wanglab/gogpt-training-data huggingface dataset:
Protein: Probable splicing factor, arginine/serine-rich 2 (CeSRp40) (RNA-binding protein srp-4) (Q23120)
Organism: Caenorhabditis elegans
Function: Plays a functionally redundant role in spermatogenesis and growth rate control. Required for the development of somatic gonad structures and for progression from larval stage to adulthood.
Subcellular location: Nucleus {ECO:0000269|PubMed:10906451}.
Interaction partners:
- Splicing factor U2AF 35 kDa subunit
- Probable splicing factor, arginine/serine-rich 6
- Splicing factor U2AF 65 kDa subunit
- Probable splicing factor, arginine/serine-rich 4
- RRM domain-containing protein
- Probable splicing factor, arginine/serine-rich 3
- Probable splicing factor, arginine/serine-rich 7
- RRM domain-containing protein
- Pre-mRNA-splicing factor SLU7
- LUC7-related splicing factor homolog
Sequence:
MVRVYIGRLPNRASDRDVEHFFRGYGKLSDVIMKNGFGFVDFQDQRDADDAVHDLNGKELCGERVILEFPRRKVGYNEERSGSGFRGREPTFRKGGERQFSNRYSRPCSTRFRLVIDNLSTRYSWQDIKDHIRKLGIEPTYSEAHKRNVNQAIVCFTSHDDLRDAMNKLQGEDLNGRKLKCTDETRDRSRSRSPRRRSRSRSPTRSRSPPARRRSPGSDRSDRKSRSASPKKRSDKRARSESKSRSRSGGRRSRSNSPPNRSPSPKKRRDNSSPRSGSASP
Protein: Protein yop1 (Q9UU91)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required to generate and maintain the structure of the tubular endoplasmic reticulum network and the vacuole. Induces high curvature in membranes and causes membrane tubule formation. Involved in membrane/vesicle trafficking (By similarity). Required for the correct positioning of the cellular division plane by delimiting the actomyosin ring assembly at the cell equator.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20434336}; Multi-pass membrane protein {ECO:0000269|PubMed:20434336}. Nucleus membrane {ECO:0000269|PubMed:20434336}; Multi-pass membrane protein {ECO:0000269|PubMed:20434336}. Note=Enriched at the cell equator during mitosis.
Interaction partners:
- Protein sey1
- Reticulon-like protein 1
- Protein transport protein yip1
- MICOS complex subunit mic60
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
Sequence:
MSFQVRVKQNMQDLDNRLAAFPQLNSLEKNFGVSKLYVFLTAAGIYALFLFLNWGGFLLTNLLAFAMPAFFSINAIETTNKADDTQWLTYYLVTSFLNVIEYWSQLILYYVPVYWLLKAIFLIWLALPKFNGATIIYRHLIRPYITPHVIRICKSVSRQNAAPAPTASSFAHTTATDIPPSI
Protein: Semaphorin-4D (M-Sema G) (Semaphorin-C-like 2) (Semaphorin-J) (Sema J) (CD antigen CD100) (O09126)
Organism: Mus musculus (Mouse)
Function: Cell surface receptor for PLXNB1 and PLXNB2 that plays an important role in cell-cell signaling (By similarity). Regulates GABAergic synapse development. Promotes the development of inhibitory synapses in a PLXNB1-dependent manner. Modulates the complexity and arborization of developing neurites in hippocampal neurons by activating PLXNB1 and interaction with PLXNB1 mediates activation of RHOA (By similarity). Promotes the migration of cerebellar granule cells. Plays a role in the immune system; induces B-cells to aggregate and improves their viability (in vitro) (By similarity). Induces endothelial cell migration through the activation of PTK2B/PYK2, SRC, and the phosphatidylinositol 3-kinase-AKT pathway (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:8969198}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Plexin-B2
- B-cell differentiation antigen CD72
- Plexin-B1
- Plexin-B3
- Receptor-type tyrosine-protein phosphatase C
- Plexin-C1
- Rho-related GTP-binding protein Rho6
- Hepatocyte growth factor receptor
- Plexin-D1
- Ras-related protein R-Ras
Sequence:
MRMCAPVRGLFLALVVVLRTAVAFAPVPRLTWEHGEVGLVQFHKPGIFNYSALLMSEDKDTLYVGAREAVFAVNALNISEKQHEVYWKVSEDKKSKCAEKGKSKQTECLNYIRVLQPLSSTSLYVCGTNAFQPTCDHLNLTSFKFLGKSEDGKGRCPFDPAHSYTSVMVGGELYSGTSYNFLGSEPIISRNSSHSPLRTEYAIPWLNEPSFVFADVIQKSPDGPEGEDDKVYFFFTEVSVEYEFVFKLMIPRVARVCKGDQGGLRTLQKKWTSFLKARLICSKPDSGLVFNILQDVFVLRAPGLKEPVFYAVFTPQLNNVGLSAVCAYTLATVEAVFSRGKYMQSATVEQSHTKWVRYNGPVPTPRPGACIDSEARAANYTSSLNLPDKTLQFVKDHPLMDDSVTPIDNRPKLIKKDVNYTQIVVDRTQALDGTFYDVMFISTDRGALHKAVILTKEVHVIEETQLFRDSEPVLTLLLSSKKGRKFVYAGSNSGVVQAPLAFCEKHGSCEDCVLARDPYCAWSPAIKACVTLHQEEASSRGWIQDMSGDTSSCLDKSKESFNQHFFKHGGTAELKCFQKSNLARVVWKFQNGELKAASPKYGFVGRKHLLIFNLSDGDSGVYQCLSEERVRNKTVSQLLAKHVLEVKMVPRTPPSPTSEDAQTEGSKITSKMPVASTQGSSPPTPALWATSPRAATLPPKSSSGTSCEPKMVINTVPQLHSEKTVYLKSSDNRLLMSLLLFIFVLFLCLFSYNCYKGYLPGQCLKFRSALLLGKKTPKSDFSDLEQSVKETLVEPGSFSQQNGDHPKPALDTGYETEQDTITSKVPTDREDSQRIDELSARDKPFDVKCELKFADSDADGD
Protein: Endoplasmic reticulum-Golgi intermediate compartment protein 3 (Serologically defined breast cancer antigen NY-BR-84) (Q9Y282)
Organism: Homo sapiens (Human)
Function: Possible role in transport between endoplasmic reticulum and Golgi. Positively regulates trafficking of the secretory proteins SERPINA1/alpha1-antitrypsin and HP/haptoglobin.
Subcellular location: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:15308636}; Multi-pass membrane protein {ECO:0000269|PubMed:15308636}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:15308636}; Multi-pass membrane protein {ECO:0000269|PubMed:15308636}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15308636}; Multi-pass membrane protein {ECO:0000269|PubMed:15308636}. Note=Cycles between the endoplasmic reticulum and the Golgi.
Interaction partners:
- Endoplasmic reticulum-Golgi intermediate compartment protein 2
- 5-taurinomethyluridine-[tRNA] synthase subunit GTPB3, mitochondrial
- Vacuolar protein sorting-associated protein 45
Sequence:
MEALGKLKQFDAYPKTLEDFRVKTCGGATVTIVSGLLMLLLFLSELQYYLTTEVHPELYVDKSRGDKLKINIDVLFPHMPCAYLSIDAMDVAGEQQLDVEHNLFKQRLDKDGIPVSSEAERHELGKVEVTVFDPDSLDPDRCESCYGAEAEDIKCCNTCEDVREAYRRRGWAFKNPDTIEQCRREGFSQKMQEQKNEGCQVYGFLEVNKVAGNFHFAPGKSFQQSHVHVHDLQSFGLDNINMTHYIQHLSFGEDYPGIVNPLDHTNVTAPQASMMFQYFVKVVPTVYMKVDGEVLRTNQFSVTRHEKVANGLLGDQGLPGVFVLYELSPMMVKLTEKHRSFTHFLTGVCAIIGGMFTVAGLIDSLIYHSARAIQKKIDLGKTT
Protein: (thale cress) hypothetical protein (A0A178UKR9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDSLTGFRMEPKWQIDPQLLFVGPKIGEGAHAKVYEGKYKNQTVAIKIVHRGETPEEIAKRDSRFLREVEMLSRVQHKNLVKFIGACKEPVMVIVTELLQGGTLRKYLLNLRPACLETRVAIGFALDIARGMECLHSHGIIHRDLKPENLLLTADHKTVKLADFGLAREESLTEMMTAETGTYRWMAPELYSTVTLRLGEKKHYNHKVDAYSFAIVLWELLHNKLPFEGMSNLQAAYAAAFKNVRPSAESLPEELGDIVTSCWNEDPNARPNFTHIIELLLNYLSKVGSPISAIPQRILASKNTLLPPDSPGTSSLMAKLDECGETPKAKSEDKRKGLFFCFNQCY
Protein: Large ribosomal subunit protein mL54 (39S ribosomal protein L54, mitochondrial) (L54mt) (MRP-L54) (Q9CPW3)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q6P161}.
Interaction partners:
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL23m
- Large ribosomal subunit protein mL41
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein uL14m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL49
- Large ribosomal subunit protein bL27m
- 39S ribosomal protein L40
Sequence:
MAAAHLLRASRVWARWHPRALPVLRRPGGFSIREYAKKPVGKGGKGGVAAEALKDPEVCTDPTQLTTHAMGVNIYKEGQDVALKADSEYPTWLFQVNLGPPKKLEELEPESREYWRLLRKQNIWRHNRLSKNKKL
Protein: Sulfotransferase 1A1 (ST1A1) (EC 2.8.2.1) (Aryl sulfotransferase 1) (HAST1/HAST2) (Phenol sulfotransferase 1) (Phenol-sulfating phenol sulfotransferase 1) (P-PST 1) (ST1A3) (Thermostable phenol sulfotransferase) (Ts-PST) (P50225)
Organism: Homo sapiens (Human)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide variety of acceptor molecules bearing a hydroxyl or an amine groupe. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Displays broad substrate specificity for small phenolic compounds. Plays an important role in the sulfonation of endogenous molecules such as steroid hormones and 3,3'-diiodothyronin. Mediates the sulfate conjugation of a variety of xenobiotics, including the drugs acetaminophen and minoxidil (By similarity). Mediates also the metabolic activation of carcinogenic N-hydroxyarylamines leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis. May play a role in gut microbiota-host metabolic interaction. O-sulfonates 4-ethylphenol (4-EP), a dietary tyrosine-derived metabolite produced by gut bacteria. The product 4-EPS crosses the blood-brain barrier and may negatively regulate oligodendrocyte maturation and myelination, affecting the functional connectivity of different brain regions associated with the limbic system.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8093002}.
Interaction partners:
- Sulfotransferase 1A2
- Sulfotransferase 1A3
- Sulfotransferase 1C2
- Sulfotransferase 2B1
- Sulfotransferase 4A1
- Aspartate aminotransferase, cytoplasmic
- Cytochrome P450 1B1
- Steryl-sulfatase
- Cytochrome P450 2C9
- UDP-glucuronosyltransferase 1A6
Sequence:
MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDMIYQGGDLEKCHRAPIFMRVPFLEFKAPGIPSGMETLKDTPAPRLLKTHLPLALLPQTLLDQKVKVVYVARNAKDVAVSYYHFYHMAKVHPEPGTWDSFLEKFMVGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDFVVQHTSFKEMKKNPMTNYTTVPQEFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL
Protein: Transforming growth factor beta regulator 4 (C9IZN7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAHLVKRCTCLLREAARQAPAMAPVGRLRLAWVAHKTLTSSATSPISHLPGSLMEPVEKERASTPYIEKQVDHLIKKATRPEELLELLGGSHDLDSNQAAMIASVWHGTLSKLLGSLYALGIPKASKELQSVEQEVRWRMRKLKYKHLAFLAESCATLSQEQHSQELLAELLTHLERRWTEIEDSHTLVTVMMKVGHLSEPLMNRLEDKCLELVEHFGPNELRKVLVMLAAQSRRSVPLLRAISYHLVQKPFSLTKDVLLDVAYAYGKLSFHQTQVSQRLAT
Protein: Cell division cycle protein 27 homolog (Anaphase-promoting complex subunit 3) (Metaphase-to-anaphase transition defect protein 1) (Q9N593)
Organism: Caenorhabditis elegans
Function: Probable component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (By similarity). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins (By similarity). Developmental role in early embryogenesis and the metaphase to anaphase transition in oocyte and spermatocyte meiosis and mitosis in germ cells. Required for embryonic anterior-posterior axis formation. Plays a role in regulating the abundance of glr-1 receptors in postmitotic neurons, which may in turn control animal locomotion.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P38042}.
Interaction partners:
- Cell division cycle protein 23 homolog
- Anaphase-promoting complex subunit 2
- Cell division cycle protein 16 homolog
- Abnormal embryogenesis protein 30
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 1
- WD repeat-containing protein fzy-1
- Mitotic checkpoint protein bub-3
- TPR-like protein
Sequence:
MKESAASVAVRPQLREVFERFPADAHRTIEDEIHEMMKCYAFDDAIFLAELHYETDKSNNSESLLLYADCLYRANKKEECYGLLSSVKLSGARLFYLLARVSYDLNKIDDCRGALFEHDDGVIRKDILEEPRVASHANLLHAQMLCDESYMDLALESCQKSLDENILLWSAIITYLRFGGHDLAHTFEKHHRKSNGLYLDSPASSLKSETPSPNVPGPSSSSAASTAEPSRLESSVRRSTRGTIASANRETRNTTSNITPRQSTPGSTPSRINPTAPRKSSRISEMTTRRTESSVTGSRSSLFTEPERPHTRATHSSRNRANAALNSDTENSNASNTRTRSGIASVTRGSSSSQRTNPVRTSIRIADAAAAANKTAKTLSQRRRNEKQPLVSRNSNLARSLSGSTNSVASTASERPSEDEVSQINPPLPSVASSLNNDEPMDIVDGVYDPEYKKLFDVYQHIALIEESISTYNWRSADALFAKLDRDIILNTSMVRLQLGRACFEQSEYRECRNILDDLHKRRKWKVDGTELLSTSMWHLQDTHALSALSQILTTESRERPQSWCAAGNCFSLQRQHTQAIECMERAIQLDKRFAYAYTLLGHELIVQDELDKAAGSFRSALLLSPRDYRAWYGLGLVHLKKEQNLTALTNIQKAVNINPTNRAMLCTLSQIEQQRGQIDTALVLIDRALTLNPLDVACRFNRSRLLFEANRNEECLVELDKLKASSPDEAFIFHLLARVHRRMGNTHLALLNYSWAAELDPRGEQNITDSNVINREEYEDDEYGSPV
Protein: FI19895p1 (Rho GTPase activating protein at 16F, isoform B) (Rho GTPase activating protein at 16F, isoform C) (Rho GTPase activating protein at 16F, isoform D) (Rho GTPase activating protein at 16F, isoform F) (Q9VWY8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQTTTSQRPVTPGTPDSAHIVIGAAGFVAHERRQPGKTLMNCFRDRSTTSSSSSQAQHAYVRGHSVTSSTLFRLEGSGGSNCTLDKAGKQDTGRPEAVVLLRELKTRPNKLALLKSSSSKDLTRLFLDDSTNTAVLVSNTSIDVCSSNSSSGGSPAVGRSKSGRDRRNGLECCSSCSKRWHDLKQRMHTLEQDLLVQTTYSQELEQKVGEMSRQLTELLQERDRERDKDKARFAAAGGVAAPGKRTAHGSPNVRPSRLVAWMNLSNWFKSRPSVETLREQRIFFDEPCFDTELEMVLKHDQHRTVPRIVVDCCDLIEQKYRRSTQPIEGIYRQCGDYNKIQTLRFSIDANDYDSLRQPDVDIHTLTGVLKLFLREIKSPLVRVNEAKTFIGQPNQWLLTDLSAKLDSLKRLIRSLPESNRDTMDYIFGHFNRITKVPLQQISAETLSISVTPSIFHTVPQGVHMQDIQQLLREGETLADCVKLMIEYQGRIFE
Protein: Photosystem II reaction center protein Z (PSII-Z) (P12194)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00644}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00644}.
Interaction partners:
- Photosystem II CP43 reaction center protein
- Photosystem II reaction center protein K
- Photosystem II reaction center protein H
- Cytochrome b559 subunit alpha
- Photosystem II reaction center protein J
- Photosystem II D2 protein
- Photosystem II reaction center protein M
- Photosystem II CP47 reaction center protein
- Photosystem II protein D1
- Cytochrome b559 subunit beta
Sequence:
MTIAFQLAVFALIVTSSVLVISVPLVFASPDGWSNNKNVVFSGTSLWIGLVFLVAILNSLIS
Protein: Heat shock 70 kDa protein 14 (Heat shock protein 70-14) (AtHsp70-14) (Heat shock protein 91) (Q9S7C0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21418353, ECO:0000269|PubMed:24728648}. Nucleus {ECO:0000269|PubMed:21418353, ECO:0000269|PubMed:24728648}. Note=Predominantly detected in the cytoplasm. {ECO:0000269|PubMed:21418353}.
Interaction partners:
- FAM10 family protein At4g22670
- Heat shock protein 90-3
- Protein HEAT-INDUCED TAS1 TARGET 1
- Heat shock protein 90-2
- Heat shock protein 90-1
- Hsp70-Hsp90 organizing protein 2
- Endoplasmin homolog
- Heat shock protein 90-4
- Heat shock 70 kDa protein 8
- Iron-sulfur cluster co-chaperone protein HscB homolog
Sequence:
MSVVGFDFGNENCLVAVARQRGIDVVLNDESNRETPAIVCFGDKQRFIGTAGAASTMMNPKNSISQIKRLIGRQFSDPELQRDIKSLPFSVTEGPDGYPLIHANYLGEKRAFTPTQVMGMMLSNLKGIAEKNLNTAVVDCCIGIPVYFTDLQRRAVLDAATIAGLHPLRLIHETTATALAYGIYKTDLPESDQLNVAFIDIGHASMQVCIAGFKKGQLKILSHAFDRSLGGRDFDEVLFNHFAAKFKDEYKIDVSQNAKASLRLRATCEKLKKVLSANPLAPLNIECLMDEKDVRGVIKREEFEEISIPILERVKRPLEKALSDAGLTVEDVHMVEVIGSGSRVPAMIKILTEFFGKEPRRTMNASECVSRGCALQCAILSPTFKVREFQVHESFPFSISLAWKGAASEAQNGGAENQQSTIVFPKGNPIPSVKALTFYRSGTFSVDVQYSDVNDLQAPPKISTYTIGPFQSSKGERAKLKVKVRLNLHGIVSVESATLLEEEEVEVPVTKEHSEETTKMDSDKASAEAAPASGDCDVNMQDAKDTSDATGTDNGVPESAEKPVQMETDSKAEAPKKKVKKTNVPLSELVYGALKTVEVEKAVEKEFEMALQDRVMEETKDRKNAVESYVYDMRNKLSDKYQEYITDSEREAFLANLQEVEDWLYEDGEDETKGVYVAKLEELKKVGDPVEVRYKESLERGSVIDQLGYCINSYREAAMSTDPKFDHIELAEKQKVLNECVEAEAWLRGKQQQQDTLPKYATPALLSADVKSKAEALDKFCRPIMTKPKPVAKAEAPQAKGGEQADEGKSEPEQPASAEPMETENPAEGST
Protein: Arabinogalactan protein 3 (Fasciclin-like arabinogalactan protein 12) (B1NHU4)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MIMKQFDHLMLFFLLHTSCSTLLTLAQAPAAAPVVAPKATPVLAPASSPAPPGPTNVTKILEKAGQFSTFIRLMKATQVANQLLGQLNNTNNGITIFAPSDSAFSSLKSGTLNSLSDEQKVELIQFHIIPTYLSSAQFQTISNPLRTQAGDSGDGKFPLNVTSSGDTVNITSGLTNTSVSGTVYTDGQLAVYQIDRVLQPLQIFDPRPPAPAPAPAKSKKKKDDDVADSPADDSTDNSKAVRFTIGNNVGLFGVTAIVIALISL
Protein: Uncharacterized protein (Q387R6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDVSRTGGNTIELQEVVFSIPKHPGGSLGAPQHLHRSCRQCHRKINWGFNSAKSHHNAVANKDYDKCGVLNFPCSHYGRSSPRGSPQWNVLPEKKSLHVSCHLKALQRARIYLCSLLSPWYCCFILTRRA
Protein: Ankyrin repeat and SOCS box protein 7 (ASB-7) (Q9H672)
Organism: Homo sapiens (Human)
Function: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
- Cullin-5
- RING-box protein 2
- Zinc finger and BTB domain-containing protein 6
- RNA polymerase II-associated protein 3
- Transcriptional adapter 2-beta
- Elongin-B
- Kelch-like protein 20
- Protein VCF1
- Coiled-coil domain-containing protein 127
Sequence:
MLHHHCRRNPELQEELQIQAAVAAGDVHTVRKMLEQGYSPNGRDANGWTLLHFSAARGKERCVRVFLEHGADPTVKDLIGGFTALHYAAMHGRARIARLMLESEYRSDIINAKSNDGWTPLHVAAHYGRDSFVRLLLEFKAEVDPLSDKGTTPLQLAIIRERSSCVKILLDHNANIDIQNGFLLRYAVIKSNHSYCRMFLQRGADTNLGRLEDGQTPLHLSALRDDVLCARMLYNYGADTNTRNYEGQTPLAVSISISGSSRPCLDFLQEVTRQPRNLQDLCRIKIRQCIGLQNLKLLDELPIAKVMKDYLKHKFDDI
Protein: Tetratricopeptide repeat protein 17 (TPR repeat protein 17) (B5DEL3)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in primary ciliogenesis by modulating actin polymerization.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24475127}. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized with CATIP at F-actin rich zones and at dynamic plasma membrane protrusions. {ECO:0000250}.
Interaction partners:
- Probable protein phosphatase 1N
Sequence:
MAAAIGVRGRFELLSCSGPGWLISLSALLSVVARGALATTHWVVTEDGKIQQQVDSPMNLKHPHDLVILMRQETTVNYLKELEKQLVAQKIHIEENEDRDTGLEQRHNKEDPDCIKAKVPLGDLDLYDGTYITLESKDVRPEDFIDTESPVPPDPEQPDCTKILELPYSIHAFQHLRGVQERVNLSAPLLPKEDPIFTYLSKRLGRSIDDIGHLIHEGLQKNSSSWVLYNLASFYWRIKNEPYQVVECTMRALHFSSRHNKDIALVNLANVLHRAHFSADAAVVVHAALDDSAFFTSYYTLGNIYAMLGEYNHSVLCYDHALQAKPGFEQAIKRKHAVLCQQKLEQKLEAQHRSLQRTLNELKEYQKQHDHYLRQQEILEKHKLIQEEQILRNIIHETQMAKEAQLGNHQICRLVNQQHSLHCQWDQPVRYHRGDIFENVDYVQFGDDSSTSSMMSVNFDVPTNQSDVSESVRSSPVAHSVLWVWGRDSDAYRDKQHILWPKRADCTDSYPRVPLGGELPTYFLPPENKGLRIHELTSDDYSSEEEAQTPDCSITDFRKSHTLSYLVKELEVRMDLKAKIPDDHARKILLSRIKNYTIPEEEIGSFLFHAINKPNAPVWLILNEAGLYWRAVGNSTFAIACLQRALNLAPVQYQDIPLVNLANLLIHYGLHLDATKLLLQALAVNSSEPLTFLSLGNAYLALKNVSGALEAFRQALKLTTRCPECESSLKLIRCMQFYPFLYNITSSVCSGHCHEKTLDNSHDKQKYFAKPQSLDAAEEEPSRHGADEDPVLSVENAGRDSDALRLESTVVEESNGSDEVEKSEETKMSEEILALVDEFQQAWPLEGLGGTLEMKGRRLDLQGIRVLKKGPQDGVAKSSCYGDCRSEDDEATEWITFQVKRVKKPKGDHKKPPGKKVEASQAENGQRYQANLEITGPKVASPGPQEKKRDYQSMGWPSPDECLKLRWVELTAIVSTWLAVSSKNIDITEHIDFATPIQQPAMEPLCNGNLPTSMHTLDHLHGVSNRASLHYTGESQLTEVLQNLGKDQYPQQSLEQIGTRIAKVLEKNQTSWVLSSMAALYWRVKGQGKKAIDCLRQALHYAPHQMKDVPLISLANILHNAKLWNDAVVVATMAVEIAPHFAVNHFTLGNVYVAMEEFEKALVWYESTLKLQPEFVPAKNRIQTIQCHLMLKKGRRSP
Protein: BMP2 (Bone morphogenetic protein 2 precursor) (O13109)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MVSSTAALMVLMVTQVFFAGSSGLVPQVGRSSLSPDVLHAFELRLLSMFGLQHRPTPSTSAVVPQYMLDLYSAHSVNAEQVSRPRAHLGKGSERSASRANTIRSFHHDESTEDPSSSSVRTTQRFLFNLTSIPDEELVTSADVRVFREQIVSSLNNASAGFHRINVHEIIRPSGSLQEPITRLLDTRLVQHSLSKWESFDVTPAVLKWTTDGHPNHGILVEISHPDQDSRKHVRVSRSLHNNEDTWSQMRPLLVTYSHDGKGNVLHSREKRQARNNKQRKKHKANCRRHSLYVDFSDVGWNDWIVAPPGYHAFYCQGECPFPLADHLNSTTNAMVQTLVNSVNSNIPRACCVPTDLSPVSLLYLDEYERVILKNYQDMVVEGCGCR
Protein: DNA polymerase (EC 2.7.7.7) (EC 3.1.11.-) (Gene product 2) (gp2) (Protein p2) (P03680)
Organism: Bacillus phage phi29 (Bacteriophage phi-29)
Function: Polymerase responsible for protein-primed viral DNA replication by strand displacement with high processivity and fidelity. To start replication, the DNA polymerase forms a heterodimer with a free primer terminal protein (TP), recognizes the replication origins at both 5' ends of the linear chromosome, and initiates replication using as primer the OH-group of Ser-232 of the TP. This polymerase possesses three enzymatic activities: DNA synthesis (polymerase), primer terminal protein (TP) deoxynucleotidylation, which is the formation of a covalent linkage (phosphoester) between the hydroxyl group of a specific serine residue in TP and 5'-dAMP, a reaction directed by the second T at the 3' end, and 3' to 5' exonuclease activity. Exonuclease activity has a proofreading purpose. DNA polymerase edits the polymerization errors using an intramolecular pathway as the primer terminus travels from one active site to the other without dissociation from the DNA. DNA polymerization catalyzed by the DNA polymerase is a highly accurate process, but the protein-primed initiation is a quite inaccurate reaction. Since the polymerase initiates the replication on the second thymine, the TP-dAMP initiation product translocates backwards to recover the template information of the first nucleotide (sliding back-mechanism).
Interaction partners:
Sequence:
MKHMPRKMYSCDFETTTKVEDCRVWAYGYMNIEDHSEYKIGNSLDEFMAWVLKVQADLYFHNLKFDGAFIINWLERNGFKWSADGLPNTYNTIISRMGQWYMIDICLGYKGKRKIHTVIYDSLKKLPFPVKKIAKDFKLTVLKGDIDYHKERPVGYKITPEEYAYIKNDIQIIAEALLIQFKQGLDRMTAGSDSLKGFKDIITTKKFKKVFPTLSLGLDKEVRYAYRGGFTWLNDRFKEKEIGEGMVFDVNSLYPAQMYSRLLPYGEPIVFEGKYVWDEDYPLHIQHIRCEFELKEGYIPTIQIKRSRFYKGNEYLKSSGGEIADLWLSNVDLELMKEHYDLYNVEYISGLKFKATTGLFKDFIDKWTYIKTTSEGAIKQLAKLMLNSLYGKFASNPDVTGKVPYLKENGALGFRLGEEETKDPVYTPMGVFITAWARYTTITAAQACYDRIIYCDTDSIHLTGTEIPDVIKDIVDPKKLGYWAHESTFKRAKYLRQKTYIQDIYMKEVDGKLVEGSPDDYTDIKFSVKCAGMTDKIKKEVTFENFKVGFSRKMKPKPVQVPGGVVLVDDTFTIK
Protein: Ubiquitin-conjugating enzyme E2 D2 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme D2) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme D2) (Ubiquitin carrier protein D2) (Ubiquitin-conjugating enzyme E2(17)KB 2) (Ubiquitin-conjugating enzyme E2-17 kDa 2) (Ubiquitin-protein ligase D2) (P62839)
Organism: Rattus norvegicus (Rat)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by RIGI in response to viral infection. Essential for viral activation of IRF3 (By similarity). Mediates ubiquitination of PEX5.
Interaction partners:
Sequence:
MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDREKYNRIAREWTQKYAM
Protein: histidine kinase (EC 2.7.13.3) (Q9AAR6)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Cell envelope regulator
- histidine kinase
- PetR protein, putative
- DUF952 domain-containing protein
- TVP38/TMEM64 family membrane protein
- Phosphohistidine phosphatase
- Dihydroorotate dehydrogenase
- Chemotaxis protein CheYI
- Histidine protein kinase DivJ
- Non-motile and phage-resistance protein
Sequence:
MVEPGSPSEDKTQKPRKRFPWPGGLSARLLLFTAVVVNFGGLLILPPALAAYEEQWLLDRVRAGELASTIAESDPELRVSDAVANQMFDQAGAVTVAVQVDGARRLVLPPKQPFETPYLVDLRRQNPGSWLAAPFYTLTSPKGSMVRVMAEPRFRKAEFIEVVLPDAPLKARLVAYFWQLAGVTIFVATLAGVLVYAFLNIFLVRPMQRITRAMEAFRSDPDDPAARIVLSNRRDEIGRAELELDRMQADLLAALSSKARLAALGEAVAKINHDLRNMLTSAQMASDRLAALGDPKVAQALPRLERALDRAINLASDVMAYGKSKEPEPVIRVIPLRPALDMAAEDAGLSAQGVSLETVIGPREQVLADPDQLHRILTNLLRNAREAIEGAPDRGGKGKVFVELRRADGSSVLRLSDDGPGVPERARANLFQPFVGSVRRGGTGLGLAIARELAQGHGGDLALVETGPGGSVFDLTLSGAPDPLPETPSEPGDRAADAPAG