wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase dyf-5 (EC 2.7.11.1) (B3WFY8)
Organism: Caenorhabditis elegans
Function: Serine/threonine-protein kinase which is required for ciliogenesis. Regulates the length and the morphology of sensory neuron cilia. In addition, plays a role in the anterograde intraflagellar transport (IFT) in the cilia by regulating the undocking of kinesin-II motor complex (composed of klp-11, klp-20 and kap-1) before reaching the distal segment and the docking of kinesin motor osm-3 onto IFT cargos.
Subcellular location: Perikaryon {ECO:0000269|PubMed:17420466}. Cell projection, dendrite {ECO:0000269|PubMed:17420466}. Cell projection, axon {ECO:0000269|PubMed:17420466}. Cell projection, cilium {ECO:0000269|PubMed:17420466}. Note=Enriched at the transition zone between the base of the cilia and the dendrites and to a lesser extent in the cilia. {ECO:0000269|PubMed:17420466}.
Interaction partners:
- Cell division control protein
- DNA replication licensing factor MCM2
- DNA replication licensing factor mcm-5
- DNA replication licensing factor MCM7
- ORC
- DNA replication licensing factor MCM3
- DNA replication licensing factor mcm-6
- DNA replication licensing factor mcm-4
- Origin recognition complex subunit 2
- CDT1 Geminin-binding domain-containing protein
Sequence:
MSSAVKLADRYLMTKRLGDGTFGEVMLAKKIDTGDRVAIKRMKKKFYSWEEAMSLREVKSLKKLNHPNIIKLREVIRENDILYFVFEFMQENLYELMKDRDRYFPESVIRNIIYQVLQGLAFMHKNGFFHRDMKPENIMCNGTELVKIADFGLAREIRSKPPYTDYVSTRWYRAPEILLRSTSYNSPIDMWALGCIMAELYILRPLFPGTSEMDQLFKIISILGTPNKDEWPEGYQLASAMNFRFQQVVATPMEQVVNTISKEGMKLMMDMMLWNPEKRPNANQSLRYKYFQVAEKLGAPVVSQPAPGSIRKTSAASVKSDTKAMTAKAAKKDYIGSENVSPQQPAKVIDRHINRNLPLNKETLFEKSDNKPLGPTKSNEAKPTAKEIYLSKSKYVPGQVSKDTHQNQIMTTNGLTGTTKTTTFSAKKEGRTAVQTRFEYAYGYIPSFGARQTGPTVSNQTNNHSANNSHSPNKMSNTGRVDWAAKYVK
Protein: Amphiphysin, isoform B (A0A0B4KEW6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MTENKGIMLAKSVQKHAGRAKEKILQNLGKVDRTADEIFDDHLNNFNRQQASANRLQKEFNNYIRCVRAAQAASKTLMDSVCEIYEPQWSGYDALQAQTGASESLWADFAHKLGDQVLIPLNTYTGQFPEMKKKVEKRNRKLIDYDGQRHSFQNLQANANKRKDDVKLTKGREQLEEARRTYEILNTELHDELPALYDSRILFLVTNLQTLFATEQVFHNETAKIYSELEAIVDKLATESQRGSNTLRKQTSNPIKTSSPVQSPVNKLNNANINSNYQNQITTNGGSSLANSQPRPESPAAALVSATPSSPVENGVTTKSLERPELSGLNASAKATTTTQTSPTEDKAVVSEAVKPSETEGAAVAASVTPAPPATPAQINGNNNEPSIVKEGGKQPKELPSTTSNAEAAAEAAANNGNSIEEHKQKKLDANTADLPPGVLYRVKATYGYAKEDVDELSFEIGDLIRVIEYDDPEDQEEGWLMGQKEGTNEKGLFPANFTRPI
Protein: Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase) (allergen Asp f 22) (Q96X30)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Pyruvate kinase
- Fructose-bisphosphate aldolase
- Phosphoglycerate kinase
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- Triosephosphate isomerase
- Triosephosphate isomerase
- Phosphoenolpyruvate carboxykinase
- ATP-dependent 6-phosphofructokinase
Sequence:
MPISKIHARSVYDSRGNPTVEVDVVTETGLHRAIVPSGASTGQHEAHELRDGDKTQWGGKGVLKAVKNVNETIGPALIKENIDVKDQSKVDEFLNKLDGTANKSNLGANAILGVSLAVAKAGAAEKGVPLYAHISDLAGTKKPYVLPVPFQNVLNGGSHAGGRLAFQEFMIVPDSAPSFSEALRQGAEVYQKLKALAKKKYGQSAGNVGDEGGVAPDIQTAEEALDLITEAIEQAGYTGKIKIAMDVASSEFYKADVKKYDLDFKNPESDPSKWLTYEQLADLYKSLAAKYPIVSIEDPFAEDDWEAWSYFYKTSDFQIVGDDLTVTNPGRIKKAIELKSCNALLLKVNQIGTLTESIQAAKDSYADNWGVMVSHRSGETEDVTIADIAVGLRSGQIKTGAPCRSERLAKLNQILRIEEELGENAVYAGSKFRTAVNL
Protein: Peripherin-2 (Retinal degeneration slow protein) (P17810)
Organism: Bos taurus (Bovine)
Function: Essential for retina photoreceptor outer segment disk morphogenesis, may also play a role with ROM1 in the maintenance of outer segment disk structure. Required for the maintenance of retinal outer nuclear layer thickness (By similarity). Required for the correct development and organization of the photoreceptor inner segment (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:2372552}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:10681511}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P15499}.
Interaction partners:
- Retinal guanylyl cyclase 1
- Rod outer segment membrane protein 1
- Proproteinase E
- Amelogenin, X isoform
- Neuropeptide Y receptor type 2
- Somatotropin
- Somatoliberin
- Short palate, lung and nasal epithelium carcinoma-associated protein 2A
- Opticin
- Rhodopsin
Sequence:
MALLKVKFDQKKRVKLAQGLWLMNWFSVLAGIIIFGLGLFLKIELRKRSDVMNNSESHFVPNSLIGVGVLSCVFNSLAGKICYDALDPAKYAKWKPWLKPYLAVCVLFNVVLFLVALCCFLLRGSLESTLAHGLKNGMKFYRDTDTPGRCFMKKTIDMLQIEFKCCGNNGFRDWFEIQWISNRYLDFSSKEVKDRIKSNVDGRYLVDGVPFSCCNPNSPRPCIQYQLTNNSAHYSYDHQTEELNLWLRGCRAALLSYYSNLMNTTGAVTLLVWLFEVTITVGLRYLHTALEGMANPEDPECESEGWLLEKSVPETWKAFLESVKKLGKGNQVEAEGEDAGQAPAAG
Protein: Alpha-synuclein (Q4JHT6)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004370}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. Secreted {ECO:0000256|ARBA:ARBA00004613}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
- Synuclein alpha interacting protein
- 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
- Heat shock 70 kDa protein 4
- Amyloid-beta A4 protein
- Transporter
- Serine/threonine-protein kinase PINK1, mitochondrial
- Non-selective voltage-gated ion channel VDAC1
- protein deglycase
- Huntingtin
- Brain-derived neurotrophic factor
Sequence:
MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSRTKEGVVHGVTTVAEKTKEQVSNVGGAVVTGVTAVAQKTVEGAGNIAAATGLVKKDQLAKQNEEGFLQEGMVNNTGVAVDPENEAYEMPPEEEYQDYEPEA
Protein: Protein SEC13 homolog (G7NYT7)
Organism: Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Subcellular location: Lysosome membrane {ECO:0000256|ARBA:ARBA00004656}. Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567}.
Interaction partners:
- GATOR2 complex protein MIOS
- SEC24 homolog A, COPII coat complex component.
- Protein transport protein Sec31A
- Protein transport protein Sec24C
- GATOR2 complex protein WDR59
- SEC24 homolog D, COPII coat complex component
- Nuclear pore complex protein Nup98-Nup96
- Nuclear pore complex protein Nup133
- SEC24 homolog B, COPII coat complex component
- Nucleoporin SEH1
Sequence:
MREPVLTWCVPLELLCSHPLPVSAFLKTQVKLYTYRACAGKDEMGKMVSVINTVDTSHEDMIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILIADLRGHEGPVWQVAWAHPMYGNILASCSYDRKVIIWREENGTWEKSHEHAGHDSSVNSVCWAPHDYGLILACGSSDGAISLLMYTGEGQWEVKKINNAHTIGCNAVSWAPAVVPGSLIDQPSGQKPNYIKRFASGGCDNLIKLWKEEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRVFIWTCDDASGNTWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKVTLWKESVDGQWVCISDVNKGQGSVSASVTEGQQNEQ
Protein: Sonic hedgehog protein (SHH) (EC 3.1.-.-) (HHG-1) (Shh unprocessed N-terminal signaling and C-terminal autoprocessing domains) (ShhNC) [Cleaved into: Sonic hedgehog protein N-product (ShhN) (Shh N-terminal processed signaling domains) (ShhNp)] (Q15465)
Organism: Homo sapiens (Human)
Function: The C-terminal part of the sonic hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity (By similarity). Both activities result in the cleavage of the full-length protein into two parts (ShhN and ShhC) followed by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated ShhN (By similarity). Both activities occur in the reticulum endoplasmic (By similarity). Once cleaved, ShhC is degraded in the endoplasmic reticulum (By similarity).
Subcellular location: [Sonic hedgehog protein]: Endoplasmic reticulum membrane {ECO:0000305|PubMed:18534984}. Golgi apparatus membrane {ECO:0000305|PubMed:18534984}. Secreted {ECO:0000269|PubMed:24342078}. Note=Co-localizes with HHAT in the ER and Golgi membrane. {ECO:0000305|PubMed:18534984}.; SUBCELLULAR LOCATION: [Sonic hedgehog protein N-product]: Cell membrane {ECO:0000250|UniProtKB:Q62226}; Lipid-anchor {ECO:0000250|UniProtKB:Q62226}. Note=The dual-lipidated sonic hedgehog protein N-product (ShhNp) is firmly tethered to the cell membrane where it forms multimers (PubMed:24522195). Further solubilization and release from the cell surface seem to be achieved through different mechanisms, including the interaction with DISP1 and SCUBE2, movement by lipoprotein particles, transport by cellular extensions called cytonemes or by the proteolytic removal of both terminal lipidated peptides (PubMed:24522195, PubMed:26875496). {ECO:0000305|PubMed:24522195, ECO:0000305|PubMed:26875496}.
Interaction partners:
- Growth arrest-specific protein 1
- Hedgehog-interacting protein
- Protein patched homolog 1
- Cell adhesion molecule-related/down-regulated by oncogenes
- Protein smoothened
- Protein patched homolog 2
- Protein dispatched homolog 1
- Brother of CDO
- Low-density lipoprotein receptor-related protein 2
- Zinc finger protein GLI1
Sequence:
MLLLARCLLLVLVSSLLVCSGLACGPGRGFGKRRHPKKLTPLAYKQFIPNVAEKTLGASGRYEGKISRNSERFKELTPNYNPDIIFKDEENTGADRLMTQRCKDKLNALAISVMNQWPGVKLRVTEGWDEDGHHSEESLHYEGRAVDITTSDRDRSKYGMLARLAVEAGFDWVYYESKAHIHCSVKAENSVAAKSGGCFPGSATVHLEQGGTKLVKDLSPGDRVLAADDQGRLLYSDFLTFLDRDDGAKKVFYVIETREPRERLLLTAAHLLFVAPHNDSATGEPEASSGSGPPSGGALGPRALFASRVRPGQRVYVVAERDGDRRLLPAAVHSVTLSEEAAGAYAPLTAQGTILINRVLASCYAVIEEHSWAHRAFAPFRLAHALLAALAPARTDRGGDSGGGDRGGGGGRVALTAPGAADAPGAGATAGIHWYSQLLYQIGTWLLDSEALHPLGMAVKSS
Protein: Uncharacterized protein C17C9.14 (Q10485)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Peroxisomal membrane protein pex13
- Uncharacterized protein C29A4.14c
- Peroxisomal membrane protein pex14
- Peroxisomal biogenesis factor 11
- T-complex protein 1 subunit delta
- Peroxisome assembly protein 12
- Peroxisome biogenesis factor 10
- Uncharacterized protein C1F12.04c
- Peroxisomal ATPase pex6
- E3 ubiquitin-protein ligase complex slx8-rfp subunit slx8
Sequence:
MSNPTIEGDENRKENTKSNTKPNFDDLDDLDDILDDLDVPSAFKNEEKKNIDEHKQTGNTSKENERIKNDDNLNSLIQEMMSKFEDLGGPSGLDGSQLSSSFQNDQLLNVILEDQFATEKDSDNGAVNYGALEAALNSLMSQVTSKEILYEPLKDLEANYPKFLKNAKETEKQGFEEQYQKIQKCIQIFESPEYDARKDADIISKLVEEIQEKPLPAPLIDNSMETAGCPTQ
Protein: Kinetoplast-associated protein 1 (Histone H1-like protein p21) (O61016)
Organism: Crithidia fasciculata
Function: Histone H1-like DNA-binding protein involved in the organization and segregation of kinetoplast DNA (kDNA). The mitochondrial DNA of kinetoplastid protozoa consists of about 5,000 minicircles and 20 to 30 maxicircles. These circular DNAs are held together by catenation into a highly organized compact disk structure referred to as a kinetoplast DNA (kDNA) network. Binds preferentially to a specific fragment of minicircle DNA and is able to compact kDNA networks through DNA charge neutralization and condensation (By similarity).
Subcellular location: Mitochondrion matrix, kinetoplast {ECO:0000269|PubMed:8446592, ECO:0000269|PubMed:9719509}.
Interaction partners:
Sequence:
MLRVSVRSLVRKASSKAGSKAAVPAAAAAASAPLSPATSAASARAVPPVGESRVSIPPIPGVAAPRSHRAAAAPAKKAAAPKAAKAKTPAKASRKIKKAASKPSAPKQAAGKMRKAAGKAQRKIKAAARKAAPKKMAKSFGKKGAAKKAHK
Protein: Transmembrane protein 183A (Q8IXX5)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MARGPGPLGRPRPDTVAMPKRGKRLKFRAHDACSGRVTVADYANSDPAVVRSGRVKKAVANAVQQEVKSLCGLEASQVPAEEALSGAGEPCDIIDSSDEMDAQEESIHERTVSRKKKSKRHKEELDGAGGEEYPMDIWLLLASYIRPEDIVNFSLICKNAWTVTCTAAFWTRLYRRHYTLDASLPLRLRPESMEKLRCLRACVIRSLYHMYEPFAARISKNPAIPESTPSTLKNSKCLLFWCRKIVGNRQEPMWEFNFKFKKQSPRLKSKCTGGLQPPVQYEDVHTNPDQDCCLLQVTTLNFIFIPIVMGMIFTLFTINVSTDMRHHRVRLVFQDSPVHGGRKLRSEQGVQVILDPVHSVRLFDWWHPQYPFSLRA
Protein: Protein king tubby (Q86PC9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Functions in regulating protein trafficking, retinal maintenance and lipid storage. Protects photoreceptor cells R1 to R6 against light-induced retinal degeneration by stimulating norpA-mediated endocytosis of the rhodopsin ninaE (Rh1). In the auditory receptor neurons, functions as a cilia trafficking regulator of various transient receptor potential (TRP) channel components including iav and nompC. Likely to deliver pre-ciliary vesicles containing membrane proteins such as iav and nompC to the intraflagellar transport complex (IFT) at the cilia base. Plays a role in the inhibition of fat storage.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12204260, ECO:0000269|PubMed:23228091, ECO:0000269|PubMed:24068974}. Nucleus {ECO:0000269|PubMed:12204260, ECO:0000269|PubMed:23228091, ECO:0000269|PubMed:24068974}. Cell projection, cilium membrane {ECO:0000269|PubMed:24068974, ECO:0000269|PubMed:26723017}; Peripheral membrane protein {ECO:0000269|PubMed:24068974, ECO:0000269|PubMed:26723017}. Cell projection, rhabdomere {ECO:0000269|PubMed:23228091}. Note=Detected in the cytoplasm and nucleus of the chordotonal neurons (PubMed:12204260, PubMed:24068974). PtdIns 4,5-P2 binds to and regulates its localization to the ciliary base (PubMed:26723017). In the dark, localizes mainly to the rhabdomere domain of photoreceptor cells R1 to R6 (PubMed:23228091). When dark-reared flies are moved into the light, the protein translocates to the cytoplasm (PubMed:23228091). Under normal conditions (12 hr light/12 hr dark), localized mainly in the nucleus of photoreceptor cells with minor staining in the cytoplasm (PubMed:23228091). {ECO:0000269|PubMed:12204260, ECO:0000269|PubMed:23228091, ECO:0000269|PubMed:24068974, ECO:0000269|PubMed:26723017}.
Interaction partners:
- RE61793p
- Reduced mechanoreceptor potential A, isoform B
Sequence:
MSGINSRNQKMEQQRQLMEAYIRQKRASPGMVQASDLQINRPMSGMRSNSRELHAYDGPMQFISSPQNPDQILTNGSPGGINPVAMNTSRNHSNNMRSLSTINQEADLIEEISSHELEDEESSPVTVIEQHQQSASHSANSTQSQKPRARQHSFSDNLDEDDYTNRNVAGAAPVRPAGMASSPYKDATLDGSSNGTGNGTGGESEGDVIGNIDQFVMQPAPQGVLYKCRITRDRKGMDRGLFPIYYLHLERDYGKKIFLLGGRKRKKSKTSNYIVSCDPTDLSRNADGFCGKLRSNVFGTSFTVFDNGNKESTESPRLDLAVIIYDTNILGFKGPRNMTVILPGMTEDDQRVKISSADPKQQGILDLWKMKNMDNIVELHNKTPVWNDETQSYVLNFHGRVTQASVKNFQLVHDSDPEYIVMQFGRTSEDVFTMDYRYPLCAMQAFAIALSSFDGKIACE
Protein: Nuclear receptor-interacting protein 1 (Nuclear factor RIP140) (Receptor-interacting protein 140) (P48552)
Organism: Homo sapiens (Human)
Function: Modulates transcriptional activation by steroid receptors such as NR3C1, NR3C2 and ESR1. Also modulates transcriptional repression by nuclear hormone receptors. Positive regulator of the circadian clock gene expression: stimulates transcription of BMAL1, CLOCK and CRY1 by acting as a coactivator for RORA and RORC. Involved in the regulation of ovarian function (By similarity). Plays a role in renal development.
Subcellular location: Nucleus {ECO:0000269|PubMed:11266503, ECO:0000269|PubMed:12773562, ECO:0000269|PubMed:15060175, ECO:0000269|PubMed:7641693}. Note=Localized to discrete foci and redistributes to larger nuclear domains upon binding to ligand-bound NR3C1.
Interaction partners:
- Estrogen receptor
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Nuclear receptor ROR-alpha
- C-terminal-binding protein 1
- Nuclear receptor subfamily 2 group C member 1
- Nuclear receptor ROR-gamma
- Nuclear receptor corepressor 1
- Hepatocyte nuclear factor 3-alpha
- Estrogen-related receptor gamma
- Retinoic acid receptor alpha
Sequence:
MTHGEELGSDVHQDSIVLTYLEGLLMHQAAGGSGTAVDKKSAGHNEEDQNFNISGSAFPTCQSNGPVLNTHTYQGSGMLHLKKARLLQSSEDWNAAKRKRLSDSIMNLNVKKEALLAGMVDSVPKGKQDSTLLASLLQSFSSRLQTVALSQQIRQSLKEQGYALSHDSLKVEKDLRCYGVASSHLKTLLKKSKVKDQKPDTNLPDVTKNLIRDRFAESPHHVGQSGTKVMSEPLSCAARLQAVASMVEKRASPATSPKPSVACSQLALLLSSEAHLQQYSREHALKTQNANQAASERLAAMARLQENGQKDVGSYQLPKGMSSHLNGQARTSSSKLMASKSSATVFQNPMGIIPSSPKNAGYKNSLERNNIKQAANNSLLLHLLKSQTIPKPMNGHSHSERGSIFEESSTPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKVPDVDIKEDQDTSKNSKLNSHQKVTLLQLLLGHKNEENVEKNTSPQGVHNDVSKFNTQNYARTSVIESPSTNRTTPVSTPPLLTSSKAGSPINLSQHSLVIKWNSPPYVCSTQSEKLTNTASNHSMDLTKSKDPPGEKPAQNEGAQNSATFSASKLLQNLAQCGMQSSMSVEEQRPSKQLLTGNTDKPIGMIDRLNSPLLSNKTNAVEENKAFSSQPTGPEPGLSGSEIENLLERRTVLQLLLGNPNKGKSEKKEKTPLRDESTQEHSERALSEQILMVKIKSEPCDDLQIPNTNVHLSHDAKSAPFLGMAPAVQRSAPALPVSEDFKSEPVSPQDFSFSKNGLLSRLLRQNQDSYLADDSDRSHRNNEMALLESKNLCMVPKKRKLYTEPLENPFKKMKNNIVDAANNHSAPEVLYGSLLNQEELKFSRNDLEFKYPAGHGSASESEHRSWARESKSFNVLKQLLLSENCVRDLSPHRSNSVADSKKKGHKNNVTNSKPEFSISSLNGLMYSSTQPSSCMDNRTFSYPGVVKTPVSPTFPEHLGCAGSRPESGLLNGCSMPSEKGPIKWVITDAEKNEYEKDSPRLTKTNPILYYMLQKGGNSVTSRETQDKDIWREASSAESVSQVTAKEELLPTAETKASFFNLRSPYNSHMGNNASRPHSANGEVYGLLGSVLTIKKESE
Protein: Sprouty RTK signaling antagonist 1 (D6RHD2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
Sequence:
MDPQNQHGSGSSLVVIQQPSLDSRQRLDYEREIQPTAILSLDQIKAIRGSNEYTEGPSVVKRPAPRTAPRQEKHERTHEIIPINVNNNYEHRHTSHLGHAVLPSNARGPILSRSTSTGSAASSGSNSSASSEQGLLGRSPPTRPVPGHRSERAIRTQPKQLIVDDLKGSLKEDLTQHKFICEQCGKCKCGECTAPRTLPSCLACNRQCL
Protein: DNA polymerase processivity factor (F5HID2)
Organism: Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Function: Plays an essential role in the viral lytic DNA replication by acting as the polymerase accessory subunit. Stimulates the viral DNA polymerase activity and appears to function with it as a holoenzyme. Increases the processivity of the viral polymerase, probably by acting as a sliding clamp that prevents dissociation of the polymerase from the active template (By similarity).
Subcellular location: Virion tegument {ECO:0000250}. Host nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MPVDFHYGVRVDVTLLSKIRRVNEHIKSATKTGVVQVHGSACTPTLSVLSSVGTAGVLGLRIKNALTPLVGHTEGSGDVSFSFRNTSVGSGFTHTRELFGANVLDAGIAFYRKGEACDTGAQPQFVRTTISYGDNLTSTVHKSVVDQKGILPFHDRMEAGGRTTRLLLCGKTGAFLLKWLRQQKTKEDQTVTVSVSETLSIVTFSLGGVSKIIDFKPETKPVSGWDGLKGKKSVDVGVVHTDALSRVSLESLIAALRLCKVPGWFTPGLIWHSNEILEVEGVPTGCQSGDVKLSVLLLEVNRSVSAEGGESSQKVPDSIPDSRRQPELESPDSPPLTPVGPFGPLEDASEDAASVTSCPPAAPTKDSTKRPHKRRSDSSQSRDRGKVPKTTFNPLI
Protein: Tropomyosin 1 (Alpha) isoform 1 (D9YZV4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI
Protein: NF-X1-type zinc finger protein NFXL1 (Ovarian zinc finger protein) (hOZFP) (Q6ZNB6)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MEASWRQVAGGRGRSRGRATAAPSGNGVHLRGAGGGREKGSVGAVPSGTSPGGVATTAAAGSRHSPAGSQALQTTAASELMSQKKFEEIKKANQAAARKLVEEQFSSSSEEGDEDFEGKQGKILANTFITYTTQTDGDTRELERTKQYVNEAFQAGAMTCLICIASVKRNQAVWSCSGCFCIFHMPCIQKWAKDSQFLVSSVTDDDFGKKDCPWPCPKCRFEYKRSETPSRYYCYCGKVEDPPLDPWLVPHSCGQVCEREFKPPCGHKCLLLCHPGPCPPCPKMVTTTCYCKKAKPIPRRCSAKEWSCQLPCGQKLLCGQHKCENPCHAGSCQPCPRVSRQKCVCGKKVAERSCASPLWHCDQVCGKTLPCGNHTCEQVCHVGACGECPRSGKRFCPCQKSKFSLPCTEDVPTCGDSCDKVLECGIHRCSQRCHRGPCETCRQEVEKHCRCGKHTKRMPCHKPYLCETKCVKMRDCQKHQCRRKCCPGNCPPCDQNCGRTLGCRNHKCPSVCHRGSCYPCPETVDVKCNCGNTKVTVPCGRERTTRPPKCKEQCSRPPTCHHTSQEKHRCHFGSCPPCHQPCQKVLEKCGHLCPAPCHDQALIKQTGRHQPTGPWEQPSEPAFIQTALPCPPCQVPIPMECLGKHEVSPLPCHAVGPYSCKRVCGRILDCQNHTCMKECHKVTKTDGCTGKNKAGPECLHCEEGCSKSRPLGCLHPCILRCHPGECPPCVQMLRIKCHCKITSLYVECRKITTADVNEKNLLSCCKNQCPKELPCGHRCKEMCHPGECPFNCNQKVKLRCPCKRIKKELQCNKVRENQVSIECDTTCKEMKRKASEIKEAEAKAALEEEKRRQQAELEAFENRLKGRRKKNRKRDEVAVELSLWQKHKYYLISVCGVVVVVFAWYITHDVN
Protein: Tubulin gamma-2 chain (Gamma-2-tubulin) (Q8VCK3)
Organism: Mus musculus (Mouse)
Function: Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation, centrosome duplication and spindle formation (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19648910}. Note=Mainly localizes to the centrosome, but a fraction is found outside of the centrosome in the cytoplasm.
Interaction partners:
- Gamma-tubulin complex component 2
- Gamma-tubulin complex component 3
- Gamma-tubulin complex component 5
- Gamma-tubulin complex component 4
- Gamma-tubulin complex component 6
- Mitotic-spindle organizing protein 1
- Tubulin gamma-1 chain
- Mitotic-spindle organizing protein 2
- Protein NEDD1
Sequence:
MPREIITLQLGQCGNQIGFEFWKQLCAEHGISPEGIVEEFATEGTDRKDVFFYQADDEHYIPRAVLLDLEPRVIHSILNSSYAKLYNPENIYLSEHGGGAGNNWGRGFSQGEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQDEMSDVVVQPYNSLLTLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFLMTGYTPLTTDQSVASVRKTTVLDVMRRLLQPKNVMVSTGRDRQTNHCYIAILNIIQGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVALSRKSPYLPSAHRVSGLMMANHTSISSLFESSCQQYDKLWKRGAFLEQFRKEDIFKDNFEEMHRSREVVQELIDEYHAATRPDYISWGTQEQ
Protein: RE58433p (Q9VPJ0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform B
- Uncharacterized protein, isoform A
- Uncharacterized protein, isoform B
Sequence:
MRIKYCWLATLVFIAAASASYSPEKPVPPPCRACTQLVSSFRAGLERTKRGHAGGDTAWEEEKLRSYKNSEVRLVEIQEKLCSEGEVINKDHCHNLANEHEALLEDWFIHKQTESPDLQSWLCIDQLTVCCPLNTYGPDCLTCTECNGNGKCKGDGTRKGNGKCKCDPGYAGPNCNECGPEHYESFRDEKKLLCTQCHAACGEGGCTGGGPKSCRKCKKGWSMDSEAGCVDINECLEQQRPNPCRPQQFCVNNEGSFSCLECDRSCDGCDGDGPDMCRKCADGYELKEGKCHDISAEQRSNYVSFTRMLTYFGMCVATCVIFQSSTHIAWGCIVGAAVAGYIAVSEYWINSEAGGGHQPEIDTKQLEELIMKSL
Protein: Protein PET10 (Petite colonies protein 10) (P36139)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Lipid droplet {ECO:0000269|PubMed:10515935}. Membrane {ECO:0000269|PubMed:10515935}; Peripheral membrane protein {ECO:0000269|PubMed:10515935}.
Interaction partners:
- Seipin
- Acyl-coenzyme A diphosphatase YFT2
- Sterol 24-C-methyltransferase ERG6
- Protein LDB16
- Acyl-coenzyme A diphosphatase SCS3
- Lipid droplet organization protein LDO16
- Inclusion body clearance protein IML2
- Diacylglycerol O-acyltransferase 1
Sequence:
MSESSISSSKPSVELPQATWSHLQRYPALSKFIKYAESLPPVERLISFNLVVLGSVNQWVSESSSSPRLVKQVVAAGKEGAFKLDELVNLLVFKEGVDGLLYNWKSHSNTPGIWLVWFFVDYVANISNTLLREFLIKPLHLQGSTASKEIGSSGEENKVTDASSLPHVAELSSTTRGMSQEIQSKVKSNYIDPTKDLAKEKYDAIVKPTTDKLQSVYIDPTKTKLNETYQRFTTVYENNLSKSESVPKAIVSTGLDLGNATIEKLKASREDQTNSKPAAVSTN
Protein: Osmotin (CpOsm) (P86363)
Organism: Calotropis procera (Roostertree) (Asclepias procera)
Function: Has antifungal activity. Inhibits spore germination and mycelia growth in F.solani (IC(50)=67.0 ug/ml), C.gloeosporioides (IC(50)=32.1 ug/ml) and a Neurospora isolate (IC(50)=57.5 ug/ml).
Interaction partners:
Sequence:
ATFTIRNNCPYTIWAAAVPGGGRRLNSGGTWTINVAPGTA
Protein: Melanocortin-2 receptor accessory protein 2 (D3Z1Q2)
Organism: Mus musculus (Mouse)
Function: Modulator of melanocortin receptor 4 (MC4R), a receptor involved in energy homeostasis. Plays a central role in the control of energy homeostasis and body weight regulation by increasing ligand-sensitivity of MC4R and MC4R-mediated generation of cAMP. May also act as a negative regulator of MC2R: competes with MRAP for binding to MC2R and impairs the binding of corticotropin (ACTH) to MC2R. May also regulate activity of other melanocortin receptors (MC1R, MC3R and MC5R); however, additional evidence is required in vivo.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=The formation of antiparallel homo- and heterodimers suggest that N- and C-terminus can both localize in the cytoplasmic and extracellular parts, depending on the context. {ECO:0000250}.
Interaction partners:
- Adrenocorticotropic hormone receptor
- Melanocortin receptor 3
- Melanocortin receptor 4
- Prokineticin receptor 1
- Melanocortin receptor 5
- SH2B adapter protein 1
- Cytochrome b5 reductase 4
Sequence:
MEMSAQRLASNRTSPQSPSNSDYTWEYEYYEIGPVSFEGLKAHKYSIVIGFWVGLAVFVIFMFFVLTLLTKTGAPHQDNAESSERRFRMNSFVSDFGKPLESDKVFSRQGNEESRSLFHCYINEVEHLDRVKVCHQTTAIDSDVHLQEASRSSGRPEEELARFMKFDIPNFVNTEQSSFGEDDLLISEAPVLLENKPVSQTSRIDLD