wanglab/gogpt-training-data huggingface dataset:
Protein: Multiple C2 and transmembrane domain-containing protein 2 (Q6DN12)
Organism: Homo sapiens (Human)
Function: Might play a role in the development of cardiac outflow tract.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDLDKPSVWGSLKQRTRPLLINLSKKKVKKNPSKPPDLRARHHLDRRLSLSVPDLLEAEALAPEGRPYSGPQSSYTSVPSSLSTAGIFPKSSSSSLKQSEEELDWSQEEASHLHVVETDSEEAYASPAERRRVSSNGIFDLQKTSLGGDAPEEPEKLCGSSDLNASMTSQHFEEQSVPGEASDGLSNLPSPFAYLLTIHLKEGRNLVVRDRCGTSDPYVKFKLNGKTLYKSKVIYKNLNPVWDEIVVLPIQSLDQKLRVKVYDRDLTTSDFMGSAFVILSDLELNRTTEHILKLEDPNSLEDDMGVIVLNLNLVVKQGDFKRHRWSNRKRLSASKSSLIRNLRLSESLKKNQLWNGIISITLLEGKNVSGGSMTEMFVQLKLGDQRYKSKTLCKSANPQWQEQFDFHYFSDRMGILDIEVWGKDNKKHEERLGTCKVDISALPLKQANCLELPLDSCLGALLMLVTLTPCAGVSVSDLCVCPLADLSERKQITQRYCLQNSLKDVKDVGILQVKVLKAADLLAADFSGKSDPFCLLELGNDRLQTHTVYKNLNPEWNKVFTFPIKDIHDVLEVTVFDEDGDKPPDFLGKVAIPLLSIRDGQPNCYVLKNKDLEQAFKGVIYLEMDLIYNPVKASIRTFTPREKRFVEDSRKLSKKILSRDVDRVKRITMAIWNTMQFLKSCFQWESTLRSTIAFAVFLITVWNFELYMIPLALLLIFVYNFIRPVKGKVSSIQDSQESTDIDDEEDEDDKESEKKGLIERIYMVQDIVSTVQNVLEEIASFGERIKNTFNWTVPFLSSLACLILAAATIILYFIPLRYIILIWGINKFTKKLRNPYSIDNNELLDFLSRVPSDVQKVQYAELKLCSSHSPLRKKRSAL
Protein: Activated in Blocked Unfolded protein response (Prion-like-(Q/N-rich)-domain-bearing protein) (G5EGB7)
Organism: Caenorhabditis elegans
Interaction partners:
- LiPocalin-Related protein
- peptidylprolyl isomerase
- LiPocalin-Related protein
- peptidylprolyl isomerase
- Activated in Blocked Unfolded protein response
- LiPocalin-Related protein
- LiPocalin-Related protein
Sequence:
MRFITLAVFFACALVASSSVLREKRHCGCAQPQQSQCSCQQVQQTQSCSCQSAPVQQQAPSCSCAQPQQTQTVQVQSTQCAPACQQSCRQQCQSAPAVSQCQPMCQQQCQSQCTPMYNPPATTTTTPAPVVQCQPMCQQQCQSTCVQQQQPVSQCQPQCQQQCNVACDATTTTTSAPQVIHIQLEIQQAQVQCQPACQQQCQSSCVQQQQPAKQCASSCNTQCTNACQQTAQATQQVIYGQNSNTQMYDPYNNQQQQQANCAPACQPACDNSCIQQTAAPIYNPTTTSAPQVVQIVLQASVAQSSQCAPQCEQSCQQQCVQQQQPVAQCQSACQSSCSSSCQAAQPATVACQQAPQSNQCSCQSNYSPCGQGQCCRRK
Protein: Ependymin (B9EN47)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MRTFVLLMCLAVGCLAQVPHTCRSPPLLTGALSVANEKFYANAKYTYDAMPKRIRFKEIGSYENKTFGVDALLLFREGVMYTINHRNKTCKKERLKREDFHPMEIPADAALLGQVILGSSSGPGQGLLVNTWYGEVATPSGEDKWMSTFTEFGCIPVSSTYYTDKTGWILTTFFNIVVGITDPQEFFPPKFCQDAKLDETAEAANFYSIFKNLTKYS
Protein: Pentatricopeptide repeat-containing protein At2g28050 (Q9ZUU7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Putative pentatricopeptide repeat-containing protein At3g01580
- Pentatricopeptide repeat-containing protein At1g09220
- Pentatricopeptide repeat-containing protein At1g06270
- Pentatricopeptide repeat-containing protein At2g33760
- Tetratricopeptide repeat
- Pentatricopeptide repeat-containing protein At3g13880
- Pentatricopeptide repeat-containing protein At3g26540
- Pentatricopeptide repeat-containing protein At3g49710
- Pentatricopeptide repeat-containing protein At2g40720
- Pentatricopeptide repeat-containing protein At1g02370
Sequence:
MTPQCFLKTLKTAKQTYTFSIYKLLLNSSSINQTLASPETPLSDLNLSTLRRILSDPDIKSWKCISLFNFILENPSLFSFQPDLRTHLSLTFRVLSERRFSYAKELLKPVAIDDILRYPFNVIVSSVIDECGCEKKVVGRFFNSMIMVYSDNGKFSEVVEVFEYMKNNEVKIDEKTCTLHLLNLKRCDQMELARDFFSLMVESGIDVVTVYSLTVVVTVLCCNGEITRARELVEEMGLVKGVKANIVTFKSMIGCCVKRWDFEELDLVLKLMEKESVMLDLDSYKVLIDGFTSYGKVEEAERLVLMMHDKKLRVESYLYNLIMNGYSRFGLVEKVIELYSEMSSRGVTPNKDTYWVLMNGLCKAGKVCEAMSFLNELRVNEFEIDEEMYSTLSEECYRVGMIDKSLEVVAEMIRDGFIPGATICERLADSLFEVNRKEAQMLITIVVKCGIKPKSCSQYGLK
Protein: Well-rounded, isoform B (Q8IN89)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit
- Serine/threonine-protein phosphatase PP2A
- Protein phosphatase PP2A 55 kDa regulatory subunit
- MIP22305p
- Protein phosphatase methylesterase 1
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine protein phosphatase 2A regulatory subunit
- Uncharacterized protein, isoform B
- Serine/threonine-protein phosphatase
- Protein kinase shaggy
Sequence:
MVFGAMLLTGNGLKGPKQQQQQHQQEPQQQQQQSQQQQQEQKKPAPIKSSSKEQETQPIAAGYYALGIRIPKSPSFHSGLDQLADDELDDQVQDQQQEQQQTGSRFRFSSVEELKAKFEGRKTPLSPPEAAAGGAAGSGAPTTSSSPSSSSTSSNSSASALSSLSQAASSSLASAAANSSASSSAATYGGGANSAAAALIASSPFGSQSSTSSLSLSSNAGMSKNAAGAGSGSGSGTTSTGAASGSNSLVSTLAQHFSAATSAAASAAAAAASSASAASSSSASSSSTATNNAASSSIAASKSPVSAAAAIKNILNATKSVGTSAAAAAAAAATSSSSSPSSAAAVPSSAATAVAAVPTTSDVPAEEMRPTVAQNLVGGISISLGIGQRNGGAAPASSAVMVTPNATMVVTTSSLSIRQNGDILPGHPAGLQPSPQTLQQLTGSPGRARDRNLFYTPPTASVAMALPALRETAASEREELFIQKIQQCCTLFDFSEPLSDLKFKEVKRAALHEMVDFLTNQNGVITEVIYPEAINMFAVNLFRTLPPSSNPNGAEFDPEEDEPTLESSWPHLQLVYELFLRFLESPDFQPSMAKRFIDHQFVLQLLDLFDSEDPRERDFLKTVLHRIYGKFLGLRAFIRKQINNVFYRFIYETEHHNGIAELLEILGSIINGFALPLKEEHKQFLLKVLLPLHKAKSLSVYHPQLTYCVVQFLEKDPSLSEAVIKSLLKFWPKTHSPKEVMFLNELEELLDVIEPAEFQKVMVPLFRQIAKCVSSPHFQVAERALYYWNNEYIMSLITDNSAVILPIMFPALNRNSKTHWNKTIHGLIYNALKLFMEIDQRLFDECSKNYKQEKQMEREKLSQREELWQQVESLAKTNPEWTKARRFNDCLPVSDSRALCDQYSENSDSAYDQSEQRARQPPPPLPPQKQAHQEPREIRGERNKDKPLLRRKSDLPSDSGTVKALNEHKRTDEYLTTPPPDGNY
Protein: Centrin-2 (Q8IL07)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Tubulin alpha chain
- Thioredoxin-like protein
- NADH-cytochrome b5 reductase, putative
Sequence:
MTDNTAVRRRYEKSFTERPGFTEDEIEEIREAFNLLDTDGTGTIDPKEIKCAMQSLGLDAKNPMIFRMIADLEKDGYSSIDFEEFMEVITSKLGNKDTREGIQRIFNLFDDDKTGSISLKNLKRVAKELGETLTDEELRDMIDRADSKGEGEISFEDFYTIMTKKSFL
Protein: E3 ubiquitin-protein ligase SIAH2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH2) (Seven in absentia homolog 2) (Siah-2) (hSiah2) (O43255)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (GPS2, POU2AF1, PML, NCOR1), a cell surface receptor (DCC), an antiapoptotic protein (BAG1), and a protein involved in synaptic vesicle function in neurons (SYP). Mediates ubiquitination and proteasomal degradation of DYRK2 in response to hypoxia. It is thereby involved in apoptosis, tumor suppression, cell cycle, transcription and signaling processes. Has some overlapping function with SIAH1. Triggers the ubiquitin-mediated degradation of TRAF2, whereas SIAH1 does not. Promotes monoubiquitination of SNCA. Regulates cellular clock function via ubiquitination of the circadian transcriptional repressors NR1D1 and NR1D2 leading to their proteasomal degradation. Plays an important role in mediating the rhythmic degradation/clearance of NR1D1 and NR1D2 contributing to their circadian profile of protein abundance. Mediates ubiquitination and degradation of EGLN2 and EGLN3 in response to the unfolded protein response (UPR), leading to their degradation and subsequent stabilization of ATF4 (By similarity). Also part of the Wnt signaling pathway in which it mediates the Wnt-induced ubiquitin-mediated proteasomal degradation of AXIN1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19224863, ECO:0000269|PubMed:22878263}. Nucleus {ECO:0000269|PubMed:22878263}. Note=Predominantly cytoplasmic. Partially nuclear. {ECO:0000269|PubMed:22878263}.
Interaction partners:
- Prolyl hydroxylase EGLN3
- Prolyl hydroxylase EGLN2
- Serine/threonine-protein kinase LATS2
- Ubiquitin carboxyl-terminal hydrolase 13
- E3 ubiquitin-protein ligase SIAH1
- Alpha-synuclein
- Egl nine homolog 1
- Hypoxia-inducible factor 1-alpha
- Homeodomain-interacting protein kinase 2
- Synphilin-1
Sequence:
MSRPSSTGPSANKPCSKQPPPQPQHTPSPAAPPAAATISAAGPGSSAVPAAAAVISGPGGGGGAGPVSPQHHELTSLFECPVCFDYVLPPILQCQAGHLVCNQCRQKLSCCPTCRGALTPSIRNLAMEKVASAVLFPCKYATTGCSLTLHHTEKPEHEDICEYRPYSCPCPGASCKWQGSLEAVMSHLMHAHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGHHFMLVLEKQEKYEGHQQFFAIVLLIGTRKQAENFAYRLELNGNRRRLTWEATPRSIHDGVAAAIMNSDCLVFDTAIAHLFADNGNLGINVTISTCCP
Protein: N-acetyltransferase SLI1 (EC 2.3.1.-) (Sphingosine-like immunosuppressant resistant protein 1) (P53304)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Confers resistance to the sphingolipid biosynthesis inhibitor drug myriocin (ISP-1). Inactivates ISP-1 by converting it into N-acetyl-myriocin. Cooperates with YPK1 in mediating resistance to myriocin.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:15025559}.
Interaction partners:
- Serine/threonine-protein kinase YPK1
- Alcohol O-acetyltransferase 2
- Ethanol acetyltransferase 1
Sequence:
MNLKLSAIESYFFHRSRLNLHSCFYVGIKLNELPKKSQLIAALKYTVIQHERLTCNVFYDELKKENFLQNILEPLKFCDLVEYRHDWDQLGETEINHIFQRYNFSYNENKPLWKILILPNQNQMLLLTDHVLMDGMSAIHVWETFMEGLQMQQPVEIDETIYSPSLNSSTEKIMSAPLYGDWPIPWNWHIVRQLVSRLHYWFPQTVVKNNRNLIQFANYSFPKDLLDDKPSDGTQKYKVKNTNHQWEFRLSPTHLNDILQECKANNTSLTSLLGALVCTSFEKIAAHEYTGSFLKIELPMNIRKPFERVLKLPSDDKLAVGNFIAVIEFNHKLHQNRGIWDIASQIQRAIRSSSEDKIIDKVNEVKLLEVISSQQYIEDKISLNNGPSSTFEVTNLGFQTFKDACNTSLPFYIVDATFNEPQGISSIFSLSVISTPGNGLHCCISYPNTLTKVLEPHWQYMKDYLNLY
Protein: Probable syndecan (P50605)
Organism: Caenorhabditis elegans
Function: Cell surface proteoglycan that bears heparan sulfate (By similarity). Required for correct mitotic spindle orientation of the ABar blastomere division plane and this may be through modulation of astral microtubule array, and in association with the wnt-signaling proteins mig-5 and dsh-2. Involved in the migration of AQR and PQR neurons, which descend from the Q neuroblasts. Promotes the axon guidance of D-type motor neurons.
Subcellular location: Membrane {ECO:0000269|PubMed:25344071}; Single-pass type I membrane protein {ECO:0000255}. Cell surface {ECO:0000269|PubMed:25344071}. Cell junction {ECO:0000269|PubMed:25344071}. Cytoplasm {ECO:0000269|PubMed:25344071}. Note=Initially localizes to the ABar blastomere cell surface during interphase and prophase, and is internalized during metaphase and anaphase. {ECO:0000269|PubMed:25344071}.
Interaction partners:
- GlyPicaN
- Protein let-756
- Heparan sulfate 2-O-sulfotransferase hst-2
- D-glucuronyl C5-epimerase
- Heparan-sulfate 6-O-sulfotransferase
- Sulfotransferase domain-containing protein
- Sulfotransferase domain-containing protein
- LONg
- Agrin
- Fibronectin type-III domain-containing protein
Sequence:
MILKLNFCLSTYSVLILLSLSTQAFAANQAKTKVVPSSTISTKSLKNGISEQVEGSANIPGRLADIEVNGSGYPTDDEDGDDVHGSGKPPSSATTKSDKVTSPSHAVVTAKPTTVPTTTASFKPPVQPKPKPAANDKEIKVEEDEDDDEDEDEDDEDDEEDFADENIHNDEDFFTTTTTTTYRPIVVATTSTPRSAATNPPRQQPPMVTSTISSGPFSPFHETLANGFYAAIAGGVLVAVITAILLVLFVVFRIRKKDEGSYALDEPKQARPYASYGYTKASTKEFYA
Protein: Vacuolar-sorting receptor 4 (AtVSR4) (BP80-like protein a) (AtBP80a) (Epidermal growth factor receptor-like protein 2b) (AtELP2b) (Q56ZQ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Vacuolar-sorting receptor (VSR) involved in clathrin-coated vesicles sorting from Golgi apparatus to vacuoles.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Prevacuolar compartment membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Receptor homology region, transmembrane domain- and RING domain-containing protein 1
- PX domain-containing protein EREL1
- Protein kinase superfamily protein
- RING-type E3 ubiquitin transferase
- Vesicle transport v-SNARE 11
- Vacuolar protein sorting-associated protein 29
- Clathrin interactor EPSIN 1
- Protein MODIFIED TRANSPORT TO THE VACUOLE 1
- ADP-ribosylation factor C1
- BTB/POZ domain-containing protein At1g55760
Sequence:
MKQLLCYLPWLLLLSLVVSPFNEARFVVEKNSLSVTSPESIKGTHDSAIGNFGIPQYGGSMAGTVVYPKENQKSCKEFSDFSISFKSQPGALPTFLLVDRGDCFFALKVWNAQKAGASAVLVADNVDEPLITMDTPEEDVSSAKYIENITIPSALVTKGFGEKLKKAISGGDMVNLNLDWREAVPHPDDRVEYELWTNSNDECGVKCDMLMEFVKDFKGAAQILEKGGFTQFRPHYITWYCPHAFTLSRQCKSQCINKGRYCAPDPEQDFSSGYDGKDVVVENLRQLCVYKVANETGKPWVWWDYVTDFQIRCPMKEKKYNKDCAESVIKSLGIDSRKIDKCMGDPDADLDNPVLKEEQDAQVGKGTRGDVTILPTLVVNNRQYRGKLEKSAVLKALCSGFEESTEPAICLSTDMETNECLDNNGGCWQDKSANITACKDTFRGKVCVCPIVDGVRFKGDGYSHCEPSGPGRCTINNGGCWHEERDGHAFSACVDKDSVKCECPPGFKGDGVKKCEDINECKEKKACQCPECSCKNTWGSYECSCSGDLLYMRDHDTCISKTGSQVKSAWAAVWLIMLSLGLAAAGAYLVYKYRLRQYMDSEIRAIMAQYMPLDSQPEVPNHTNDERA
Protein: Phosphatidylinositol-3-phosphatase SAC1 (EC 3.1.3.64) (Phosphatidylinositol-4-phosphate phosphatase) (Suppressor of actin mutations 1-like protein) (Q9W0I6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Phosphoinositide phosphatase which catalyzes the hydrolysis of phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P) (By similarity). Has low activity towards phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P32368}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P32368}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phosphatidylinositol 4-kinase alpha
- EG:86E4.5 protein
- Phosphatidylinositol 4-kinase beta
- Phosphatidylinositol 4-kinase type 2
- Inositol polyphosphate 5-phosphatase E
- Golgi phosphoprotein 3 homolog sauron
- phosphatidylinositol-3,5-bisphosphate 3-phosphatase
- Phosphatidylinositol 4-phosphate 5-kinase type-1 sktl
- phosphatidylinositol-3,5-bisphosphate 3-phosphatase
- phosphoinositide 5-phosphatase
Sequence:
MDSREENAVYDDMNLYIAPQSFIIEPNGGDELLVIGRHDKVTRVQPASGGLVANLRPTRRICGVLGTIHLLSCDYLLVATHRLFVGVLNGAVVWRLAGYDIIPYIPNSFQRKENENYLRLLRQTLDTKFFYFSYRYDLTNSLQRQREVAQSRPEVSGLLQRAEQRFVWNGYVLRQFNCDKMEKFQLPLVLGFVSINQVQINGQTFFWSIITRRSVQRAGTRLFCRGSDEQGHVANFVETEQIVEFNGQLTGFVQTRGSMPFHWHQLPNLRYKPRPVLVPGKDHLAACGLHFKEQIRLYGNNVAVNLVDHKGAEGELEATYARLVREMGNPQVRYESFDFHSECRKMRWDRLNILIDRLAHEQDQFGVYHVFDDGKLVSTQTGVFRTNCIDCLDRTNVVQSMLARRSLTAVLQKLGVLHVGQKVEHASDIFESIFKGVWADNADLVSLQYSGTCALKTDFTRTGKRTKSGAMQDGKNSLMRYYLNNFADGQRQDSIDLFLGKYLVNDNEGGAVPSPLESKHGWRFFTFPSVLLVAVAMFMITMTYPAEFNTENLLFMLFWGAMIAVSATGILHYGVEFVQWPRLFPPISFRDP
Protein: Bestrophin homolog (Q9V3J6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU363126}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363126}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTITYTGEVATCRGFGCFLKLLLRWRGSIYKLVWLDLLAFLTIYYAINMVYRFGLNPAQKETFEAIVQYCDSYRELIPLSFVLGFYVSIVMTRWWNQYTSIPWPDPIAVFVSSNVHGQDERGRMMRRTIMRYVCLCLTMVLANVSPRVKKRFPGLNNLVEAGLLNDNEKTIIETMNKAFPRPSKHWLPIVWAASIITRARKEGRIRDDFAVKTIIDELNKFRGQCGLLISYDTISVPLVYTQVVTLAVYSYFLTCCMGQQWTDGKVVGNTTYLNKVDLYFPVFTTLQFFFYMGWLKVAESLINPFGEDDDDFEVNWMVDRNLQVSYLIVDEMHHDHPELLKDQYWDEVFPNELPYTIAAERFRENHPEPSTAKIEVPKNAAMPSTMSSVRIDEMADDASGIHFSAGNGKMRLDSSPSLVSVSGTLSRVNTVASALKRFLSRDDSRPGSATPSQDQPYKFPASASSASLSGAVVGSATSAGKPAGSLRITQQVIEEVDEQATITSMRANDPRPNVMDIFAQTSSGAGTSGPLQPPPAHSEPVDIPSRPPSYNRAQSQYEPNLFPPGGVDALLSTSAPAGGSPLLLSNAATAPSSPVGESSKSLYDPQKGASRETVESMDLRSSTDLLGDAAVQPEDEGDDFDKLKAEREKEKLMRQQKNLARTISTAPGMEATAVPMVPMVPVNVAVQQAQLQPVASSADLLAGGDQFSNSTMKSEDAINGS
Protein: AT03020p (Q8MSP7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEQLAATSAQLLHAKPATPGTPATPTPSATKAKEFVCSEPLSPVDIVDTINFDLVAQHMERLTLADPGDLDPRAELIEAVNKTLVNKPLVRSSSAACASTICSSPLLTYARTKSLGAKASTLGGGVPIKLPTAEQLAELEEANKLSAESLDRLTDIKPKFAARLSELARLNNRPLSSSSICSTSSSSSSGSDQLLNGKLMATSYLASVESLAESENELGDQHHPPAMSVLEKTCLEIVDSERSFVEDLGQVIKGYLQDWKERACLRVDELQILFANIEEIYEFNSMLLQRLINTGRDPGRIARCFIDLRDGFDVYTTYCTSYPEAISLLTKLLQATHTYSLLASTQKLLQHRLPLGSYLLKPVQRILKYHLLLDSLRKHCDVKEVVEAHVIMRQVAHNIDQVKRKQEQQSRVKELSGILDGWLGPELTVLGELRQEGLLMEQHNKQRLVLLFATMLIITKQKEDGRLQFKTYISQNNLMLSEHLPGEPTSFYVIPFDEPRHQIKLTARNRDQKRIWTQHIKGVMLEKLDIPMRAKELVYQLGNEEDRTPDRSTWKWSLHSGSNSTPTYLERRNACRRSEIRQRNSKFKRKTVANSSSFDSFNESLEQEEESVSQAKPSKPLARNNSLDDTALQKLAAAMRYRKRDAAVKEEMKTPVKEPCKCDQDAKQDERIEPCSCILRDQRSRSAKSQSPVFSYKALKERSKSVPRIGGFSLDEEAEREREQDEDSAASLRGSKPDLSERKTKGKGFFEVKQYNHKTMPKKIANLKKQRSSTTKSCSRFYMDLSEFDSSSSTVLKITESTEELRPDGEIELAQEAATLDESTQDQYYSPDNETELLSPAEKSKRDAQIVLDLLKNSKEFERIYNKQQKRRESPVSPVSPDISRGPILPPPRPPSRSPPPLELEEQEKKPVEEVDSVSEEPIYETLLRNVHVPYKFSPVLGRAKSSQILKKRSKTAPAASRPESDYVTLVYSPEGVLQRVGEEVVQRDSCSSSTTSTSSNGSGSTLKRDSQSTVINLLMEAAQEHGSRPLPKNSVSGSESSLLPRALKSIDNLSMAFGRSNRPPERRVSDVSEMCRQSVLHRQGSEAVSERMAHVDYADPKALFGLGVLNHSERDSVFSLTSSSSDSMCEQQRKRSGVDPPGATFEYEQQVEDSLENDFRDSAIYSDDNEKRSGDYDVHLRRPSSPPPPPPPLGPRPHQPPQIAPKPSKDQLIQQRSGVIVCQSASRSWVLQQIENFNK
Protein: Thymidine phosphorylase (TP) (EC 2.4.2.4) (Gliostatin) (Platelet-derived endothelial cell growth factor) (PD-ECGF) (TdRPase) (P19971)
Organism: Homo sapiens (Human)
Function: May have a role in maintaining the integrity of the blood vessels. Has growth promoting activity on endothelial cells, angiogenic activity in vivo and chemotactic activity on endothelial cells in vitro.
Interaction partners:
- Uridine phosphorylase 1
- Cytidine deaminase
- Uridine phosphorylase 2
- Dihydropyrimidine dehydrogenase [NADP
- Thymidine kinase 2, mitochondrial
- Uridine 5'-monophosphate synthase
- Uracil phosphoribosyltransferase homolog
- 5'
- Purine nucleoside phosphorylase
- 5'
Sequence:
MAALMTPGTGAPPAPGDFSGEGSQGLPDPSPEPKQLPELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQQLVDKHSTGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVPADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKPLGRCVGHALEVEEALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPGLARALCSGSPAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRGTPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAPSPFAELVLPPQQ
Protein: Netrin-1 (Q90922)
Organism: Gallus gallus (Chicken)
Function: Netrins control guidance of CNS commissural axons and peripheral motor axons. Promotes neurite outgrowth from commissural axons but acts as a chemorepellent for trochlear motor axons. These effects are mediated by distinct receptors.
Subcellular location: Secreted {ECO:0000250|UniProtKB:O95631}. Cytoplasm {ECO:0000250|UniProtKB:O95631}. Note=Mainly secreted. {ECO:0000250|UniProtKB:O95631}.
Interaction partners:
- Neogenin
- Netrin receptor UNC5C
- Unc-5 netrin receptor A.
- Cell adhesion molecule DSCAM
- Uncharacterized protein.
- Netrin receptor UNC5
- Draxin
- Netrin receptor UNC5
- Semaphorin-3A
- Uncharacterized protein.
Sequence:
MPRRGAEGPLALLLAAAWLAQPLRGGYPGLNMFAVQTAQPDPCYDEHGLPRRCIPDFVNSAFGKEVKVSSTCGKPPSRYCVVTEKGEEQVRSCHLCNASDPKRAHPPSFLTDLNNPHNLTCWQSDSYVQYPHNVTLTLSLGKKFEVTYVSLQFCSPRPESMAIYKSMDYGKTWVPFQFYSTQCRKMYNKPSRAAITKQNEQEAICTDSHTDVRPLSGGLIAFSTLDGRPTAHDFDNSPVLQDWVTATDIKVTFSRLHTFGDENEDDSELARDSYFYAVSDLQVGGRCKCNGHASRCVRDRDDNLVCDCKHNTAGPECDRCKPFHYDRPWQRATAREANECVACNCNLHARRCRFNMELYKLSGRKSGGVCLNCRHNTAGRHCHYCKEGFYRDLSKPISHRKACKECDCHPVGAAGQTCNQTTGQCPCKDGVTGITCNRCAKGYQQSRSPIAPCIKIPAAPPPTAASSTEEPADCDSYCKASKGKLKINMKKYCKKDYAVQIHILKAEKNADWWKFTVNIISVYKQGSNRLRRGDQTLWVHAKDIACKCPKVKPMKKYLLLGSTEDSPDQSGIIADKSSLVIQWRDTWARRLRKFQQREKKGKCRKA
Protein: Demethylmacrocin O-methyltransferase (EC 2.1.1.102) (Tylosin biosynthesis protein E) (Q9ZHQ4)
Organism: Streptomyces fradiae (Streptomyces roseoflavus)
Function: O-methyltransferase that catalyzes the conversion of demethylmacrocin to macrocin, the penultimate step of tylosin antibiotic biosynthesis. Also able to mediate the conversion of demethyllactenocin to lactenocin.
Interaction partners:
Sequence:
MAVQKEATLVRQIIRAAGGHAADVRELVAEHGPEAVTAVLVDEIVSRAPHPVNDVPVLVELAVRSGDALVPRRLAVAQGAPVRRAAPDDDGFVAMRVEYELDELVRELFGPCRERAAGTRGTTLFPYATSGTGHIDTYFLAAQQATATVLAGCTSAKPDLNELTSRYLTPKWGSLHWFTPHYDRHFREYRNEEVRVLEIGIGGYQHPEWGGGSLRMWKHFFHRGLIYGLDIEDKSHAEEQRITTVVGDQNDPGCLTELAARYGPFDIVIDDGSHINEHVRTSFHALFPHVRPGGLYVIEDLWTAYWPGFGGDSDPGKSDLTSLGLVKSLVDSLQHQELPEDSGRSPGYADRHVVGLHVYHNLAFIEKGVNSEGGIPGWIPRDFDALVAASSGGAA
Protein: Sarcolipin (P42532)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Reversibly inhibits the activity of ATP2A1 and ATP2A2 in sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in muscle. Required for muscle-based, non-shivering thermogenesis (By similarity).
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:1416990, ECO:0000269|PubMed:23362265, ECO:0000269|PubMed:9575189}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23362265}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
- Phospholamban
- Myoregulin
- Calcium-transporting ATPase
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Myozenin 1
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin regulatory light chain 11
Sequence:
MERSTRELCLNFTVVLITVILIWLLVRSYQY
Protein: Ceramide very long chain fatty acid hydroxylase (EC 1.-.-.-) (Q5A668)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- Sphingosine hydroxylase
- Erg251p
- C-4 methylsterol oxidase
- Acyl-CoA desaturase
- Delta
- 3-ketodihydrosphingosine reductase TSC10
- Lanosterol 14-alpha demethylase
- Sphingolipid delta
- Delta 8-
- serine C-palmitoyltransferase
Sequence:
MSKNLPLLSIQEVSKHNHVKDCWVTLYQRKIYNVTGFLEEHPGGGEIILPYAGKDITEIMADIQSHQHSESAYEILDEGMLVGYLATEQEEKGLLRNKNNTPVEVKLVNKDDKDFDMYEFHDHLPAEEKLSIQTDFEEDSKKHRFLDLNKPLLMQLLTSNFSKEFYLDQVHRPRHYGKGSAPLFGNFLEPISLTPWWVIPLVWLPPNFYLFYVGFVNQSPITALSLWVMGLFIWTLVEYCLHRFLFHLDYFLPDHPYAFALHFLLHGIHHYLPMDGYRLVLPPTLFLVLAYPFYKLIFSIFPFYMACSGFAGGTLGYIMYDITHYVLHHTKLPKYFQTVKRLHLEHHYKNYELGFGVTSPFWDVVFGTELTNTFEKRR
Protein: Regulator of G-protein signaling 19 (RGS19) (Q9CX84)
Organism: Mus musculus (Mouse)
Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G-alpha subfamily 1 members, with the order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoylation of the G-protein (By similarity).
Subcellular location: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
Interaction partners:
- PDZ domain-containing protein GIPC1
- Vitamin K-dependent protein C
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MPTPHEAEKQHTGPEEADRPPSMSSHDAAPSGPPSRNPCCLCWCCCCSCSWNQERQRAWQVSRESKLQPLPSCEVCTPPSPKEVQSWAQSFDKLMHSPTGRSVFRAFLRTEYSEENMLFWLACEELKAEANQHVVDEKARLIYEDYVSILSPKEVSLDSRVREGINRKMQEPSPHTFDDAQLQIYTLMHRDSYPRFLTSPTYRSLLLQGAPQSSEA
Protein: Zinc-alpha-2-glycoprotein (Zn-alpha-2-GP) (Zn-alpha-2-glycoprotein) (P25311)
Organism: Homo sapiens (Human)
Function: Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. May bind polyunsaturated fatty acids.
Subcellular location: Secreted.
Interaction partners:
- Prolactin-inducible protein
- Prostate-specific antigen
- Vitamin D-binding protein
- Beta-2-glycoprotein 1
- Alpha-2-HS-glycoprotein
- Alpha-1-acid glycoprotein 1
- Hemopexin
- Haptoglobin
- Retinol-binding protein 4
- Prostatic acid phosphatase
Sequence:
MVRMVPVLLSLLLLLGPAVPQENQDGRYSLTYIYTGLSKHVEDVPAFQALGSLNDLQFFRYNSKDRKSQPMGLWRQVEGMEDWKQDSQLQKAREDIFMETLKDIVEYYNDSNGSHVLQGRFGCEIENNRSSGAFWKYYYDGKDYIEFNKEIPAWVPFDPAAQITKQKWEAEPVYVQRAKAYLEEECPATLRKYLKYSKNILDRQDPPSVVVTSHQAPGEKKKLKCLAYDFYPGKIDVHWTRAGEVQEPELRGDVLHNGNGTYQSWVVVAVPPQDTAPYSCHVQHSSLAQPLVVPWEAS