresses the insulin receptor and EGFR-transduced MAPK signaling pathway, but does not inhibit MAPK activation by a constitutively active mutant Ras. Probably impairs the formation of GTP-Ras. Inhibits Ras-independent, but not Ras-dependent, activation of RAF1. Represses integrin-mediated cell spreading via inhibition of TESK1-mediated phosphorylation of cofilin.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12027893, ECO:0000269|PubMed:15584898}. Cell projection, ruffle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Found in the cytoplasm in unstimulated cells but is translocated to the membrane ruffles in cells stimulated with EGF (epidermal growth factor) (By similarity). Colocalizes with TESK1 in vesicular spots in the cytoplasm (PubMed:15584898). {ECO:0000250|UniProtKB:Q9WTP2, ECO:0000269|PubMed:15584898}.
Interaction partners:
- Dual specificity testis-specific protein kinase 1
- Interleukin-17 receptor D
- RAF proto-oncogene serine/threonine-protein kinase
- Dual specificity protein phosphatase 6
- Fibroblast growth factor 8
- Sprouty-related, EVH1 domain-containing protein 2
Sequence:
MEPPIPQSAPLTPNSVMVQPLLDSRMSHSRLQHPLTILPIDQVKTSHVENDYIDNPSLALTTGPKRTRGGAPELAPTPARCDQDVTHHWISFSGRPSSVSSSSSTSSDQRLLDHMAPPPVADQASPRAVRIQPKVVHCQPLDLKGPAVPPELDKHFLLCEACGKCKCKECASPRTLPSCWVCNQECLCSAQTLVNYGTCMCLVQGIFYHCTNEDDEGSCADHPCSCSRSNCCARWSFMGALSVVLPCLLCYLPATGCVKLAQRGYDRLRRPGCRCKHTNSVICKAASGDAKTSRPDKPF
Protein: Uncharacterized protein Rv2895c (P9WL31)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein
- UPF0102 protein Rv2898c
- Uncharacterized protein Rv2897c
- Putative DNA processing protein DprA
- Tyrosine recombinase XerC
- Phenyloxazoline synthase MbtB
Sequence:
MAGRPLHAFEVVATRHLAPHMVRVVLGGSGFDTFVPSDFTDSYIKLVFVDDDVDVGRLPRPLTLDSFADLPTAKRPPVRTMTVRHVDAAAREIAVDIVLHGEHGVAGPWAAGAQRGQPIYLMGPGGAYAPDPAADWHLLAGDESAIPAIAAALEALPPDAIGRAFIEVAGPDDEIGLTAPDAVEVNWVYRGGRADLVPEDRAGDHAPLIEAVTTTAWLPGQVHVFIHGEAQAVMHNLRPYVRNERGVDAKWASSISGYWRRGRTEEMFRKWKKELAEAEAGTH
Protein: DNA-binding transcriptional regulatory protein KdgR (E0SDE6)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Interaction partners:
- Urea carboxylase
Sequence:
MAIADLDKQPDSVSSVLKVFGILQALGEEREIGITELSQRVMMSKSTVYRFLQTMKSLGYVAQEGESEKYSLTLKLFELGAKALQNVDLIRSADIQMRELSALTRETIHLGALDEDSIVYIHKIDSMYNLRMYSRIGRRNPLHSTAIGKVLLAWRDREEVKEILSQVEFKRSTVHTIGSTEELLPQLDLVRQQGYGEDNEEQEEGLRCIAVPVFDRFGVVIAGLSISFPTIRFSEDNKHEYVAMLHTAARNISDQMGYHDYPF
Protein: Peptidyl-prolyl cis-trans isomerase FKBP7 (PPIase FKBP7) (EC 5.2.1.8) (23 kDa FK506-binding protein) (23 kDa FKBP) (FKBP-23) (FK506-binding protein 7) (FKBP-7) (Rotamase) (Q9Y680)
Organism: Homo sapiens (Human)
Function: PPIases accelerate the folding of proteins during protein synthesis.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
Sequence:
MPKTMHFLFRFIVFFYLWGLFTAQRQKKEESTEEVKIEVLHRPENCSKTSKKGDLLNAHYDGYLAKDGSKFYCSRTQNEGHPKWFVLGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGYAEGKIPPDATLIFEIELYAVTKGPRSIETFKQIDMDNDRQLSKAEINLYLQREFEKDEKPRDKSYQDAVLEDIFKKNDHDGDGFISPKEYNVYQHDEL
Protein: Leukocyte cell-derived chemotaxin-2 (LECT-2) (Chondromodulin II) (ChM-II) (O88803)
Organism: Mus musculus (Mouse)
Function: Has a neutrophil chemotactic activity. Also a positive regulator of chondrocyte proliferation.
Subcellular location: Secreted {ECO:0000250|UniProtKB:O14960}.
Interaction partners:
- Plasminogen
- Solute carrier organic anion transporter family member 1B2
- CD209 antigen-like protein A
- Tyrosine-protein kinase receptor Tie-1
Sequence:
MIPTTILISAALLSSALAGPWANICASKSSNEIRTCDSYGCGQYSAQRTQRHHPGVDVLCSDGSVVYAPFTGKIVGQEKPYRNKNAINDGIRLSGRGFCVKIFYIKPIKYKGSIKKGEKLGTLLPLQKIYPGIQSHVHVENCDSSDPTAYL
Protein: Peripherin (P15331)
Organism: Mus musculus (Mouse)
Function: Class-III neuronal intermediate filament protein (By similarity). May form an independent structural network without the involvement of other neurofilaments or may cooperate with the neuronal intermediate filament proteins NEFL, NEFH, NEFM and INA to form filamentous networks. Assembly of the neuronal intermediate filaments may be regulated by RAB7A. Plays a role in the development of unmyelinated sensory neurons. May be involved in axon elongation and axon regeneration after injury (By similarity). Inhibits neurite extension in type II spiral ganglion neurons in the cochlea.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10426285, ECO:0000269|PubMed:15322088, ECO:0000269|PubMed:18709437, ECO:0000269|PubMed:20132868, ECO:0000269|PubMed:22723690, ECO:0000269|PubMed:23179371, ECO:0000269|PubMed:9971739}. Cell projection, axon {ECO:0000269|PubMed:17899157, ECO:0000269|PubMed:18709437, ECO:0000269|PubMed:20132868, ECO:0000269|PubMed:22723690, ECO:0000269|PubMed:23179371}. Perikaryon {ECO:0000269|PubMed:17899157, ECO:0000269|PubMed:18709437, ECO:0000269|PubMed:20132868}.
Interaction partners:
- Neurofilament light polypeptide
- Neurofilament medium polypeptide
- Neurofilament heavy polypeptide
Sequence:
MPSSASMSHHHSSGLRSSISSTSYRRTFGPPPSLSPGAFSYSSSSRFSSSRLLGSGSPSSSARLGSFRAPRAGALRLPSERLDFSMAEALNQEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLCQQELRELRRELELLGRERDRVQVERDGLAEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQQVEVEATVKPELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESRISVPVHSFASLSLKTTVPEMEPLQDSHSKKMVLIRTIETRDGEKVVTESQKEQHSDLDKSSIHSY
Protein: Tehao (Q58SL7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
FCLGLXPQXTCAAEGNVVRFHCPDEYAMLLEVSEPGASLYMSYYASTELQWLPRFNISSLVXIXFDAYIFWPEKFLSDLLKTLGVQTVKTIIFRDRTLETVVTRDVLNSGNGYMETSQPENITTWHFGSVPGLKKFKFFSHVPELQESIFHGFDTLRDLHLSVNVTTLPGNMLSTVNGTLKTLTIESPGIVSFGNPLLRELQQLRNLSLALIHPFHERDKQLQPHFFGSMTNLEEVRLASATSSVNRSMFKGTNKLQLIKMNGNDDLMELPGEIFLDQVNLKTLDLSCNAIVTLHEDVFKGLGNLTLLDLSKNRLTNLS
Protein: NALCN channel auxiliary factor 1 (Transmembrane protein FAM155A) (B1AL88)
Organism: Homo sapiens (Human)
Function: Auxillary component of the NALCN sodium channel complex, a channel that regulates the resting membrane potential and controls neuronal excitability.
Subcellular location: Cell membrane {ECO:0000269|PubMed:32494638}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sodium leak channel NALCN
- Protein unc-79 homolog
- Protein unc-80 homolog
- Calmodulin-1
Sequence:
MTRGAWMCRQYDDGLKIWLAAPRENEKPFIDSERAQKWRLSLASLLFFTVLLSDHLWFCAEAKLTRARDKEHQQQQRQQQQQQQQQRQRQQQQQQRRQQEPSWPALLASMGESSPAAQAHRLLSASSSPTLPPSPGDGGGGGGKGNRGKDDRGKALFLGNSAKPVWRLETCYPQGASSGQCFTVENADAVCARNWSRGAAGGDGQEVRSKHPTPLWNLSDFYLSFCNSYTLWELFSGLSSPNTLNCSLDVVLKEGGEMTTCRQCVEAYQDYDHHAQEKYEEFESVLHKYLQSEEYSVKSCPEDCKIVYKAWLCSQYFEVTQFNCRKTIPCKQYCLEVQTRCPFILPDNDEVIYGGLSSFICTGLYETFLTNDEPECCDVRREEKSNNPSKGTVEKSGSCHRTSLTVSSATRLCNSRLKLCVLVLILLHTVLTASAAQNTAGLSFGGINTLEENSTNEE
Protein: Peptidoglycan-N-acetylglucosamine deacetylase (Peptidoglycan GlcNAc deacetylase) (EC 3.5.1.104) (Peptidoglycan N-deacetylase) (PG N-deacetylase) (Q8DP63)
Organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Function: Catalyzes the deacetylation of N-acetylglucosamine (GlcNAc) residues in peptidoglycan, a modification that confers host lysozyme resistance and contributes to pneumococcal virulence.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Glycosyltransferase 2-like domain-containing protein
Sequence:
MNKSRLGRGRHGKTRHVLLALIGILAISICLLGGFIAFKIYQQKSFEQKIESLKKEKDDQLSEGNQKEHFRQGQAEVIAYYPLQGEKVISSVRELINQDVKDKLESKDNLVFYYTEQEESGLKGVVNRNVTKQIYDLVAFKIEETEKTSLGKVHLTEDGQPFTLDQLFSDASKAKEQLIKELTSFIEDKKIEQDQSEQIVKNFSDQDLSAWNFDYKDSQIILYPSPVVENLEEIALPVSAFFDVIQSSYLLEKDAALYQSYFDKKHQKVVALTFDDGPNPATTPQVLETLAKYDIKATFFVLGKNVSGNEDLVKRIKSEGHVVGNHSWSHPILSQLSLDEAKKQITDTEDVLTKVLGSSSKLMRPPYGAITDDIRNSLDLSFIMWDVDSLDWKSKNEASILTEIQHQVANGSIVLMHDIHSPTVNALPRVIEYLKNQGYTFVTIPEMLNTRLKAHELYYSRDE
Protein: Aspartoacylase (EC 3.5.1.15) (Aminoacylase-2) (ACY-2) (Q8R3P0)
Organism: Mus musculus (Mouse)
Function: Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9R1T5}. Nucleus {ECO:0000250|UniProtKB:Q9R1T5}.
Interaction partners:
- N-acetylaspartate synthetase
- Glutamate carboxypeptidase 2
- Isoaspartyl peptidase/L-asparaginase
- Aspartate aminotransferase, cytoplasmic
- Beta-citrylglutamate synthase B
- N-acetylaspartylglutamate synthase A
- Putative aspartate aminotransferase, cytoplasmic 2
- Argininosuccinate synthase
- Asparagine synthetase
- Aspartate aminotransferase, mitochondrial
Sequence:
MTSCVAKEPIKKIAIFGGTHGNELTGVFLVTHWLRNGTEVHRAGLDVKPFITNPRAVEKCTRYIDCDLNRVFDLENLSKEMSEDLPYEVRRAQEINHLFGPKNSDDAYDLVFDLHNTTSNMGCTLILEDSRNDFLIQMFHYIKTCMAPLPCSVYLIEHPSLKYATTRSIAKYPVGIEVGPQPHGVLRADILDQMRKMIKHALDFIQHFNEGKEFPPCSIDVYKIMEKVDYPRNESGDMAAVIHPNLQDQDWKPLHPGDPVFVSLDGKVIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTKLTLSAKSIRSTLH
Protein: t-SNARE coiled-coil homology domain-containing protein (Q2UJN0)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
Interaction partners:
- V-SNARE coiled-coil homology domain-containing protein
- t-SNARE coiled-coil homology domain-containing protein
- Soluble NSF attachment protein
- t-SNARE coiled-coil homology domain-containing protein
- t-SNARE coiled-coil homology domain-containing protein
- Protein transport protein SEC22
- t-SNARE affecting a late Golgi compartment protein 1
- Pep3/Vps18/deep orange beta-propeller domain-containing protein
- Synaptobrevin homolog YKT6
- E3 ubiquitin-protein ligase PEP5
Sequence:
MSNPLDTDAGSELFSSYEAELKLIQADLNQTLDQIAESSGEQRKSTIRKAEQVLDEATELLDQMRMEKQNIPSAARSKVNARFRNYATDLDESKRKLKSLSDDRKALFGDRYTDDPQDVHLEQRQQLLSGTDRLERSSARLQESQRIALETEDIGRNTLADLNTQRETIMNTRSNLQQSEGYVDTSIKTLRGMARRMATNRIITIAIITVLVLLIIAVIYSKFH
Protein: Protein DLS1 (DPB3-like subunit of ISW2 complex 1) (P40366)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as component of the ISW2 complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW2 complex is involved in coordinating transcriptional repression and in inheritance of telomeric silencing. It is involved in repression of MAT a-specific genes, INO1, and early meiotic genes during mitotic growth dependent upon transcription factor UME6 and in a parallel pathway to the RPD3-SIN3 histone deacetylase complex. DLS1 is partially required for the ISW2 complex chromatin remodeling activity and is not required for its interaction with chromatin.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Imitation switch two complex protein 1
- DNA polymerase epsilon subunit D
- ISWI chromatin-remodeling complex ATPase ISW2
- ISWI one complex protein 2
- DNA polymerase epsilon subunit B
- ISWI one complex protein 4
- DNA polymerase epsilon catalytic subunit A
- ISWI one complex protein 3
- DNA polymerase epsilon subunit C
- ISWI chromatin-remodeling complex ATPase ISW1
Sequence:
MNNETSGKETASAPLCSPKLPVEKVQRIAKNDPEYMDTSDDAFVATAFATEFFVQVLTHESLHRQQQQQQQQVPPLPDELTLSYDDISAAIVHSSDGHLQFLNDVIPTTKNLRLLVEENRVRYTTSVMPPNEVYSAYVVNDTAPKPNIVEIDLDNDEDDDEDVTDQE
Protein: Homogentisate 1,2-dioxygenase (HGDO) (EC 1.13.11.5) (Homogentisate oxygenase) (Homogentisic acid oxidase) (Homogentisicase) (Q88E47)
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Function: Involved in the catabolism of homogentisate (2,5-dihydroxyphenylacetate or 2,5-OH-PhAc), a central intermediate in the degradation of phenylalanine and tyrosine. Catalyzes the oxidative ring cleavage of the ar omatic ring of 2,5-dihydroxyphenylacetate to yield maleylacetoacetate.
Interaction partners:
- Maleylacetoacetate isomerase
- fumarylacetoacetase
- 4-hydroxyphenylpyruvate dioxygenase
- 3-dehydroshikimate dehydratase
- Phenylalanine-4-hydroxylase
- Fumarylacetoacetate hydrolase family protein
- Hmg transcriptional repressor
- Fumarylacetoacetate hydrolase family protein
- Aminotransferase
- 4-hydroxybenzoate 3-monooxygenase
Sequence:
MNRDTSPDLHYLSGFGNEFASEALPGALPVGQNSPQKAPYGLYAELLSGTAFTMARSELRRTWLYRIRPSALHPRFERLARQPLGGPLGGINPNRLRWSPQPIPAEPTDFIEGWLPMAANAGAEKPAGVSIYIYRANRSMERVFFNADGELLLVPEQGRLRIATELGVMEVEPLEIAVIPRGMKFRVELLDGQARGYIAENHGAPLRLPDLGPIGSNGLANPRDFLTPVAHYEEAEGPVQLVQKFLGEHWACELQHSPLDVVAWHGSNVPYKYDLRRFNTIGTVSFDHPDPSIFTVLTSPTSVHGMANMDFVIFPPRWMVAENTFRPPWFHRNLMNEFMGLINGAYDAKAEGFLPGGASLHGVMSAHGPDAETCEKAIAADLAPHKIDNTMAFMFETSQVLRPSLQALECPQLQADYDSCWATLPSTFNPNRR
Protein: Replication protein (Q52546)
Organism: Pseudomonas syringae
Interaction partners:
Sequence:
MMVENKVTQSNKLIESSHTLTLNEKRLVLCAASLIDSRKPLPKDGYLTIRADTFAEVFGIDVKHAYAALDDAATKLFNRDIRRYVKGKVVERMRWVFHVKYREGQGCVELGFSPTIIPHLTMLHKEFTSYQLKQIGSLSSFYAVRLYELMSQFIKLKQRECTLAQLREMFDLGDKYQDVKDMRKRVLYPALEEVNKNTDLTVAVEPRRQGRRIIGFSFTIAKNDQLALSLE
Protein: Large ribosomal subunit protein uL11 (60S ribosomal protein L12) (P23358)
Organism: Rattus norvegicus (Rat)
Function: Binds directly to 26S ribosomal RNA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P30050}.
Interaction partners:
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL4
- Ubiquitin-ribosomal protein eL40 fusion protein
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein eS17
Sequence:
MPPKFDPNEIKVVYLRCTGGEVGATSALAPKIGPLGLSPKKVGDDIAKATGDWKGLRITVKLTIQNRQAQIEVVPSASALIIKALKEPPRDRKKQKNIKHNGNITFDEIVNIARQMRHRSLARELSGTIKEILGTAQSVGCNVDGRHPHDIIDDINSGAVECPAS
Protein: Small ribosomal subunit protein mS29 (V9GYA7)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
XGSPLGEVVEQGITRVRNATDAVGIVLKELKRQSSLGMFHLLVAVDGINALWGRTTLKREDKSPIAPEELALVHNLRKMMKNDWHGGAIVSALSQTGSLFKPRKAYLPQELLGKGFTTWPRLVWNSWAQAICPSQPPKVLGLQEGFDALDPFIPILVSNYNPKEFESCIQYYLENNWLQHEKAPTEEGKKELLFLSNANPSLLERHCAYL
Protein: Cation/calcium exchanger 5 (Protein CATION EXCHANGER 11) (O04034)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Membrane-localized H(+)-dependent K(+) and Na(+) transporter.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21945443}; Multi-pass membrane protein {ECO:0000269|PubMed:21945443}.
Interaction partners:
- Vacuolar cation/proton exchanger 1
- Vacuolar cation/proton exchanger 3
- Magnesium/proton exchanger
- Vacuolar cation/proton exchanger 4
- Vacuolar cation/proton exchanger 5
- Putative vacuolar cation/proton exchanger 6
- Vacuolar cation/proton exchanger 2
- Sodium/calcium exchanger NCL
- Uncharacterized protein
- Alpha carbonic anhydrase 2
Sequence:
MELISSSTIGNSALCLTLISILIFFFLTTTTIPTFPDHPLRSLLDDSQITTNSSSIVNPKSSCVSSRSHDNGGVINYFSLHYCIFNENLFFSIPILSLLILLHFYILIKTAQTHFSTVTTKLADRLNLSPSMAAVTLLALGNGAPDVFASVAALRGGQYRTGFGAILSAGTFVSAFVVGFVAIYAAPFPVDAASFVRDVLFYLIAALFLFYVYLSGEIFVWQAIGFVGFYIFFVGFVFWMDFGTNVEKGKSISEEEKDLLRLQDCEIAAGSLGSYKAEKEHQFSGIFRLYGTISRMWETPVSVLLNLTIPKPSPSEWSRFYRSANIVFCPFALLYTCNSFVQLNHPISFLFPNTHLPLWLVVLFMTSSLAFLHFTVEKQPPKTEQLPVIVVAFIMSVFWISTIAGELLNCLAALGTLLKLPPALLGLTVLAWGNSVGDLVADVAVAKAGRPAMAMAGCFAGPMFNMLVGLGSALVMQTANVYPDAYKLGFHVGIVIAFVFLLLSLMGSLLVITWSRFRVPRFWGICLVGLYVAFTFVSLIIASVST
Protein: S-methyl-5'-thioadenosine phosphorylase (EC 2.4.2.28) (5'-methylthioadenosine phosphorylase) (MTA phosphorylase) (MTAP) (MTAPase) (Q57XS4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03155}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03155}.
Interaction partners:
- Methylthioribose-1-phosphate isomerase
- Spermidine synthase, putative
- Nucleoside phosphorylase, putative
- GMP synthase
- Hypoxanthine phosphoribosyltransferase
- Hypoxanthine phosphoribosyltransferase
Sequence:
MMYTSPHDAPVLIGVIGGSGTYNLNAMQNVKKYTIPTPYGMPSGSISVATVSGVLCAFIPRHGYSHEFTPDEVNYRANIYALKLLGVKYLIGVNAVGSLDAEYQPGDMVLVDQLIDRTTGRRTTFFGEGIVAHVDYAYPLSANFRKLAHDTLTKAMGKLTTAVSGGKPWKLHNGATLVTMSGPQFSTRAESLINKSLNGHLIGMTTSTESKLAREAEMAYLVVAAVTDMDAWSDAPHVDAESVRKVMAANVEKVQLIVVELIAAVSANQFDDPAHHCLEYAVPTKPEAITKEVRQRIAPLMAKYPIFAP
Protein: Auxin-responsive protein IAA34 (Indoleacetic acid-induced protein 34) (Q9C5X0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Auxin-responsive protein IAA33
- Auxin response factor 22
- Auxin response factor 5
- Auxin response factor 1
- Auxin response factor 9
- Auxin response factor 12
- Putative auxin response factor 14
- Solute carrier family 35 protein
- Auxin response factor 7
- Auxin response factor 18
Sequence:
MYCSDPPHPLHLVASDKQQKDHKLILSWKKPTMDSDPLGVFPNSPKYHPYYSQTTEFGGVIDLGLSLRTIQHEIYHSSGQRYCSNEGYRRKWGYVKVTMDGLVVGRKVCVLDHGSYSTLAHQLEDMFGMQSVSGLRLFQMESEFCLVYRDEEGLWRNAGDVPWNEFIESVERLRITRRNDAVLPF
Protein: Meiotic drive suppressor wtf18 (O74495)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a suppressor component of the dual wtf meiotic drive system, and can suppress but not confer meiotic drive by compatible poisons. Wtf meiotic drive systems promote unequal transmission of alleles from the parental zygote to progeny spores by encoding a poison and an antidote from the same locus; the poison is trans-acting and forms toxic aggregates in all spores within an ascus, wherease the antidote is spore-specific and targets aggregates for degradation by the vacuole (By similarity). Meiotic drive by wtf systems therefore lead to poisoning of all progeny that do not inherit the dual poison/antidote allele, or express a compatible antidote.
Subcellular location: Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Wtf element wtf14
- Wtf element wtf11
Sequence:
MKNNYTSLKSPLDEEDELKTDHEIDLEKGLLPEYNSEEEGTLPLYSDISKLANPVPEDSSTGPTEIANPNVERRQEFKDSHPNIYFLLRLLISVLAVSVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPILFIATFCFFETWTQAVAQCIKVTVIFLAQCVKVTVIFLAQCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMECPGALKRMPKFIRNGIASFLEGIGNAFGGIGNAIGRIGNAFRGANDNNNNIPLEETEAESEV