wanglab/gogpt-training-data huggingface dataset:
Protein: Interleukin-2 receptor subunit alpha (IL-2 receptor subunit alpha) (IL-2-RA) (IL-2R subunit alpha) (IL2-RA) (p55) (CD antigen CD25) (P01590)
Organism: Mus musculus (Mouse)
Function: Receptor for interleukin-2. The receptor is involved in the regulation of immune tolerance by controlling regulatory T cells (TREGs) activity. TREGs suppress the activation and expansion of autoreactive T-cells.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Interleukin-2
- Cytokine receptor common subunit gamma
- Interleukin-2 receptor subunit beta
- Tyrosine-protein kinase JAK3
- Signal transducer and activator of transcription
- Interleukin-15
- Forkhead box protein P3
- Interleukin-4
- Interferon gamma
- Interleukin-7
Sequence:
MEPRLLMLGFLSLTIVPSCRAELCLYDPPEVPNATFKALSYKNGTILNCECKRGFRRLKELVYMRCLGNSWSSNCQCTSNSHDKSRKQVTAQLEHQKEQQTTTDMQKPTQSMHQENLTGHCREPPPWKHEDSKRIYHFVEGQSVHYECIPGYKALQRGPAISICKMKCGKTGWTQPQLTCVDEREHHRFLASEESQGSRNSSPESETSCPITTTDFPQPTETTAMTETFVLTMEYKVAVASCLFLLISILLLSGLTWQHRWRKSRRTI
Protein: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase (EC 2.1.1.14) (C8V8J7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- S-adenosylmethionine synthase
- Homocysteine S-methyltransferase
- Cystathionine beta-lyase
- Adenosylhomocysteinase
- Homocysteine synthase
- cystathionine gamma-synthase
- cystathionine gamma-lyase
- Cystathionine beta-synthase
- Cysteine synthase 1
- Homoserine dehydrogenase
Sequence:
MVQSAVLGFPRMGKLRDLKKATEAYWGEKISRDELLSEGKRLRAEHWKIQKDAGVDIIPSNDFAFYDQVLDHIQLFGVVPERYSKYNLHPLDEYFAMGRGLQKPAKDGQPAIDVPSLEMVKWFDSNYHYVKPTLQDNQTFKLAANPKPVVEFLEAKEAGIVTRPVILGPVSFLTLAKADRGQTLDPISKIDELLPLYVELLTKLKEAGVEDVQIDEPVLVFDLPLKSKNAFKPAYEKLGSLGAQAPRLVLATYFGDIVHNIDVLPALHNIYGIHIDLVRNPEQLDSVIGALGPKQVLSAGVVDGRNIWKTNFKAAIEKVELAIQKLGKDRVIVSTSSSLLHVPHTLASEKNLDPEVQDWFSFAVEKTSEVVVIAKAVTEGPAAVREQLEANAKSVQARASSKRTNDPKVKERQAAVTPEQHNRKSPFPVRIAEQTKSIKLPLFPTTTIGSFPQTKEIRIQRNKFTKGEITAEEYEKFIEKEIAEVVKIQEELGLDVLVHGEPERNDMVQYFGERLTGYVFTTHAWVQSYGSRCVRPPIIVGDISRPAPMTVKESKYAVSISSKPMKGMLTGPITCLRWSFPRDDVHQSVQAQQLALALRDEVVDLEAAGVKVIQVDEPALREGLPLRAGKEREDYLQWAVAAFRLSTSGVSDGTQIHSHFCYSEFQDFFHAIAALDADVLSIENSKSDAKLLKVFIDEAYPRHIGPGVYDIHSPRVPSEQEIKDRVEEMLAYLRPEQLWINPDCGLKTRQWPETKAALSNLVQAAKYFREKYAK
Protein: Proteasome subunit beta (A0A140VK46)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR001213}. Nucleus {ECO:0000256|PIRNR:PIRNR001213}.
Interaction partners:
Sequence:
MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE
Protein: DnaJ homolog subfamily B member 12 (Q9NXW2)
Organism: Homo sapiens (Human)
Function: Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum-associated degradation (ERAD) pathway. Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act independently of HSPA8/Hsc70: together with DNAJB14, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers. While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70. When overexpressed, forms membranous structures together with DNAJB14 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21148293, ECO:0000269|PubMed:21150129, ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:24732912}; Single-pass membrane protein {ECO:0000305}. Note=Localizes to the endoplasmic reticulum membrane (PubMed:21148293, PubMed:21150129, PubMed:24732912, PubMed:27916661). When overexpressed, forms membranous structures in the nucleus (PubMed:24732912). {ECO:0000269|PubMed:21148293, ECO:0000269|PubMed:21150129, ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}.; SUBCELLULAR LOCATION: Note=(Microbial infection) Upon SV40 infection, colocalizes with BCAP31, DNAJC18 and DNAJB14 in punctate structures within the endoplasmic reticulum membrane. {ECO:0000269|PubMed:25631089}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock-related 70 kDa protein 2
- Stress-70 protein, mitochondrial
- Exocyst complex component 3
- Endoplasmic reticulum chaperone BiP
- Heat shock 70 kDa protein 1-like
- Small glutamine-rich tetratricopeptide repeat-containing protein alpha
- Heat shock protein 105 kDa
- Heat shock 70 kDa protein 1A
- E3 ubiquitin-protein ligase RNF5
Sequence:
MESNKDEAERCISIALKAIQSNQPDRALRFLEKAQRLYPTPRVRALIESLNQKPQTAGDQPPPTDTTHATHRKAGGTDAPSANGEAGGESTKGYTAEQVAAVKRVKQCKDYYEILGVSRGASDEDLKKAYRRLALKFHPDKNHAPGATEAFKAIGTAYAVLSNPEKRKQYDQFGDDKSQAARHGHGHGDFHRGFEADISPEDLFNMFFGGGFPSSNVHVYSNGRMRYTYQQRQDRRDNQGDGGLGVFVQLMPILILILVSALSQLMVSSPPYSLSPRPSVGHIHRRVTDHLGVVYYVGDTFSEEYTGSSLKTVERNVEDDYIANLRNNCWKEKQQKEGLLYRARYFGDTDMYHRAQKMGTPSCSRLSEVQASLHG
Protein: Neutral amino acid transporter 9 (Solute carrier family 38 member 9) (Q08BA4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Lysosomal amino acid transporter involved in the activation of mTORC1 in response to amino acid levels. Probably acts as an amino acid sensor of the Rag GTPases and Ragulator complexes, 2 complexes involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Following activation by amino acids, the Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. SLC38A9 mediates transport of amino acids with low capacity and specificity with a slight preference for polar amino acids (By similarity). Acts as an arginine sensor. Following activation by arginine binding, mediates transport of L-glutamine, leucine and tyrosine with high efficiency, and is required for the efficient utilization of these amino acids after lysosomal protein degradation. However, the transport mechanism is not well defined and the role of sodium is not clear. Guanine exchange factor (GEF) that, upon arginine binding, stimulates GDP release from RRAGA and therefore activates the Rag GTPase heterodimer and the mTORC1 pathway in response to nutrient sufficiency (By similarity).
Subcellular location: Lysosome membrane {ECO:0000250|UniProtKB:Q8NBW4}; Multi-pass membrane protein {ECO:0000269|PubMed:29872228}. Late endosome membrane {ECO:0000250|UniProtKB:Q8NBW4}; Multi-pass membrane protein {ECO:0000269|PubMed:29872228}.
Interaction partners:
- Ragulator complex protein LAMTOR2
- Ragulator complex protein LAMTOR1
- Ragulator complex protein LAMTOR3
- Ragulator complex protein LAMTOR5
- Ras-related GTP-binding A.
- Ragulator complex protein LAMTOR4
- Folliculin-interacting protein 2
- Folliculin
- Cytosolic arginine sensor for mTORC1 subunit 1.
- Ras-related GTP-binding protein
Sequence:
MDEDSKPLLGSVPTGDYYTDSLDPKQRRPFHVEPRNIVGEDVQERVSAEAAVLSSRVHYYSRLTGSSDRLLAPPDHVIPSHEDIYIYSPLGTAFKVQGGDSPIKNPSIVTIFAIWNTMMGTSILSIPWGIKQAGFTLGIIIIVLMGLLTLYCCYRVLKSTKSIPYVDTSDWEFPDVCKYYFGGFGKWSSLVFSLVSLIGAMVVYWVLMSNFLFNTGKFIFNYVHNVNTSDAFGTNGTERVICPYPDVDPHGNSSTSLYSGSDNSTGLEFDHWWSKTNTIPFYLILLLLPLLNFRSASFFARFTFLGTISVIYLIFLVTYKAIQLGFHLEFHWFDSSMFFVPEFRTLFPQLSGVLTLAFFIHNCIITLMKNNKHQENNVRDLSLAYLLVGLTYLYVGVLIFAAFPSPPLSKECIEPNFLDNFPSSDILVFVARTFLLFQMTTVYPLLGYLVRVQLMGQIFGNHYPGFLHVFVLNVFVVGAGVLMARFYPNIGSIIRYSGALCGLALVFVLPSLIHMVSLKRRGELRWTSTLFHGFLILLGVANLLGQFFM
Protein: DNA ligase 1 (EC 6.5.1.1) (DNA ligase I) (Polydeoxyribonucleotide synthase [ATP] 1) (P18858)
Organism: Homo sapiens (Human)
Function: DNA ligase that seals nicks in double-stranded during DNA repair. Also involved in DNA replication and DNA recombination.
Subcellular location: Nucleus.
Interaction partners:
- Flap endonuclease 1
- Proliferating cell nuclear antigen
- DNA repair protein XRCC1
- DNA repair nuclease/redox regulator APEX1
- DNA polymerase beta
- E3 ubiquitin-protein ligase UHRF1
- DNA polymerase delta catalytic subunit
- Replication factor C subunit 4
- Uracil-DNA glycosylase
- DNA replication licensing factor MCM5
Sequence:
MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAALKEWNGVVSESDSPVKRPGRKAARVLGSEGEEEDEALSPAKGQKPALDCSQVSPPRPATSPENNASLSDTSPMDSSPSGIPKRRTARKQLPKRTIQEVLEEQSEDEDREAKRKKEEEEEETPKESLTEAEVATEKEGEDGDQPTTPPKPLKTSKAETPTESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPLDPSGYNPAKNNYHPVEDACWKPGQKVPYLAVARTFEKIEEVSARLRMVETLSNLLRSVVALSPPDLLPVLYLSLNHLGPPQQGLELGVGDGVLLKAVAQATGRQLESVRAEAAEKGDVGLVAENSRSTQRLMLPPPPLTASGVFSKFRDIARLTGSASTAKKIDIIKGLFVACRHSEARFIARSLSGRLRLGLAEQSVLAALSQAVSLTPPGQEFPPAMVDAGKGKTAEARKTWLEEQGMILKQTFCEVPDLDRIIPVLLEHGLERLPEHCKLSPGIPLKPMLAHPTRGISEVLKRFEEAAFTCEYKYDGQRAQIHALEGGEVKIFSRNQEDNTGKYPDIISRIPKIKLPSVTSFILDTEAVAWDREKKQIQPFQVLTTRKRKEVDASEIQVQVCLYAFDLIYLNGESLVREPLSRRRQLLRENFVETEGEFVFATSLDTKDIEQIAEFLEQSVKDSCEGLMVKTLDVDATYEIAKRSHNWLKLKKDYLDGVGDTLDLVVIGAYLGRGKRAGRYGGFLLASYDEDSEELQAICKLGTGFSDEELEEHHQSLKALVLPSPRPYVRIDGAVIPDHWLDPSAVWEVKCADLSLSPIYPAARGLVDSDKGISLRFPRFIRVREDKQPEQATTSAQVACLYRKQSQIQNQQGEDSGSDPEDTY
Protein: Stromal processing peptidase, chloroplastic (EC 3.4.24.-) (B8B0E2)
Organism: Oryza sativa subsp. indica (Rice)
Function: Cleaves presequences (transit peptides) from chloroplastic protein precursors. Initially recognizes a precursor by binding to the C-terminus of its transit peptide and then removes the transit peptide in a single endoproteolytic step. In a next step, pursues the cleavage of transit peptide to a subfragment form.
Subcellular location: Plastid, chloroplast stroma {ECO:0000250|UniProtKB:Q40983, ECO:0000269|PubMed:20097911}.
Interaction partners:
- Ubiquitin-like domain-containing protein
- Ubiquitin-like domain-containing protein
- Ubiquitin-like domain-containing protein
- Ubiquitin-like domain-containing protein
Sequence:
MASFPSPPLAAAAAAAPPRLAPGLPLAAAAVRRPSSLARRSSIALAAPANPLRCIHRRAVSPRLRRRTEAVGAASAAIGSLGEEREGCLSCFPRGRRRGRPGLARFAPCALPHTYGLSSLHSGLTGAKIRRRHVLHAAGPDEPHVASPTWSETALDKHYVDQPIGKEELEGFLNTPLPSHPKLVRGQLKNGLRYLILPNKVPANRFEAHMEVHVGSIDEEEDEQGIAHMIEHVAFLGSKKREKLLGTGARSNAYTDFHHTVFHIHSPTKTKEYGEDLLPSVLDALNEIAFHPKFSSSRVEKERRAILSELQMMNTIEYRVDCQLLQHLHSENKLSERFPIGLEEQIHKWDPDKIRRFHERWYYPANATLYLVGEINDIPRAIREIEAVFEHTLPEGEAAPMSTASPFGAMASLFAPKLPGGLAASLTGERSPAADKIKPVKRERQAIRPPVEHKWSLPGVAQDAKPPAIFQHELIQSFSINMFCKIPVNQVQTYKDLRSVLMKRIFLSALHFRINTRYKSSNPPFTSVELDHSDSGREGCTVTTLTVTAEPQNWRSAIKVAVHEVRRLKEFGVTMGEMTRYMDALIKDSEQLAMMIDSVPSVDNLDFIMESDALRHTVMDQLQGHESLLAVAETVTLEEVNTVGAEVLEFISDYGKPDAPLPAAIVACVPKKVHMDGVGETDFEIHPEEITDSIKAGLEEPIYPEPELEVPKELITQSELEDLKLQRKPSFASLSKEENVVKIFDDETGIAQRRLSNGISINYKITQNEARVGVMRLIVGGGRATEDSESKGSVIVGVRTLSEGGCVGNFSREQVELFCVNNLINCSLESNEEFIFMEFRFALRDNGMRAAFQLLHMVLEHNVWLEDAFDRATQLYLSYYRSIPKSLERSTAHKLMLAMLNHDERFVEPSPHSLQKLTLQSVKDAVMNQFVGDNMEVSIVGDFTEEEVESCVLDYLGTVSAPKSSKTQEHIEKISFLPFPSDLHFQQVYIKDTDERACAYIAGPAPNRWGFATEGNDLFNVIRSSSGDAQVSESANTDLTERKHNDVRSHSLFFGITLSLLAEIINSRLFTTVRDSMGLTYDVSFELNLFDKLDLGWYVIAVTSTPSKVHKAVDACKGVLRGLHSNKIVERELDRAKRTLLMKHEAETKTNAYWLGLLAHLQSSSVPRKEISCIKELTMLYESATIEDLYLAYEHLKVDESSLFACIGIAGAESGEETTDDELDMGLHGMGPIGGRGLSTMTRPTT
Protein: LL-diaminopimelate aminotransferase (DAP-AT) (DAP-aminotransferase) (LL-DAP-aminotransferase) (EC 2.6.1.83) (Q6LX26)
Organism: Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)
Function: Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Diaminopimelate epimerase
- 4-hydroxy-tetrahydrodipicolinate reductase
- Uncharacterized metallohydrolase MMP1398
- Diaminopimelate decarboxylase
Sequence:
MESYIQNLFAERIGGKSFGKEDVIYKFEKIKRAKQAAKLKYPDMELIDMGVGEPDEMADESVVEVLCEEAKKHVNRGYSDNGVQALKDEIPIYLEKIFGVKDLDPVNEVVHSIGSKPALAYITSVFINPGDVTLMTVPGYPVTATHTKWYGGSVETLPLLEKNNFLPELDAISKEVRENAKILYLNYPNNPTGAQATKKFYKEAVDFAFENDLIVIQDAAYAALTYGDKPLSFLSVKDAKEVGVEIHSFSKAYNMTGWRLAFVAGNELIVRGFAAVKDNYDSGQFIPIQKAGIHCLRHPEITEKTRAKYERRLSKMVKILKEAGFNAKMPGGTFYLYVKAPIGTKDGAKFANAEEFSQFMIKEKLISTVPWDDAGNFVRMAACFEAFKDGEISIEEEDRILNEVKRRLTEVEFVFE
Protein: BARP protein (Q38CV5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSITFHNLWLLLTVLCTAGIRADASKEECPDKGSYPAAEDVLVLCHVAEQLRGLPDTVSSALVTAAAASSKAFEAKVQAEEAVELAESRGLNVTKAKEAAVRATLAAEAAATAVSYANAHGTKVGSMTEILWEADEELRELVVCKRMDEETIKAAAECTGTAEVVTAQSLSEALEALANLHYGDENVAETLRRKDVVFHKELKSLEGYVEEAVHAQKQAEDAAADANQVATGNSVASPEKSVLLLMAGLFLGSVL
Protein: CG10206-PA (LD32943p) (Nop5) (Q9VM69)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- Lethal
- LD17611p
- LD10780p
- FI03455p
- LD47550p
- H/ACA ribonucleoprotein complex subunit 4
- NHP2-like protein 1 homolog
- LD47749p
- Nucleolar protein 56
- FI12406p
Sequence:
MFVLYETPAGYAIFKLLDEKKLEQVDNLYQEFETPEKANKLLKLKHFEKFNDTTEALAAATAAVEGKVAKPLKKTLKKLLVDDVQSSLLVADAKLGTAIKDKLSVQCVCNTGVQELMRCIRQQADSLLGGLPKREMTAMALGLAHSLSRYKLKFSPDKIDTMIVQAQCLLDDLDKELNNYMMRAREWYGWHFPELGKIITDNIAFVKTIKLVGTRDNMATSDLSDILPEDVEEKVKEAAEISMGTEISEEDVLNIQCLCDEIISINDYRTHLYDYLKARMMAMAPNLTVLVGDTVGARLIAHAGSLINLAKHPSSTVQILGAEKALFRALKTKKDTPKYGLIYHAQLVGQASQKNKGKMSRSLAAKASLATRVDAFGEEATFELGAAHKVKLESRLRLLEEGNLRKLSGTGKAKAKFEKYQAKSEVFTYQPEADNTLNVKKKRKHSESEQQTPVKKEEPAEEEAEVKSEKKKKKKKKQKDEEVEAVEEAAAPEPEDQPTPAKKKKKSKHQE
Protein: Phosphatidylcholine:ceramide cholinephosphotransferase 2 (EC 2.7.8.27) (Sphingomyelin synthase 2) (Sms2) (Q9D4B1)
Organism: Mus musculus (Mouse)
Function: Sphingomyelin synthase that primarily contributes to sphingomyelin synthesis and homeostasis at the plasma membrane. Catalyzes the reversible transfer of phosphocholine moiety in sphingomyelin biosynthesis: in the forward reaction transfers phosphocholine head group of phosphatidylcholine (PC) on to ceramide (CER) to form ceramide phosphocholine (sphingomyelin, SM) and diacylglycerol (DAG) as by-product, and in the reverse reaction transfers phosphocholine from SM to DAG to form PC and CER. The direction of the reaction appears to depend on the levels of CER and DAG in the plasma membrane. Does not use free phosphorylcholine or CDP-choline as donors (By similarity). Can also transfer phosphoethanolamine head group of phosphatidylethanolamine (PE) on to ceramide (CER) to form ceramide phosphoethanolamine (CPE) (By similarity). Regulates receptor-mediated signal transduction via mitogenic DAG and proapoptotic CER, as well as via SM, a structural component of membrane rafts that serve as platforms for signal transduction and protein sorting. To a lesser extent, plays a role in secretory transport via regulation of DAG pool at the Golgi apparatus and its downstream effects on PRKD1. Required for normal bone matrix mineralization (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8NHU3}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8NHU3}; Multi-pass membrane protein {ECO:0000255}. Note=Primarily localized at the plasma membrane with a small fraction at the Golgi apparatus. {ECO:0000250|UniProtKB:Q8NHU3}.
Interaction partners:
- Sphingomyelin phosphodiesterase
- Sphingomyelin phosphodiesterase 2
- Ceramide glucosyltransferase
- Ceramide synthase 2
- Ceramide synthase 4
- Neutral ceramidase
- Ceramide kinase
- Sphingomyelin phosphodiesterase 4
- Sphingomyelin phosphodiesterase 3
- Acid ceramidase
Sequence:
MDIIETAKLEGHLESQTNDSTNTYTSPTEAVEEEGKNGKGKPKTLSNGLRKGAKKYPDYIQISMPNDSKNKFPLEWWKTGIAFVYALFNLILTTVMITVVHERVPPKELSPPLPDKFFDYFDRVKWAFSVSEINGMVLVGLWITQWLFLRYKSIVGRRFFFIMGTLYLYRCITMYVTTLPVPGMHFQCAPKLNGDSQAKIQRILRLISGGGLSITGSHILCGDFLFSGHTVVLTLTYLFIKEYSPRHFWWYHLVCWLLSAAGIICILVAHEHYTVDVIIAYYITTRLFWWYHSMANEKNLKVSSQTNFLSRAWWFPIFYFFEKNVQGSIPCCFSWPLSWPPGCFKSSCRKYSRVQKIGEDNEKST
Protein: Uncharacterized protein, isoform A (Q9VR26)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RRM domain-containing protein
- LD32469p
- RNA-binding protein 1
- U1-C C2H2-type zinc finger domain-containing protein
- Splicing factor U2AF 50 kDa subunit
- Splicing factor U2AF subunit
- LD40489p
- LD21442p
- Zinc finger protein 830
- Splicing factor 3B subunit 1
Sequence:
MPGRKARRKLIKKQQRKRRRQKHAKERDKLEEEAENQRLMQPEYQKWSQEQEEMQEFQRLADERERQLAEESWLRREATAQRQFQMDEAKKRQEQEEVERLQREQAKERAEREERQRKQREEETRKAAKAAAEFDAMMESMDEYLNNPRIEKPPSHLLRVMETHPEERACEFFSRTNCCRYGHACTFNHRRPMLGRILLIRHFFNHSMLQKRCTHKEYASAEEHLELTEQDLRHDYDEFFNDVVEELRKFGTIVNFRTVRNTLEHLRGHVFVEYTNERSALRAFTNLQGRYYASKRLNVEFSNLRTWRGAVCGLSLTRKCPKGNDCGYLHLFGNPNNLFNTELEYTSGPRSERRSSQTPTAKTPSWDEHSEHGRNWRWSASPEVELENSKDLGNRGRDLKNNQQRNHHSRSRSDRSSVRSKREHSSSGSSHDDRRSKRHHHHHNSTTPDHQHNHCQ
Protein: Galectin-2 (Gal-2) (Beta-galactoside-binding lectin L-14-II) (HL14) (Lactose-binding lectin 2) (S-Lac lectin 2) (P05162)
Organism: Homo sapiens (Human)
Function: This protein binds beta-galactoside. Its physiological function is not yet known.
Interaction partners:
- Lymphotoxin-alpha
- Galanin peptides
- Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase
- Chromodomain-helicase-DNA-binding protein 7
- Galectin-10
- Spexin
Sequence:
MTGELEVKNMDMKPGSTLKITGSIADGTDGFVINLGQGTDKLNLHFNPRFSESTIVCNSLDGSNWGQEQREDHLCFSPGSEVKFTVTFESDKFKVKLPDGHELTFPNRLGHSHLSYLSVRGGFNMSSFKLKE
Protein: General transcription and DNA repair factor IIH helicase subunit XPD (TFIIH subunit XPD) (EC 5.6.2.3) (DNA 5'-3' helicase XPD) (ERCC2 homolog) (RAD3 homolog) (UV hypersensitive protein 6) (AtUVH6) (XPD homolog) (AtXPD) (Q8W4M7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. XPD acts by forming a bridge between CAK and the core-TFIIH complex (By similarity). Essential during plant growth. May negatively regulate a common response program mediated by UV damage and heat stress, that leads to tissue death and reduced chloroplast function.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- General transcription and DNA repair factor IIH subunit TFB4
- Cyclin-H1-1
- General transcription factor IIH subunit 2
- Pentatricopeptide repeat-containing protein At4g30825
- General transcription and DNA repair factor IIH subunit TFB1-1
- General transcription and DNA repair factor IIH subunit TFB2
- DNA-directed RNA polymerase II subunit 4
- Transcription initiation factor IIF subunit alpha
- Transcription initiation factor IIA subunit 2
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB1
Sequence:
MIFKIEDVTVYFPYDNIYPEQYEYMVELKRALDAKGHCLLEMPTGTGKTIALLSLITSYRLSRPDSPIKLVYCTRTVHEMEKTLGELKLLHDYQVRHLGTQAKILALGLSSRKNLCVNTKVLAAENRDSVDAACRKRTASWVRALSTENPNVELCDFFENYEKAAENALLPPGVYTLEDLRAFGKNRGWCPYFLARHMIQFANVIVYSYQYLLDPKVAGFISKELQKESVVVFDEAHNIDNVCIEALSVSVRRVTLEGANRNLNKIRQEIDRFKATDAGRLRAEYNRLVEGLALRGDLSGGDQWLANPALPHDILKEAVPGNIRRAEHFVHVLRRLLQYLGVRLDTENVEKESPVSFVSSLNSQAGIEQKTLKFCYDRLQSLMLTLEITDTDEFLPIQTVCDFATLVGTYARGFSIIIEPYDERMPHIPDPILQLSCHDASLAIKPVFDRFQSVVITSGTLSPIDLYPRLLNFTPVVSRSFKMSMTRDCICPMVLTRGSDQLPVSTKFDMRSDPGVVRNYGKLLVEMVSIVPDGVVCFFVSYSYMDGIIATWNETGILKEIMQQKLVFIETQDVVETTLALDNYRRACDCGRGAVFFSVARGKVAEGIDFDRHYGRLVVMYGVPFQYTLSKILRARLEYLHDTFQIKEGDFLTFDALRQAAQCVGRVIRSKADYGMMIFADKRYSRHDKRSKLPGWILSHLRDAHLNLSTDMAIHIAREFLRKMAQPYDKAGTMGRKTLLTQEDLEKMAETGVQDMAY
Protein: Conserved domain protein (A0A0H2UNW5)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MEVVMDNIIDVSIPVAEVVDKHPEVLEILVELGFKPLANPLMRNTVGRKVSLKQGSKLAGTPMDKIVRTLEANGYEVIGLD
Protein: Chloride channel CLIC-like protein 1 (ER anion channel 1) (ERAC1) (Mid-1-related chloride channel protein 1) (Q9WU61)
Organism: Rattus norvegicus (Rat)
Function: Seems to act as a chloride ion channel. Plays a role in retina development (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11279057}; Multi-pass membrane protein {ECO:0000255}. Note=Within the endoplasmic reticulum (ER), localizes to the mitochondria-associated ER membrane, a zone of contact between the ER and mitochondrial membranes. Enriched in the rough ER. {ECO:0000250|UniProtKB:Q96S66, ECO:0000250|UniProtKB:Q99LI2}.
Interaction partners:
Sequence:
MLCSLLLCGCLLLITGYAHDDDWIDPTDMLNYDAASGTMRKSQAKYGTSEKKEVNPGLSDAQELSDCLQRLDSLTHKVDDCEKKKMKDYESQSNPVFRRYLNKILIEAGKLGLPDEDRVDVRYDAEILLTRQTLLEIQKFLSGEEWKPGALDDALSDILTNFKSHDAEAWKWQFEDYFGVDPYNVFMVLLCLLCIVALVATELWTYVRWHTQLKRVCIISFLVSLGWNWIYLYKVAFAQHQANVAKMAPLNDVCAKKMDWTENLWEWFRISWTYKDDPCQKYYELLIVNPIWLVPPTKALAVTFTNFVTEPLKYIGKGTGEFIKALMKEIPVLLQIPVLVILALAVLGFCYGAGQSVPMLRHFRGPEREPPRALEPDDRRRQKELDYRFHGGAGDADFSYRGPAGSIEQGPYDKMHVCERDVLRQRQVNMRFPSGNKSPEVLRAFDLPDTEAQEHPEVVPSHKPSIVNTSLKETSELPRESTLAECSQCAKDGSGQVPSTAESSPIVEKAQLKTDSECRPHSTEAAAAAARGTDPVSSPCG
Protein: RUN and FYVE domain-containing protein 4 (Q3TYX8)
Organism: Mus musculus (Mouse)
Function: Positively regulates macroautophagy in primary dendritic cells. Increases autophagic flux, probably by stimulating both autophagosome formation and facilitating tethering with lysosomes. Binds to phosphatidylinositol 3-phosphate (PtdIns3P) through its FYVE-type zinc finger.
Subcellular location: Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q6ZNE9}. Lysosome {ECO:0000250|UniProtKB:Q6ZNE9}. Note=In the presence of ARL8, recruited to endolysosomes. {ECO:0000250|UniProtKB:Q6ZNE9}.
Interaction partners:
- RUN and FYVE domain-containing protein 2
Sequence:
MANNGTILKISRSLKNAVSAILQGYGDGQEPVTETSAELHRLCGCLELLLQFDQKEQRSFLGARKDYWDFLFTALRRHRGYTEQMSFICSQDKLKTSLGKGRAFIRLCLARGQLAESMQLCLLNPQLTREWYGPRSPLLCAELQEDILDSLYALNGVAFNLDLQRPDLDEAWPMFSESRCSSPSRTGKRRPGKPKGFPEEVRCSRGEQLQEPDTGGTSCLQDATREDRTPDLCKPLQPSHLPTFLEEKREDSRSLSCPQSTWETEREGFQLDQKDGGPKPRKFLENSTASIQQQRSRAKDVKMQLTGRKVEGKGSLSGTEDQRTTEGIQKRAADWDLGQGLMAPGLQGREDAELGYRCEWNQPDVLRQSWVLGTKKSSPTEKPQEWTGVTSGTMQEDGSEVPLQQEVIKDPGYGLQLAKEQAQCQEQLRAQEAELQALQEQLSRCQKERALLQVKLEQKQQEAERRDAMYQTELEGQRDLVQAMKRRVLELIHEKDLQWQRLQQLSTVAPGHCIGCNKVFRRLSRRYPCRLCGGLVCHACSVDYKKRERCCPTCAQQEEIQDT
Protein: Phospholipid/glycerol acyltransferase domain-containing protein (Q38BL2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase
Sequence:
MFWAITGSNVATALEATTRFGEEPAAEAQSSATDRRRTQYATGAPTLEPTFRKPRPALPREADNPFYYSEAASNEPLQRLRKITYTTILVPLRVLYITLLIVLYWLLEMIIQKRGCHTAAKEVDNLSKVSCLFRYIAGTLPRWSILGLGYLRVNRRNKCNYGRRADGSRVVGPVIVANHVTIQDGLLLLFECDASLVTGNLAEANFTSMLLRGRTYNGEDRRIVKSLELKHRQKTQEEIDGTEASTNNNPQTEMSADMSDCNETEVREGGEGVVAHVVFPEPCCTNGRVMMRFSTDAFATGLPVQPVVLRHSHKYFNTSWCGAASPTSILLGTAAQLFNQVEVIYLPVCEPSKEEKLNPSLYAERVRRAMASTLNVPATWHSEADVHLALVAARLSLPVDAVNVETAHPHFAGMPYDRVVRMLYRFSALLQRSDGGPQPQMNITPKGYMSPTALGRFLSPIGLYPTLNERLLLHLSRRASVRGCYISFRDFLSALYTEPIIVGSSDSHGASDKTGESSVPSNAHMVFIDELRKGEADDEVALDFILRRTFAMMLLAGEDLLRQQEKYRSHIKDTFVTVGEVQGAGRENVEAGDANVISCAESPLPTGTCPSSYTTVYGCKVRFLFRPCQNINRCAPVAASLAATALSVEERRLGRAEFDALLDMLFVPHHSTLWRGPATKSQVQLAEEDSLFSYIRSGATEEWEATVGKKTVQIEEVGRGTNRSGEYITFDAFLRFCFRHRAMAEYFHACCEHFLLCDDLA