wanglab/gogpt-training-data huggingface dataset:
Protein: ATP-dependent zinc metalloprotease FTSH 8, chloroplastic (AtFTSH8) (EC 3.4.24.-) (Q8W585)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Part of a complex that function as an ATP-dependent zinc metallopeptidase. Involved in the thylakoid formation and in the removal of damaged D1 in the photosystem II, preventing cell death under high-intensity light conditions.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:18431481}; Single-pass membrane protein {ECO:0000269|PubMed:14630971}; Stromal side {ECO:0000269|PubMed:14630971}.
Interaction partners:
- ATP-dependent zinc metalloprotease FTSH 5, chloroplastic
- ATP-dependent zinc metalloprotease FTSH 2, chloroplastic
- ATP-dependent Clp protease proteolytic subunit 3, chloroplastic
- Protease Do-like 1, chloroplastic
- ATP-dependent Clp protease proteolytic subunit-related protein 4, chloroplastic
- ATP-dependent Clp protease proteolytic subunit-related protein 3, chloroplastic
- ATP-dependent zinc metalloprotease FTSH 1, chloroplastic
- Protease Do-like 5, chloroplastic
- Presequence protease 1, chloroplastic/mitochondrial
- Protease Do-like 8, chloroplastic
Sequence:
MAASSACLLGNGLSVYTTKQRFQKLGLDRTSKVTVVKASLDEKKHEGRRGFFKLLLGNAAAGVGLLASGNANADEQGQGVSSSRMSYSRFLEYLDKGRVEKVDLYENGTIAIVEAVSPELGNRIQRVRVQLPGLSQELLQKLRAKNIDFAAHNAQEDQGSPILNLIGNLAFPVILIGGLFLLSRRSSGGMGGPGGPGFPLQIGQSKAKFQMEPNTGVTFDDVAGVDEAKQDFMEVVEFLKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPGRFDRQVSVDVPDVKGRTDILKVHSGNKKFESGVSLEVIAMRTPGFSGADLANLLNEAAILAGRRGKTAISSKEIDDSIDRIVAGMEGTVMTDGKSKSLVAYHEVGHAICGTLTPGHDAVQKVTLIPRGQARGLTWFIPSDDPTLISKQQLFARIVGGLGGRAAEEVIFGESEVTTGAVSDLQQITGLAKQMVTTFGMSEIGPWSLMDSSEQSDVIMRMMARNSMSEKLANDIDTAVKTLSDKAYEIALSQIRNNREAMDKIVEILLEKETMSGDEFRAILSEFTEIPPENRVASSTSTSTPTPASV
Protein: Killer cell immunoglobulin-like receptor 2DS1 (CD158 antigen-like family member H) (MHC class I NK cell receptor Eb6 ActI) (CD antigen CD158h) (Q14954)
Organism: Homo sapiens (Human)
Function: Receptor on natural killer (NK) cells for some HLA-C alleles such as w6. Does not inhibit the activity of NK cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18682925, ECO:0000269|PubMed:23715743, ECO:0000269|PubMed:9430221}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSLTVVSMACVGFFLLQGAWPHEGVHRKPSLLAHPGRLVKSEETVILQCWSDVMFEHFLLHREGMFNDTLRLIGEHHDGVSKANFSISRMKQDLAGTYRCYGSVTHSPYQLSAPSDPLDIVIIGLYEKPSLSAQPGPTVLAGENVTLSCSSRSSYDMYHLSREGEAHERRLPAGTKVNGTFQANFPLGPATHGGTYRCFGSFRDSPYEWSKSSDPLLVSVTGNPSNSWPSPTEPSSETGNPRHLHVLIGTSVVKIPFTILLFFLLHRWCSDKKNAAVMDQEPAGNRTVNSEDSDEQDHQEVSYA
Protein: AP-1 complex subunit gamma (Q7KVR8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004156}. Endomembrane system {ECO:0000256|ARBA:ARBA00029433}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029433}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00029433}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
- AP complex subunit beta
- Adaptor protein complex 1, mu subunit
- AP complex subunit sigma
- Clathrin heavy chain
- Adaptor protein complex AP-3 small chain sigma3
- Carmine, isoform A
- AP-3 complex subunit beta
- Adaptor protein complex 2, mu subunit, isoform A
- AP complex subunit sigma
- ADP-ribosylation factor 1
Sequence:
MYPYYEQDWSVLPPENNRRFNPAFNMATIRQAFTEAVERVRMPTPTRLRDLIRQIRAARTAAEERAVVNKECAYIRSTFREEDSVWRCRNIAKLLYIHMLGYPAHFGQLECLKLTASTRFTDKRIGYLGAMLLLDERQDVHLLITNCLKNDLNSSTQFVVGLALCTLGAIASPEMARDLASEVERLMKSPNTYIRKKATLCAFRVIRRVPELMEIFLPATRSLLSEKNHGILITGVTLITEMCENSSDTLMHFKKDSGNREIVPNLVRILKNLILGGYSPEHDVSGVSDPFLQVKILRLLRILGHNDPDASEAMNDILAQVATNTETSKNVGNTILYETVLSIMDIRSEGGLRVLAVNILGRFLLNSDKNIRYVALNTLLRTVHADTSAVQRHRTTILECLKDPDVSIRRRAMELSFALINAQNIRTMTKELLLFLEKADAEFKAQCSSGMILAAERYSPTTRWHLDTQLSVLIAAGNYVRDDVVSSTIQLVSSSPVPEQTYITNRFWESLQVANHCEDKQPLLQVAVWAIGEYGDLFMYGANEDEFERPTESDLIAVYYKFLTSAQVSTTSKQYALVSLAKLSTRLQQCVEEIQALITSFGSHLNVDLQQRGVEFTQLFGHYKHLRPPLLEKMPAMQISRISSQNGESGGGSFDDNSPDVIENGVEGGGGGGHSLIESNMNTLGDNTNILLDLLGSTDLSAGGAGDLVAATDLSNAVHKKNSRNANDVVAPVSNNQDLLDLLDLDLSAPSSTTTGAPAGGGGGGGIVALVGDNNQSSAANMNNMLGGLDLGGFGSGLDSSASIPTNGNDLASMLGGLGAPPAASPSLAASAPVGNLIDGHAGSLLADLNPTAASNNVVVPPQGPRLTALDKDGLLVQLVSVRGSDCMRIYMTTTNNSDNTLDQYLLQAAVQRSFQLQMLTPSGSVLPPGGVITQEMRVVATSNATLRMRLRIQYVLDGQQQVEQTEVSGFPEQQPAPAAAE
Protein: t-SNARE coiled-coil homology domain-containing protein (Q57Y13)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTPAASRLRRALREARRLLEEVKLSEDTAVGQCNQRQVTELLKYIKRIGFLLSLVKQEMQANADNSDKRETATTEVSLSGDDVGNAPTVVDAAEAFLSQFLDSYFPHLHVPVACVGLVARHRAPKQPFAVCEPFLIHEDSNAPCVRASIQLEPSPTVKSSTTPAKMGQSGGGDIAITNMAARSTNASSLISSSAFSSAPQDADDAAQKQVINEINDAIREIKEGALRVSDIMNQEKGRLEENAALLQRGVDGTTSQCKKMDRVGSAFGGGPVLPHFLRALPGVEVFWDSILAPLWRIIAQAVFICAIVAVTGGTVMLMLVTPKSYVYER
Protein: Baculoviral IAP repeat-containing protein 3 (EC 2.3.2.27) (Apoptosis inhibitor 2) (API2) (Cellular inhibitor of apoptosis 2) (C-IAP2) (IAP homolog C) (Inhibitor of apoptosis protein 1) (hIAP-1) (hIAP1) (RING finger protein 49) (RING-type E3 ubiquitin transferase BIRC3) (TNFR2-TRAF-signaling complex protein 1) (Q13489)
Organism: Homo sapiens (Human)
Function: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, IKBKE, TRAF1, and BCL10. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15665297}. Nucleus {ECO:0000269|PubMed:15665297}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 1A
- TNF receptor-associated factor 3
- TNF receptor-associated factor 2
- Receptor-interacting serine/threonine-protein kinase 1
- TNF receptor-associated factor 1
- Ubiquitin-conjugating enzyme E2 D2
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Diablo IAP-binding mitochondrial protein
- Caspase-3
- TNF receptor-associated factor 5
Sequence:
MNIVENSIFLSNLMKSANTFELKYDLSCELYRMSTYSTFPAGVPVSERSLARAGFYYTGVNDKVKCFCCGLMLDNWKRGDSPTEKHKKLYPSCRFVQSLNSVNNLEATSQPTFPSSVTNSTHSLLPGTENSGYFRGSYSNSPSNPVNSRANQDFSALMRSSYHCAMNNENARLLTFQTWPLTFLSPTDLAKAGFYYIGPGDRVACFACGGKLSNWEPKDNAMSEHLRHFPKCPFIENQLQDTSRYTVSNLSMQTHAARFKTFFNWPSSVLVNPEQLASAGFYYVGNSDDVKCFCCDGGLRCWESGDDPWVQHAKWFPRCEYLIRIKGQEFIRQVQASYPHLLEQLLSTSDSPGDENAESSIIHFEPGEDHSEDAIMMNTPVINAAVEMGFSRSLVKQTVQRKILATGENYRLVNDLVLDLLNAEDEIREEERERATEEKESNDLLLIRKNRMALFQHLTCVIPILDSLLTAGIINEQEHDVIKQKTQTSLQARELIDTILVKGNIAATVFRNSLQEAEAVLYEHLFVQQDIKYIPTEDVSDLPVEEQLRRLQEERTCKVCMDKEVSIVFIPCGHLVVCKDCAPSLRKCPICRSTIKGTVRTFLS
Protein: Uridine 5'-monophosphate synthase (UMP synthase) [Includes: Orotate phosphoribosyltransferase (OPRT) (OPRTase) (EC 2.4.2.10); Orotidine 5'-phosphate decarboxylase (ODC) (ODCase) (EC 4.1.1.23)] (G5EDZ2)
Organism: Caenorhabditis elegans
Function: Bifunctional enzyme which catalyzes the formation of UMP from orotate in the de novo pathway of pyrimidine biosynthesis. May also form UMP from uracil. Regulates the size of gut granules during embryonic development. Involved in resistance to DNA damaging agents including UV-C and X-ray radiation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20148972}. Note=Localizes near the apical surface of the embryonic intestine. Appears not to localize to gut granules. {ECO:0000269|PubMed:20148972}.
Interaction partners:
- Dihydroorotate dehydrogenase
- Dihydropyrimidine dehydrogenase [NADP
- Probable Golgi transport protein 1
- Multifunctional protein pyr-1
- Uracil phosphoribosyltransferase homolog
- Uridine and thymidine phosphorylase
- Trifunctional purine biosynthetic protein adenosine-3
- UMP-CMP kinase 2
- UMP-CMP kinase 1
- Uridine kinase
Sequence:
MSSLTDKTRNGALKRNLLRQMLKASVFKFGEFQLKSGQISPIYIDLRECFGHPGLLMLISEAISKQVEISEVQYAGVLGIPYAALPYASVAAGNYLKKPLLIVRKEAKSYGTKKLIEGLYQPNDRLILIEDVVTTGGSILDVVKVLHTENLVASDVFCILDREQGGRQKLQDAGVTLHSLLDMQTVLTFLYSTGAIGDEQWHGIVQALNLPYTSPTKLEINSELENLSSLPYVENVRTPLAERESLTESALIKKILGIMRRKKSNLCLAVDYTTVEQCLQMIELAGPFVLAIKLHADAITDFNEEFTRKLTTMANDMDFIIFEDRKFGDTGNTNLLQLTGAQKIANWADVVTVHAVQGSDSIAGVFRKLAKDPTYRLSGVLLIAQLSTKGSLTALEGYTETAVKIANENRDVISGFITQTRVSACSDLLNWTPGVNLDAKSDSAGQQWRGVDEAIEVQQNDIIIVGRGVTSSSEPVQQLKRYRQIAWDALTRSDDSI
Protein: Nuclear hormone receptor family member nhr-91 (Q9U2R6)
Organism: Caenorhabditis elegans
Function: Orphan nuclear receptor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
- Uncharacterized protein
Sequence:
MDVADSTSETPPVFDHDNLALAAQTNLLQFYLTHLASTLVPPMKLDMRDSMTPSFSQTESPNSETDDSTSAANKVLFSILGTPTTDSTSNAVSKSSSKLCSVCGDKSTGLHYGAATCEGCKGFFKRSVQNKKVYHCSQDNCCEIDKQNRNRCQSCRFRKCISKGMLTEAVREDRMPGGRNGNSIYSNYKQRRSIIRKTKDYVEEQERRPFQSLPSGKKLIKELVEMDCLDRLINLKGLRINPSANCDIAPACKRLTRIGDEIVEQLVEWTKTLPFFDELPVEAHTHLLTQRWAELVLLSAGYYACSVFTPDSPDTTEMIDETDEISFTNPQVNLRLLQNRLSLVLGKEIPLEHVAKEAGPLVTRFTTLLHSFSNLKVSPEAYVCIKAITLLHLSADSTLDRSIIDKVNTLQDHFVKTLQIHLHQPGEDAQTTSLAQILDWLPDLRNASSVLLHSKMFYVPFLLCKNPRRLVFDE
Protein: Uncharacterized protein C2F3.07c (O14090)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MLVRENNSNDRSIIEYVIKILLISGISRIIILILAMFESIRHIIFHNDTNPSDARKFQMAICRLSSQKSRKLKNPIESSTTSHKKKGYVRKCYECLQIQVS
Protein: Dynamin associated protein 160, isoform A (Q9VIF7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNSAVDAWAVTPRERLKYQEQFRALQPQAGFVTGAQAKGFFLQSQLPPLILGQIWALADTDSDGKMNINEFSIACKLINLKLRGMDVPKVLPPSLLSSLTGDVPSMTPRGSTSSLSPLDPLKGIVPAVAPVVPVVAPPVAVATVISPPGVSVPSGPTPPTSNPPSRHTSISERAPSIESVNQGEWAVQAAQKRKYTQVFNANDRTRSGYLTGSQARGVLVQSKLPQVTLAQIWTLSDIDGDGRLNCDEFILAMFLCEKAMAGEKIPVTLPQEWVPPNLRKIKSRPGSVSGVVSRPGSQPASRHASVSSQSGVGVVDADPTAGLPGQTSFEDKRKENYVKGQAELDRRRKIMEDQQRKEREERERKEREEADKREKARLEAERKQQEELERQLQRQREIEMEKEEQRKRELEAKEAARKELEKQRQQEWEQARIAEMNAQKEREQERVLKQKAHNTQLNVELSTLNEKIKELSQRICDTRAGVTNVKTVIDGMRTQRDTSMSEMSQLKARIKEQNAKLLQLTQERAKWEAKSKASGAALGGENAQQEQLNAAFAHKQLIINQIKDKVENISKEIESKKEDINTNDVQMSELKAELSALITKCEDLYKEYDVQRTSVLELKYNRKNETSVSSAWDTGSSSAWEETGTTVTDPYAVASNDISALAAPAVDLGGPAPEGFVKYQAVYEFNARNAEEITFVPGDIILVPLEQNAEPGWLAGEINGHTGWFPESYVEKLEVGEVAPVAAVEAPVDAQVATVADTYNDNINTSSIPAASADLTAAGDVEYYIAAYPYESAEEGDLSFSAGEMVMVIKKEGEWWTGTIGSRTGMFPSNYVQKADVGTASTAAAEPVESLDQETTLNGNAAYTAAPVEAQEQVYQPLPVQEPSEQPISSPGVGAEEAHEDLDTEVSQINTQSKTQSSEPAESYSRPMSRTSSMTPGMRAKRSEIAQVIAPYEATSTEQLSLTRGQLIMIRKKTDSGWWEGELQAKGRRRQIGWFPATYVKVLQGGRNSGRNTPVSGSRIEMTEQILDKVIALYPYKAQNDDELSFDKDDIISVLGRDEPEWWRGELNGLSGLFPSNYVGPFVTSGKPAKANGTTKK
Protein: EG:86E4.5 protein (LD39196p) (Oculocerebrorenal syndrome of lowe, isoform A) (Oculocerebrorenal syndrome of lowe, isoform B (EC 3.1.3.-, EC 3.1.3.36)) (O46094)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle, phagosome membrane {ECO:0000256|ARBA:ARBA00004580}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004146}.
Interaction partners:
- Phosphatidylinositol-3-phosphatase SAC1
- Inositol phosphatase interacting protein, isoform A
- Phosphatidylinositol 4-kinase alpha
- Phosphatidylinositol 4-phosphate 5-kinase type-1 sktl
- Phosphatidylinositol 4-kinase type 2
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Phosphatidylinositol 4-kinase beta
- LD21953p
- phosphatidylinositol-3,4-bisphosphate 4-phosphatase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma
Sequence:
MDTLSEAVANGTATAATRTTKDIVKERFKEDETIEYIFEAYQIKGPEYSNRLLALVSSQSGGTFAIIAFSYLRTPLSSANELIINKVFAIDHNFQLRQDSKSSITTQQFDLSTAEDGPIKYYYYATESHHYEEFVAKVISFKSTMAQHDPETVLNFRWLNDYRQIGEVKQELKKRESEYIVYKDIIIYCATWNVNNKTCSDSNNPLRAWLACSEKPPDIYAIGLQELDTPTKAMLNSTQVQAIEKQWIDKMMDSVHPDVEYEILMSHRLVATMLTVIVRKQLRQHIIRCRPKSVARGIFNTLGNKGGVAISLQLNEGNICFVNSHLAAHMGYVEERNQDYNAIVEGIRFDDGRTISDHDHIFWVGDLNYRIQEPPGQQRPGPLSDAQTYELLLQYDQLRQEMRRGKCFEGYTEGEIKFRPTYKYDPGTDNYDSSEKQRAPAYCDRVLWKGTRIEQLAYNSIMEIRQSDHKPVYAVFQVKVKTRDEVKYKRVQEEVLKAVDKRENDNQPQINVEKTVIDFGTVRFNEPSTRDFNVYNNCPLPVDFSFKEKDIHAICEPWLHVDPRQDSLLIDSARSIRLKMNANVRTIAGLLRKIRASDNFDILILHVENGRDIFITVTGDYQPSCFGLSMETMCRTDRPLSEYSQDQIKQLMNDESPEYRVTMPREFFLLIDYLYRQGSKQVGAFPSYDSRLSLGAQFNSVRDWLDTWSDDPFPANAETAAQALLLLLDLPEHALLEPVVENLLECTNKSQAMDYISLLSPPKRNVFMHLCMFLRAGIESQFYDLHQVASTFGRILLRSTERAAWMDYHSRCIQFMRLFIDTDVEAMGNGNEGAGTGTGSGSGTRAGLQA
Protein: Protein S100-A3 (Protein S-100E) (S100 calcium-binding protein A3) (P62818)
Organism: Mus musculus (Mouse)
Function: Binds both calcium and zinc. May be involved in calcium-dependent cuticle cell differentiation, hair shaft and hair cuticular barrier formation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Protein S100-A16
- S100 calcium binding protein A2
Sequence:
MTRPLEQAVAAIVCTFQEYAGRCGDKYKICQSELKELLQKELPTWTPSEFRECDYNKFMSVLDTNKDCEVDFGEYVRSLASLCLYCHEYFKECPPEPPCPQ
Protein: protein kinase C (EC 2.7.11.13) (O44393)
Organism: Pisaster ochraceus (Ochre sea star) (Asterias ochracea)
Subcellular location: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Midbody {ECO:0000256|ARBA:ARBA00004214}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
AGFQQNLEYIKEQIKKDIRKELKLKEGAENIRKVTTDKKSIANINNMVKQANIKLHELRQELNELNAHIVVNTDEITAASGDASPMSPVKSDGSTSDDTGAIRTGPTTNSRVFALEKQLAIEMKVKQGAENMIQMYTSGTKDRKLLAEAQQMLQDSKVKIEVIKMEIIKVQQMAGNSFIGDSSNVDGADLGYRRASAADLQLSPLEFRIEELRHHFKIELAVVEGFKNVTKMLSESRSSDKKGLAEAEKGMVESAHKLDILRLALEKRITELPPDHLDKMQQIRDELTSGKSVSYGTLPKPAALTGRLEVRLMGCQDLIESIPNRSKSNSISGGAFSPGESRGLLKGKASFHGRTGSRSSSTRRDELSNDICAILKLDNNPVAQTSFKPISNQCWNQRFSVELDKSRELEISVLYKDWRSLCAVKFLRLEHFLDNQRHGLCLNLEPGGMLFAEITFFNPSIERRTKLQRQRKIFPKYKGKNFLRANQMNINVATWGRLMKRAIPPNCTSPSTLGPAGLGSSLPPPVRERPAIPMQRLSFEGDLPEINQNMETSPKKTNGDPGDKRRVPENELEDVLSAFDFLKSPGSGSAPPTPDLPESESRPIVPSPSTPVPQPSNAVAQHEISSSSFVSMENFRCISVLGRGHFGKVLLAEYKNTGELFAIKALKKGDIIAREEVESLMCESRILETANSMRHPFLVNLFACFQTDAHVCFVMEYAIGGDLMMHIHTDVFSEPRTVFYAACVVLGLQYLHENNIVYRDLKLDNLLLDQEGFLKIADFGLCKEGMGFGDRTSTFCGTPEFLAPEVLTEASYTRAVDWWGLGVLIFEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAIAIMRRLLRRNPERRLGSSRRDAEDVKKQAFFRNVQWEELLMRKTTPPFVPNINHPEDVSNFDEEFTQERPVLTPPTRDPRAITDQEQNLFKDFNYTADWC
Protein: Lymphotactin (ATAC) (C motif chemokine 1) (Cytokine SCM-1) (Lymphotaxin) (SCM-1-alpha) (Small-inducible cytokine C1) (XC chemokine ligand 1) (P47992)
Organism: Homo sapiens (Human)
Function: Chemotactic activity for lymphocytes but not for monocytes or neutrophils. In thymus, mediates medullary accumulation of thymic dendritic cells and contributes to regulatoy T cell development, playing a role in self-tolerance establishment.
Subcellular location: Secreted.
Interaction partners:
- Chemokine XC receptor 1
- C-C motif chemokine 21
- C-X-C motif chemokine 9
- C-X-C motif chemokine 10
- C-X-C motif chemokine 11
- Stromal cell-derived factor 1
- Platelet factor 4
- C-X-C motif chemokine 2
- C-X-C motif chemokine 14
- C-C motif chemokine 5
Sequence:
MRLLILALLGICSLTAYIVEGVGSEVSDKRTCVSLTTQRLPVSRIKTYTITEGSLRAVIFITKRGLKVCADPQATWVRDVVRSMDRKSNTRNNMIQTKPTGTQQSTNTAVTLTG
Protein: Auxilin (EC 3.1.3.-) (DnaJ homolog subfamily C member 6) (Q80TZ3)
Organism: Mus musculus (Mouse)
Function: Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles. Plays a role in clathrin-mediated endocytosis in neurons.
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q27974}. Note=Appears on coated vesicles in successive transient bursts, immediately after the vesicle release from the plasma membrane. Recruitment to clathrin-coated vesicles depends on temporal variations in phosphoinositide composition of clathrin-coated vesicles. {ECO:0000250|UniProtKB:Q27974}.
Interaction partners:
- Clathrin heavy chain 1
- Heat shock cognate 71 kDa protein
- Clathrin heavy chain linker domain-containing protein 1
- Synaptojanin-1
- Clathrin light chain A
- Endophilin-A1
- DnaJ heat shock protein family
- Vacuolar protein sorting-associated protein 35
- Clathrin light chain B
- E3 ubiquitin-protein ligase parkin
Sequence:
MTNPKSGVAESAGLACSRAAAGENRMKDSENKGASSPDMEPSYGGGLFDMVKGGAGRLFSNLKDNLKDTLKDTSSRVIQSVSSYTKGDLDFTYVTSRIIVMSFPVDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQAPSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGLSPSHRRYLGYMCDLLADKPYRPHFKPLTIKAITVSPVPFFNKQRNGCRPYCDVLIGETKIYSTCTDFERMKEYRVQDGKIFIPLNITVQGDVIVSMYHLRSTIGSRLQAKVTNTQIFQLQFHSGFIPLDTTVLKFTKPELDACDVPEKYPQLFQVTLDIEVQPQDKVIDLTPPWEHYCTKDVNPSILFSSQQEHQDTLALGGQAPADLPPDHPRNLGQGGFFASLCWQDQKSEKSRCEEDHAALVNQESEQSDDELLTLSSPHGNAEGDKPHGAKKPGKKQQEPAAPPPPEEVDLLGLEGSDVSTNFSSLAAPPSNSELLSDLFGGVGATGPAQAGQAGVEDVFHPSGPVSAQSTPRRTATSASASPTLRVGEGATFDPFGAPAKPPGQDLLGSFLNTSSASSDPFLQPTRSPSPTVHASSTPAVNIQPDIAGGWDWHTKPGGFGMGSKSAATSPTGSSHGTPTHQSKPQTLDPFADLGTLGSSSFASKPTTPTGLGGGFPPLSSPQKASPQPMGGGWQQPAGYNWQQTQSKPQSSMPHSSPQNRPNYNVSFSAMPAGQSERGKGSTNLEGKQKAADFEDLLSSQGFNAHKDKKGPRTIAEMRKEEMAKEMDPEKLKILEWIEGKERNIRALLSTMHTVLWAGETKWKPVGMADLVTPEQVKKVYRRAVLVVHPDKATGQPYEQYAKMIFMELNDAWSEFENQGQKPLY
Protein: High-affinity nicotinic acid transporter (Nicotinic acid permease) (P53322)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the uptake of nicotinic acid.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- 3-hydroxyanthranilate 3,4-dioxygenase
- Kynurenine 3-monooxygenase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Uridine nucleosidase
- Purine nucleoside phosphorylase
- Glutamine-dependent NAD
- NAD-dependent histone deacetylase SIR2
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Nicotinamide riboside transporter 1
Sequence:
MSNKFTMESPKHLVDDVLFISPTNDGSEEKPTEVTFQEDEGHDASLHNRSHDKKSELATEREIMATTTDDDGIPSPSHPMEKRVLRKMDIYLIPLMGMLYFLSNLDKSNIGNAEVAGLSKDIHLVGTQYNTCVTVFFATYVLFDPIGTNLLKIMGPPLMMSICLTCFGAISLGTAWVKNYAQLIVVRLLLGAFEGMIYPAINMYLSVCYRREQYALRFAFVFSAACLSSSFGGLIAYGCSKISGSLKDWQYIYIVEGCISLGFVPFYAFGLSKNLEDSWFFNKEEKEYISERYKTMNTFDPDEKFEWFQVWQAVKDVKTWASAVALFGIDLTTFGLTVFLPIIITSMGFTNVRAQLMTVPIYFLTAIVFFICAVWSDRIKLRSPFILGACLTTSIGIAIVLGSQVHGVRYFGVYILCMGIYVNAACNCLWLSGNTGNYFKRATALGINLFFGSGSGLVSGQIFVAKDKPRYIKGLSISLAFQVFSIFMTVVQIFLYKRENDKKKAIIDRCNELGEPIPYDERLSDKNPEFKYMY
Protein: Large ribosomal subunit protein uL13c (50S ribosomal protein L13, chloroplastic) (CL13) (Protein EMBRYO DEFECTIVE 1473) (Q9SYL9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Large ribosomal subunit protein bL21c
- Large ribosomal subunit protein uL24c
- 50S ribosomal protein L20
- Large ribosomal subunit protein uL6c
- Large ribosomal subunit protein uL4c
- Large ribosomal subunit protein uL5c
- Large ribosomal subunit protein eL38z/eL38y
- Small ribosomal subunit protein uS9c
- Large ribosomal subunit protein uL3c
- Small ribosomal subunit protein uS14m
Sequence:
MAVLCSSSTVILSSSSVKSSGSERKSPFLGFSLTAISKPSVRVGIYANSKRGLQVKCEAEPTTTTSLVPANQRWMFDEEEANGPDIWNTTWYPKASDHVNTDKPWFVVDATDKILGRLASTIANHIRGKNLASYTPSVDMGAFVIVVNAEKVAVSGKKRNQKLYRRHSGRPGGMTVETFDQLQQRIPERIVEHAVRGMLPKGRLGRALFNHLKVYKGPDHPHEAQKPLDLPIRDKRIQLQK
Protein: receptor protein serine/threonine kinase (EC 2.7.11.30) (A1Z7L8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- LD29161p
- Mothers against decapentaplegic homolog
- Inhibin beta chain
- Protein decapentaplegic
- Serine/threonine-protein kinase receptor
- Dawdle, isoform A
- Peptidyl-prolyl cis-trans isomerase Fkbp12
- Maverick
- E3 ubiquitin-protein ligase Smurf1
- Protein screw
Sequence:
MLSALRLIFLGALLGASVCASPIEFVMDTSLNGSRSDPATATHPGKWPPTTKAPALRAPAGTAGHAYQSPSSSLAADNRSHDNNNASAVSMLLPQDGDASGAVAPAVTPQLPIYIAQPSAKKPENKIKCHCDTCKESNNICETDGFCFTSVEKNSDGSIIFSYRCLHKSQIFPPGRSIWCNDGLHGGPTARPVGRNGAHACCKDRDFCNRFLWPKTKDQRSDRVEEGRQISVQDYVPHRLTSWEFVAIILGATLFICFTGTSTWYYCQRRKRMASGRTFAKEDSAYDPILNGNTTIHDIIEMTTSGSGSAGLPLLVQRSIARQVQLCHVIGKGRFGEVWRGRWRGENVAVKIFSSREECSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVTDYHENGSLFDYLTTHPVDTNTMLNMSLSIATGLAHLHMDIVGTRGKPAIAHRDLKSKNILVKSNLSCAIGDLGLAVRHVEKNDSVDIPSTHRVGTKRYMAPEVLDESMNDQHFDSYKRADVYAFGLILWEIARRCNMGMIYDEYQLPYYDVVQPDPSIEEMKKVVCIEKCRPNIPNRWHASDVLHNMAKVMKECWYPNPVARLTALRIKKTLASISVEDKVKN
Protein: C2H2 finger domain transcription factor (Eurofung) (C8VUD1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MQWITSPLLGLEEVKPILAPRPPTPPPFAHQGLSPESSVKGADKGSHKSKQLSLQIGAAAANAALLRNNFAAHFPDLWRYEIENPLLDPSSVDRHSNRKLNQARPVNSFKSAPEPKPIELEFKADLKGIAEEALLKEAKTQQPPSREPLEEKENGNVVLPPLSALVNGSAGPKAQPILGPSPSPLSKFHISAPESRDSLAAFRNPPAAQTADTSGLRLPPIQTKLSQLNELGPVLPPPNGPSPRPVGTPYSLPPVTAVSPPLTRVDTNPREQYHSAASLAQSKIPPTPYSHLSPASTQAISTASSPASQQPYWRNVKAAYPYDPPSTASNRSPASSYPTPIERAPTGACEPVGFAPSSQGSTAAPTGTFKCSHPGCTAPPFQTQYLLNSHANVHSQDRPHFCPIEGCSRGPGGKGFKRKNEMIRHGLVHNSPGYVCPFCPDQQHKYPRPDNLQRHVRVHHMDKNKDDPALRHVLSQRPEGSGRGRRRRMNPQ
Protein: Transmembrane protein 39B (Q9GZU3)
Organism: Homo sapiens (Human)
Function: May protect the cells against DNA damage caused by exposure to the cold-warming stress and facilitates tissue damage repair during the recovery phase.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q7ZW11}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGGRRGPNRTSYCRNPLCEPGSSGGSSGSHTSSASVTSVRSRTRSSSGTGLSSPPLATQTVVPLQHCKIPELPVQASILFELQLFFCQLIALFVHYINIYKTVWWYPPSHPPSHTSLNFHLIDFNLLMVTTIVLGRRFIGSIVKEASQRGKVSLFRSILLFLTRFTVLTATGWSLCRSLIHLFRTYSFLNLLFLCYPFGMYIPFLQLNCDLRKTSLFNHMASMGPREAVSGLAKSRDYLLTLRETWKQHTRQLYGPDAMPTHACCLSPSLIRSEVEFLKMDFNWRMKEVLVSSMLSAYYVAFVPVWFVKNTHYYDKRWSCELFLLVSISTSVILMQHLLPASYCDLLHKAAAHLGCWQKVDPALCSNVLQHPWTEECMWPQGVLVKHSKNVYKAVGHYNVAIPSDVSHFRFHFFFSKPLRILNILLLLEGAVIVYQLYSLMSSEKWHQTISLALILFSNYYAFFKLLRDRLVLGKAYSYSASPQRDLDHRFS
Protein: Neuralized-like protein 2 (Q9D0S4)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the process of myofiber differentiation and maturation. Probable substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex, which mediates the ubiquitination of proteins. Probably contributes to catalysis through recognition and positioning of the substrate and the ubiquitin-conjugating enzyme. During myogenesis, controls the ubiquitination and degradation of the specific pool of CTNNB1/beta-catenin located at the sarcolemma.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14960280}. Note=In primary myoblasts, localized predominantly at the tips of differentiating myofibers.
Interaction partners:
- Elongin-B
- Elongin-C
- E3 ubiquitin-protein ligase RBX1
- Cullin-2
- Protein sel-1 homolog 1
- E3 ubiquitin-protein ligase synoviolin
- von Hippel-Lindau disease tumor suppressor
- Ubiquitin-like-conjugating enzyme ATG3
- Family with sequence similarity 8, member A1
Sequence:
MADPSEHVGLGGPRSPARPEPPPTRFHQVHGANIRMDPSGTRATRVESFAHGVCFSREPLAPGQVFLVEIEEKELGWCGHLRLGLTALDPASLAAVPEFSLPDLVSLGHSWVFAITRHHNRVPREGQPEAEAAVPSGPQALLVEPYLRIEQFRIPRDRLVGRSRPGLYSHLLDQLYEQNVLPPTARRSRLGVLFCPREDGTADMHIIINGEDMGPSARGLPAAQPLYAVVDVFASTKSVRLVQLEYGLPSLQTLCRLVIHKRVVHRLAIDVLHLPKGLKDFCKYE