wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein C63.05 (Q9Y7T1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Type 2A phosphatase activator tip41
- Serine/threonine-protein phosphatase ppe1
- Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- Minor serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Serine/threonine-protein kinase tor1
- Serine/threonine-protein kinase tor2
- Putative serine/threonine-protein phosphatase C26H8.05c
- Target of rapamycin complex subunit wat1
- Target of rapamycin complex 1 subunit mip1
- Serine/threonine-protein phosphatase 2A activator 1
Sequence:
MESKSLRELWEETEKLKDSSSTDEKTRSEIVEGYEKCLKLVLQLRIFSSNEEVDEIKTSELRYLMIDYELAKCVEQWTKGDRLKAVQYAKTHYETFLSICDDYGLKPMQDEKPKTEADTRTLKIARYRMRQNLEKELKALSKDSETNEEQERKFWLTKLQIAVEDTLDSLPHIEMEIDLLKRAQAELMKSEDSPEKDEETLRREERKQKEGSSWRLDLNTRDKILDKNNRPLQPFTIVSDRNETRKNVFGFGYNLPTMTVDEYLDEEMKRGNIISQKDNPPKSDSDDEDDYEKLDAKTMKDRYWDEFKEANPRGSGNTMVNRG
Protein: SCF-associated factor 1 (P38352)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Targets AAH1 adenine deaminase for proteasome-dependent degradation upon entry into quiescence. Targets also URA7.
Interaction partners:
- Adenine deaminase
- Cerevisin
- Cell division control protein 53
- Suppressor of kinetochore protein 1
- Vacuolar serine-type carboxypeptidase ATG42
- GTP-binding protein YPT1
Sequence:
MSEVESREKEPDAGLSPDIVQATLPFLSSDDIKNLSQTNKYYNTLLDFDHSKILWHELFHKAFGTLKTNDEPFQGRNSAEFKTCTETILREAFPTLSWQEVYQLRAYDAKFYSWGYLKHGRLGYTASSNNELVATSLNGPSPRFKYGVNTPTEVPWFNSRTTSRTSNFTPSEDPLSAIKKDGDEIIAQVSSGGFSFQILTESGNLYSSGSTFSGGLKGPGPSGSQHDYNPFREMIHNMERSYPRITSRSNGSTVNTTGTFSGRRMSGSHPSTAYEPGNATTAQHITIDSGGAPAASPGGSHSGVPRTTMPSMGPHENIYSQIEMLERSANKAVPGNNHIRRMFARNSFPLYSGRDENLGSFNDIQFVAVSSGRSHFLAMDTDNNIYSWDSTESDQGVKIEFANLPSRATNPILKIASGWNFNCCYIYKVGLVAWKERDAIQKGESFAFAKYEIVPNTNDVNGDSRIVDFACLQDNCVFFINNNGDKLWKYHNGLNQIVDLNIVGKLCKINACFASLVLFTDTHCYTLKVTNGDVDKDSLTELDINENVISVASGDYHTVALTERGHLYSWGIESQDCGCLGLGPSEKIVNELHIGNWEGQRNIRVVKPTKIELPEDYICVSVTAGGWQTGALIIKKH
Protein: UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase (UDP-Glc:Und-P Glc-1-P transferase) (EC 2.7.8.31) (Colanic acid biosynthesis UDP-glucose lipid carrier transferase) (Glucosyl-P-P-undecaprenol synthase) (P71241)
Organism: Escherichia coli (strain K12)
Function: Is the initiating enzyme for colanic acid (CA) synthesis. Catalyzes the transfer of the glucose-1-phosphate moiety from UDP-Glc onto the carrier lipid undecaprenyl phosphate (C55-P), forming a phosphoanhydride bond yielding to glucosyl-pyrophosphoryl-undecaprenol (Glc-PP-C55). Also possesses a weak galactose-1-P transferase activity.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:22408159}; Multi-pass membrane protein {ECO:0000269|PubMed:22408159}.
Interaction partners:
- Tyrosine-protein kinase wzc
- Lipopolysaccharide biosynthesis protein WzxC
- Putative colanic acid biosynthesis glycosyl transferase WcaI
- Mannose-1-phosphate guanylyltransferase
- Putative polysaccharide export protein Wza
- GDP-L-fucose synthase
- Putative colanic acid biosynthesis glycosyl transferase WcaA
- GDP-mannose 4,6-dehydratase
- Putative colanic acid biosynthesis glycosyl transferase WcaC
- Tyrosine-protein kinase etk
Sequence:
MTNLKKRERAKTNASLISMVQRFSDITIMFAGLWLVCEVSGLSFLYMHLLVALITLVVFQMLGGITDFYRSWRGVRAATEFALLLQNWTLSVIFSAGLVAFNNDFDTQLKIWLAWYALTSIGLVVCRSCIRIGAGWLRNHGYNKRMVAVAGDLAAGQMLMESFRNQPWLGFEVVGVYHDPKPGGVSNDWAGNLQQLVEDAKAGKIHNVYIAMQMCDGARVKKLVHQLADTTCSVLLIPDVFTFNILHSRLEEMNGVPVVPLYDTPLSGVNRLLKRAEDIVLATLILLLISPVLCCIALAVKLSSPGPVIFRQTRYGMDGKPIKVWKFRSMKVMENDKVVTQATQNDPRVTKVGNFLRRTSLDELPQFINVLTGGMSIVGPRPHAVAHNEQYRQLIEGYMLRHKVKPGITGWAQINGWRGETDTLEKMEKRVEFDLEYIREWSVWFDIKIVFLTVFKGFVNKAAY
Protein: Iroquois-class homeodomain protein irx-2 (Irx2-A) (Iroquois homeobox protein 2) (Xiro2) (Q6DCQ1)
Organism: Xenopus laevis (African clawed frog)
Function: Acts partially redundantly with other irx members in neural patterning. Required for formation of the posterior forebrain, midbrain, hindbrain, and to a lesser extent, spinal cord. Acts early in neural plate development to induce expression of some but not all proneural genes, and specify a neural precursor state. Also up-regulates repressors that prevent neuronal differentiation. Patterns the neuroectoderm in both the anterior/posterior and dorsal/ventral axes. Probably dispensable for pronephric kidney development.
Subcellular location: Nucleus {ECO:0000255, ECO:0000305}.
Interaction partners:
Sequence:
MSYPQGYLYQPPGSLALYSCPAYGASALAAPRSEELARSSSGSAFSPYPGSAAFSAQAATGFSSPLQYSSDPTGFPSYMGSPYDAHAAGMTGALSYHPYGSAAYPYQLNDPAYRKNATRDATATLKAWLQEHRKNPYPTKGEKIMLAIITKMTLTQVSTWFANARRRLKKENKMTWAPRNKSDDEDDDEGDGERVKEEQSEKAQDSNETSAEDEGISLHVDSLTDHSCSADSDGEKLPCRAADHLCESGSESKEKYEDEEDDGDEEDRVLPVKPATSSPLTGVEAPILNRQQEGSPRNSNKTNLDNGMSSSSQTPASKPKLWSLAEIATSDHKHPNLGSVLSSATSSSAAHNPSYPSSSLLGRHIYYTSPFYSNYTNYGNFNALQSQGILRYSSTAMTANEGLNQTVLSTSSMHKHTSDSVRTASNQLDQHYRPTNYESKKDPSEVCTVGVQPYP
Protein: Zinc finger CCHC domain-containing protein 17 (Nucleolar protein of 40 kDa) (pNO40) (Putative S1 RNA-binding domain protein) (PS1D protein) (Q9ESX4)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12202495, ECO:0000269|PubMed:12893261}.
Interaction partners:
- Nuclear cap-binding protein subunit 2
- Bystin
- Splicing factor 3B subunit 4
- WD repeat domain 36
- U3 small nucleolar ribonucleoprotein protein IMP3
- SR-related and CTD-associated factor 4
Sequence:
MNSGRPETMENLPALYTIFQGEVAMVTDYGAFIKIPGCRKQGLVHRTHMSSCRVDKPSEIVDVGDKVWVKLIGREMKNDRIKVSLSMKVVNQGTGKDLDPNNVVIEQEERRRRSFQDYTGQKITLEAVLNTTCKKCGCKGHFAKDCFMQPGGTKYSLIPEEEEEKEEAKAEGLEKPDPTKNSSRKRKKEKKKKKHRDRKSSDCDSSDSESDTGKKARHSSKDSKATKKKKKKKKHKKKHKE
Protein: Glutaredoxin domain-containing cysteine-rich protein 2 (GRXCR1-like protein) (Glutaredoxin domain-containing cysteine-rich protein 1-like protein) (A6NFK2)
Organism: Homo sapiens (Human)
Function: Could play a role in maintaining cochlear stereocilia bundles that are involved in sound detection.
Subcellular location: Cell projection, stereocilium {ECO:0000250|UniProtKB:Q3TYR5}. Note=Concentrated at the basal taper region of stereocilia in early postnatal development. In adult hair cells, concentrated at the basal region but also detected along the stereocilium shaft. {ECO:0000250|UniProtKB:Q3TYR5}.
Interaction partners:
- Chloride intracellular channel protein 5
- Taperin
- Rho family-interacting cell polarization regulator 2
- Unconventional myosin-VIIa
- Glutaredoxin domain-containing cysteine-rich protein 1
- Twinfilin-1
- Unconventional myosin-Ic
- Radixin
- Xin actin-binding repeat-containing protein 2
- Plastin-1
Sequence:
MEDPEKKLNQKSDGKPRKVRFKISSSYSGRVLKQVFEDGQELESPKEEYPHSFLQESLETMDGVYGSGEVPRPQMCSPKLTAQRISVFREGNAYTLAGGQPRFNDYKANDHKPLPIIDFGKIIIYTNNLKIIRTPMDKRDFVRKILQKEEEAEEESLMNKEESYGGRDQHDRPLVEAESTLPQNRYTQEGDIPEDSCFHCRGSGSATCSLCHGSKFSMLANRFKESYRALRCPACNENGLQPCQICNQ
Protein: Baramicin A2 [Cleaved into: Immune-induced peptide 24 (DIM-24) (DIM24) (IM24); Immune-induced peptide 10 (DIM-10) (DIM10) (IM10); Immune-induced peptide 12 (DIM-12) (DIM12) (IM12); Immune-induced peptide 13 (DIM-13) (DIM13) (IM13); Immune-induced peptide 22 (DIM-22) (DIM22) (IM22); Immune-induced peptide 5 (DIM-5) (DIM5) (IM5); Immune-induced peptide 6 (DIM-6) (DIM6) (IM6); Immune-induced peptide 8 (DIM-8) (DIM8) (IM8)] (C0HM00)
Organism: Drosophila melanogaster (Fruit fly)
Function: Secreted immune-induced peptides induced by Toll signaling. Has a significant role in resistance to infection by the entomopathogenic fungus B.bassiana R444 and weak antifungal activity against M.rileyi PHP1705. In adult males, activity appears to be important for neuromuscular processes that mediate correct wing posture upon Toll activation.
Subcellular location: [Immune-induced peptide 24]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 6]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 12]: Secreted {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 10]: Secreted {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851, ECO:0000269|PubMed:9736738}.; SUBCELLULAR LOCATION: [Immune-induced peptide 5]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 8]: Secreted {ECO:0000269|PubMed:34432851}.; SUBCELLULAR LOCATION: [Immune-induced peptide 13]: Secreted {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851, ECO:0000269|Ref.6}.; SUBCELLULAR LOCATION: [Immune-induced peptide 22]: Secreted {ECO:0000269|PubMed:34432851}.
Interaction partners:
Sequence:
MKSFGLIALAICGVICVAAEPQHTYDGRNGPHVFGSPGNQVYIRGQNEGTYSVPGVGGQFQNAPQRGEHVYTDEAGNTFVNRKNAGGPASHTISGPNFSAKNLGPNGAKSVGIPQRARRSPQFHVERPGRTVDVGNGGFYIQRGRRSPQLHVARPDRTVTIGNGGVYIQRSRRSPQFHVERPDRTVDFGNGGFSAQRFRRGINDARVQGENFVARDDQAGIWDNNVSVWKRPDGRTVTIDRNGHTIVSGRGRPAQHY
Protein: Aldehyde:ferredoxin oxidoreductase, tungsten-containing, putative (Q72E91)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Iron-sulfur cluster-binding protein
- Aldehyde:ferredoxin oxidoreductase, tungsten-containing
- Hydroxypyruvate reductase, putative
- Molybdopterin molybdenumtransferase
- DUF302 domain-containing protein
- Ribonuclease H
Sequence:
MTLRRWGMPIEGTASRVLHVDLESGASRVLLFEGRPHHLGGSGLAAALYDAYGLPESPAFDPRQPLIFAIGPLSGFFPLMSKVVCGFRSPYTGEWAESHAGGRLALSLRFAGYDALMITGRARTLSCLVVGSRRLEIHDVHYLRGQDVFTSGKYLRRYGKESSGHRSTVRIGPAGERGVTFACANVDSFRHFGRLGAGAVMGGKNLKALVVTGDSGIELPEGRDYPKLYKEVYQSVTGTDMMQKYHDLGTAENLLVLNELKALPWRNLQATTDPAIDGISGERFAEQLLLRQTACAGCPVGCIHIGLLRQQFARDHEFLYKQVSYDYEPIFAQGSMLGLTNASDVLALLDETEKLGLDCMSAGVALAWVAEAFEKGVVTEKETLGPVHFGNVATFVAALHHLANGTSEFWQALGKGVLYAADIYGGADFACVLGQEMAGYATGEVYFVSQALGFRHSHLDSGGYAYDQSAKDKDVDKAVRHLLDDEYKRLTINCMVACLFARKAYPPERLQEALASLGMRAEADALPESGRAMQALRWSLKFRTGFRPENVRIPKRFTEVVTWKGPMDVDYMDAVRQAYTSELYRMVVDAAREA
Protein: Carbohydrate-responsive element-binding protein (ChREBP) (MLX interactor) (MLX-interacting protein-like) (Williams-Beuren syndrome chromosomal region 14 protein homolog) (Q99MZ3)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor. Binds to the canonical and non-canonical E box sequences 5'-CACGTG-3'.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- MLX-interacting protein
- Max-like protein X
- Peroxisome proliferator-activated receptor gamma coactivator 1-beta
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- 14-3-3 protein beta/alpha
- Serine/threonine-protein phosphatase 2A activator
- Sterol regulatory element-binding protein 1
- Transducin beta-like protein 2
- Hormone-sensitive lipase
- Oxysterols receptor LXR-alpha
Sequence:
MARALADLSVNLQVPRVVPSPDSDSDTDLEDPSPRRSAGGLHRSQVIHSGHFMVSSPHSDSLTRRRDQEGPVGLADFGPRSIDPTLTHLFECLSLAYSGKLVSPKWKNFKGLKLLCRDKIRLNNAIWRAWYIQYVQRRKSPVCGFVTPLQGSEADEHRKPEAVILEGNYWKRRIEVVMREYHKWRIYYKKRLRKSSREGDFLAPKQVEGGWPPPERWCEQLFSSVVPVLLGGSEEEPGGRQLLDLDCFLSDISDTLFTMTQPSPSSLQLPPEDAYVGNADMIQPDLTPLQPSLDDFMEISDFFTNYRPPQTPTSSNYIESPSFGPMADSLFSSGILAPEMPSPASSSSSSGMTPHSGNTRLQARNSCSGPLDPNPFLSSEFLLPEDPKTKIPPAPGPTPLLPFPTPVKVHGLEPCTPSPFPTMAPPPSLLPEESLLSARFPFTSAPPAPGVSTLPAPTTFVPTPQPGPGPVPFSVDHLPHGYLEPVFGPHFTVPQGMQPRCKPSSPSPGGQKASPPTLASATASPTATATARDNNPCLTQLLRAAKPEQALEPPTMPGTLLRPPESPQDTVSEIPRARAFFPPIPAPTPPRPPPGPATLAPPRSLVVPKAERLSPPASSGSERRLSGDLNSIQPSGALSVHLSPPQTVLSRGRVDNNKMENRRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPSLKVSKATTLQKTAEYILMLQQERAAMQEEAQQLRDEIEELNAAINLCQQQLPATGVPITHQRFDQMRDMFDDYVRTRTLHNWKFWVFSILIRPLFESFNGMVSTASLHSLRQTSLAWLEQYCSLPALRPTVLNSLRQLSTSTSILTDPSLVPEQATRAVTEGTLGRPL
Protein: Sodium/potassium-transporting ATPase subunit beta (Q6NYH5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}. Membrane {ECO:0000256|RuleBase:RU362099}.
Interaction partners:
Sequence:
MPANKDGDGGWKSFIWNSDKKEFLGRTGCSWLKIFIFYVIFYGCLAGIFIGTIQAMLLTLSNYKPTYQDRVAPPGLSHSPRPDKAEINYNINDESTYLPYVNHIDAFLKAYNEDVQKDDTKFEECGDKPQFYTDRGELESDNGVRKACRFRREWLGECSGQKDEKLKNYGFDDGQPCLIVKLNRIVNFMPRPPASNDSIPEAVRPKLQGNVIPIHCSSKREEEANLLGQIKYFGLGTGFPLQYYPYYGKLLQPQYLQPLVAIKFYNITTDVDVRVECKVYGENIDYSEKDRSQGRFDIKFTIKTKS
Protein: Seripauperin-22 (P0CE87)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
Sequence:
MTNEGIGINRDTSTICLREYVFIHFFPVKLISALTNKTNTMVKLTSIAAGVAAIAAGVAAAPATTTLSPSDERVNLVELGVYVSDIRAHLAQYYLFQAAHPTETYPVEIAEAVFNYGDFTTMLTGIPAEQVTRVITGVPWYSTRLRPAISSALSKDGIYTAIPK
Protein: Prostaglandin E2 receptor EP1 subtype (PGE receptor EP1 subtype) (PGE2 receptor EP1 subtype) (Prostanoid EP1 receptor) (P35375)
Organism: Mus musculus (Mouse)
Function: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(q) proteins which activate a phosphatidylinositol-calcium second messenger system. May play a role as an important modulator of renal function. Implicated the smooth muscle contractile response to PGE2 in various tissues.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein subunit alpha-14
- Guanine nucleotide-binding protein G
Sequence:
MSPCGLNLSLADEAATCATPRLPNTSVVLPTGDNGTSPALPIFSMTLGAVSNVLALALLAQVAGRMRRRRSAATFLLFVASLLAIDLAGHVIPGALVLRLYTAGRAPAGGACHFLGGCMVFFGLCPLLLGCGMAVERCVGVTQPLIHAARVSVARARLALAVLAAMALAVALLPLVHVGRYELQYPGTWCFISLGPRGGWRQALLAGLFAGLGLAALLAALVCNTLSGLALLRARWRRRRSRRFRKTAGPDDRRRWGSRGPRLASASSASSITSATATLRSSRGGGSARRVHAHDVEMVGQLVGIMVVSCICWSPLLVLVVLAIGGWNSNSLQRPLFLAVRLASWNQILDPWVYILLRQAMLRQLLRLLPLRVSAKGGPTELGLTKSAWEASSLRSSRHSGFSHL
Protein: Iron-sulfur cluster co-chaperone protein HscB [Cleaved into: Iron-sulfur cluster co-chaperone protein HscB, mitochondrial (C-HSC20); Iron-sulfur cluster co-chaperone protein HscB, cytoplasmic] (Q8K3A0)
Organism: Mus musculus (Mouse)
Function: Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria. Required for incorporation of iron-sulfur clusters into SDHB, the iron-sulfur protein subunit of succinate dehydrogenase that is involved in complex II of the mitochondrial electron transport chain. Recruited to SDHB by interaction with SDHAF1 which first binds SDHB and then recruits the iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through direct binding to HSC20 (By similarity). Plays an essential role in hematopoiesis.
Subcellular location: [Iron-sulfur cluster co-chaperone protein HscB, cytoplasmic]: Cytoplasm {ECO:0000250|UniProtKB:Q8IWL3}.; SUBCELLULAR LOCATION: [Iron-sulfur cluster co-chaperone protein HscB, mitochondrial]: Mitochondrion {ECO:0000250|UniProtKB:Q8IWL3}.
Interaction partners:
- Stress-70 protein, mitochondrial
- Iron-sulfur cluster assembly enzyme ISCU
- Complex III assembly factor LYRM7
- Glutaredoxin-related protein 5, mitochondrial
- Cysteine desulfurase
- Frataxin, mitochondrial
- Iron-sulfur cluster assembly 2 homolog, mitochondrial
Sequence:
MWGCGARALLGVWEVRLAGFLGRRLLGSNAAAGKSIAPQCWNCGHAREAGCGDEFFCSHCRALQPPDPTRDYFSLMNCNRSFRVDVTKLQHRYQQLQRLVHPDFFSQKSQTEKHFSDKHSTLVNDAYKTLQAPLTRGLYLLKLQGIEIPEGTDYKADSQFLVEIMEINERLADAQSEAAMEEIEATVRAKQKEFTDNINSAFEQGDFEKAKELLTKMRYFSNIEEKIKLSKTPL
Protein: HL04706p (Water witch, isoform A) (Water witch, isoform B) (Water witch, isoform C) (Q9VHY7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Inactive
Sequence:
MENLGYKEGSTKPRRMTRSISVVTKTEVEQPLTENNANNRFKSIPPNLMVRWRNNTDAMIEAQYPTAGEFEYMECGPSPPAESAPSMYDSFEEPTSELSVQICNDTLRISLIDQMKSAAGRVKLFEDIEQSNVVAEGIRTHFESASKLEKNLCYLWAAYLKRWDLIESLLEAGADLHFCDQNGISALHLSAFSGCLATLGLLVAKGLNVNLQSKCYTPLHCAAFGNAAEAAKLLINNGADISKDTSKPNCEESLLHCAVRSNALECLQIFIAEGADVNSLKPNGTNAIHLAADLGNIQCLEALLNAPNADANVRICIREKESTALHLAADEGNVECVDLLLAKGADAKLKNHRGFTPLHLAARTSSLDCVESLLRNGNADANAEDFDHRTPLHAAVGKSENAYDIMETLIQWGANVNHKDIYGFTALHLAALDGLVQCVEMLIFHGADVTTKSKKGTSALNVITRKTPASVAMIRQKLDAAITLHHSQDPVNREVELELDFRQLLQHCHPREISYLNTFVDEGQKEILEHPLCSSFLYIKWGKIRKYYIGRLIFCFSFVLFLTLYVLTALAHNCYNGSKNDNTTIPAQELCQKQSILGDMLRNNPFVMEMQWWVLVAITIVEIFRKLYGITGYSSFRHYVTQVENIMEWFVITSVFVISYIYTNKTYTFQNHIGAFAVLLGWTNLMLMIGQLPVFDVYVAMYTRVQGEFAKLFMAYSCMLIGFTISFCVIFPSSSSFANPFMGFITVLVMMIGEQDLSLLINDPEGKDPPFLLEVSAQITFVLFLLFVTIILMNLLVGIAVHDIQGLKKTAGLSKLVRQTKLISYIESALFNGYLPTWLRNLLHYTALVSPQAYRVVLCVKPLNPSEKRLPREILMKAYEVGKMRKHFGHTISSKNSAENYLSYKNKYNNNNGATTGYVLPDSDPDAGQFTTLTTKIDDNADRIEFLTQEIQELKQALISQQQQASKVIDKLLIVISNQQKQNLRK
Protein: V-type proton ATPase subunit F (A0A1D8PH17)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Vacuole membrane {ECO:0000256|ARBA:ARBA00029427}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029427}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00029427}.
Interaction partners:
- H
- V-type proton ATPase subunit C
- V-type proton ATPase subunit G
- V-type proton ATPase subunit B
- V-type proton ATPase subunit D
- V-type proton ATPase subunit H
- V-type proton ATPase catalytic subunit A
- H
- V-type proton ATPase subunit a
- V-type proton ATPase subunit
Sequence:
MEKRKLVAAIADEDTVTGLLLAGIGQISNEPGKESNFLTVIPGKTTVEQIEEAFTTFTSTRDDIAILLINQHLADLIRFKVDSFSNAFPAILEIPSKDHPYDPEKDSILKKVRKLFGE
Protein: SH3 and cysteine-rich domain-containing protein 3 (Q6DBR6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required for normal excitation-contraction coupling in skeletal muscle and for normal muscle contraction in response to membrane depolarization. Required for normal Ca(2+) release from the sarcplasmic reticulum, which ultimately leads to muscle contraction. Probably functions via its effects on muscle calcium channels. Increases CACNA1S channel activity, in addition to its role in enhancing the expression of CACNA1S at the cell membrane. Has a redundant role in promoting the expression of the calcium channel CACNA1S at the cell membrane (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8BZ71}. Cell membrane, sarcolemma {ECO:0000269|PubMed:23736855}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8BZ71}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8BZ71}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:23736855}.
Interaction partners:
- Ryanodine receptor 1a
- Voltage-dependent L-type calcium channel subunit beta-1
- Voltage-dependent L-type calcium channel subunit alpha
- Voltage-dependent N-type calcium channel subunit alpha
- Voltage-dependent L-type calcium channel subunit beta-2
- Calsequestrin
- Calsequestrin
Sequence:
MAQYDQLEDKDSLDIHDNPPAPENVVKEDDNTVYFVYDEEVEEEEAPPPPTPEPIVQVNDKPHKFKDHYCKKPKFCDVCARMIVLNNKFALRCKNCKTNIHHSCQSYVQFQRCFGKIPPGFRRAYSSPLYDQEINNPGQQNRTDPVFDTLRVGVIMANKERKKGSEDKKNMMMMMMEEEEAQQPKEDEEGAEGKQDGDKKDKTATDDKNKKQQQTFSQSHYYMALYRFKAIEKDDLDFHPGDRITVLDDSNEEWWRGKIGEKTGYLPMTYIIRVRAGERVYKVTRSFVGNREMGQITLKKDQIVVKKGEEVNGYLKVSTGRKLGFFPADLLHEL
Protein: UDP-glucuronosyltransferase 1A4 (UGT1A4) (EC 2.4.1.17) (Bilirubin-specific UDPGT isozyme 2) (hUG-BR2) (UDP-glucuronosyltransferase 1-4) (UDPGT 1-4) (UGT1*4) (UGT1-04) (UGT1.4) (UDP-glucuronosyltransferase 1-D) (UGT-1D) (UGT1D) (P22310)
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. Involved in the glucuronidation of calcidiol, which is the major circulating form of vitamin D3 essential for the regulation of calcium and phosphate homeostasis. Also glucuronidates the biologically active form of vitamin D3, calcitriol, probably leading to its biliary transport and intestinal reabsorption.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:17179145}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- UDP-glucuronosyltransferase 1A3
- UDP-glucuronosyltransferase 1A9
- UDP-glucuronosyltransferase 1A6
- UDP-glucuronosyltransferase 1A8
- UDP-glucuronosyltransferase 1A10
- UDP-glucuronosyltransferase 1A7
- UDP-glucuronosyltransferase 1A1
- Cytochrome P450 3A4)
- UDP-galactose translocator
- Cytochrome P450 1A1
Sequence:
MARGLQVPLPRLATGLLLLLSVQPWAESGKVLVVPTDGSPWLSMREALRELHARGHQAVVLTPEVNMHIKEEKFFTLTAYAVPWTQKEFDRVTLGYTQGFFETEHLLKRYSRSMAIMNNVSLALHRCCVELLHNEALIRHLNATSFDVVLTDPVNLCGAVLAKYLSIPAVFFWRYIPCDLDFKGTQCPNPSSYIPKLLTTNSDHMTFLQRVKNMLYPLALSYICHTFSAPYASLASELFQREVSVVDLVSYASVWLFRGDFVMDYPRPIMPNMVFIGGINCANGKPLSQEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Protein: Aryl-hydrocarbon-interacting protein-like 1 (Q924K1)
Organism: Mus musculus (Mouse)
Function: May be important in protein trafficking and/or protein folding and stabilization.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Aryl hydrocarbon receptor
- AH receptor-interacting protein
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- X-linked retinitis pigmentosa GTPase regulator-interacting protein 1
- Guanylate cyclase D
- Recoverin
- Rhodopsin
- Spermatogenesis-associated protein 7 homolog
- Retinol dehydrogenase 12
Sequence:
MDVSLLLNVEGVKKTILHGGTGELPSFITGSRVTFHFRTMKCDDERTVIDDSKQVGQPMSIIIGNMFKLEVWETLLTSMRLGEVAEFWCDTIHTGVYPMLSRSLRQVAEGKDPTSWHVHTCGLANMFAYHTLGYEDLDELQKEPQPLVFLIELLQVEAPNEYQRETWNLNNEERMQAVPLLHGEGNRLYKLGRYDQAATKYQEAIVCLRNLQTKEKPWEVEWLKLEKMINTLILNYCQCLLKKEEYYEVLEHTSDILRHHPGIVKAYYMRARAHAEVWNAEEAKADLEKVLELEPSMRKAVLRELRLLESRLADKQEEERQRCRSMLG
Protein: Transcription factor SOX-21 (Q9W7R5)
Organism: Gallus gallus (Chicken)
Function: Acts as a negative regulator of transcription.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Sulfhydryl oxidase 1
- G protein-coupled receptor 180.
Sequence:
MSKPVDHVKRPMNAFMVWSRAQRRKMAQENPKMHNSEISKRLGAEWKLLSEAEKRPFIDEAKRLRAMHMKEHPDYKYRPRRKPKTLLKKDKFAFPVPYGLGAVAEHEPPHGLKAAALHGGAAGGLGPDSLLGNPEKAAAAAAAAAARVFFPQSAAAAAAAAAAAAAGGPYSLLDLGSKMAEISSSSSAGSALPYASSLGYPGAGGAGAFHGAAAAAAAAAAAAGGHTHSHPSPGNPGYMIPCNCSAWPGPGLQPPLAYILLPGMGKPQLDPYPAAYAAAL
Protein: Tetraspanin-13 (Tspan-13) (Tetraspan NET-6) (Transmembrane 4 superfamily member 13) (O95857)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Tetraspanin-7
Sequence:
MVCGGFACSKNCLCALNLLYTLVSLLLIGIAAWGIGFGLISSLRVVGVVIAVGIFLFLIALVGLIGAVKHHQVLLFFYMIILLLVFIVQFSVSCACLALNQEQQGQLLEVGWNNTASARNDIQRNLNCCGFRSVNPNDTCLASCVKSDHSCSPCAPIIGEYAGEVLRFVGGIGLFFSFTEILGVWLTYRYRNQKDPRANPSAFL
Protein: Pentalenolactone F synthase (EC 1.14.11.36) (Pentalenolactone biosynthesis protein D) (E3VWK4)
Organism: Streptomyces exfoliatus (Streptomyces hydrogenans)
Function: Catalyzes the Fe(2+) and alpha-ketoglutarate-dependent oxidation of pentalenolactone D to pentalenolactone F in the biosynthesis of pentalenolactone antibiotic. Also able to catalyze the oxidation of pentalenolactone D to pentalenolactone E.
Interaction partners:
Sequence:
MDVTPIPGAALGAVVHGAHVTGDMDKTQFEEIWAALDAHLVLVFRGHRTPSYEEFLAFGRRFGYIPKTGLTSGAHPDHNEILIVSNLVEDGRKIGVGDAEWMGWHTDYSFRPRVSQVGFLEAVEVPSCGGETLFTDMYALYESLSPEERKRMHSYRVRHAMRTGYEETIEEKLQREVSLGGSGEQILPEDGTSTIHPLIARNPRTGRQSVYISTLNTERIVDLAPDDSRKLLDELLSHAGKPEHTYAHTWQPGDIVMWDQLGTVHAKQAFDPAELRVMRQVVSIFDDPTDPWHAEVAA