wanglab/gogpt-training-data huggingface dataset:
Protein: O(6)-methylguanine-induced apoptosis 2 (MAPO2) (Sperm-tail PG-rich repeat-containing protein 1) (Q5TH74)
Organism: Homo sapiens (Human)
Function: May positively contribute to the induction of apoptosis triggered by O(6)-methylguanine.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MDNSAQKNERTGKHPRRASEVQKGFTAAYPTQSSIPFKSQASVIPESEKKGFNSQAKRFPHKKNDIPGPGFYNVIHQSPVSNSVSLSKKGTCMFPSMCARLDTIISKYPAANAYTIPSDFISKRDFSNSCSSMFQLPSFMKALKFETPAPNYYNASVSCCKQRNNVCTRAGFMSKTQRGSFAFADKGPPPGHYDINESLVKQSPNTLMSCFKSKTNRGLKLTSTGPGPGYYNPSDCTKVPKKTLFPKNPILNFSAQPSPLPPKPPFPGPGQYEIVDYLGPRKHFISSASFVSNTSRWTAAPPQPGLPGPATYKPELPGKQSFLYNEDKKWIPVL
Protein: Phosphatidylinositol-binding clathrin assembly protein (Clathrin assembly lymphoid myeloid leukemia) (CALM) (Q7M6Y3)
Organism: Mus musculus (Mouse)
Function: Cytoplasmic adapter protein that plays a critical role in clathrin-mediated endocytosis which is important in processes such as internalization of cell receptors, synaptic transmission or removal of apoptotic cells. Recruits AP-2 and attaches clathrin triskelions to the cytoplasmic side of plasma membrane leading to clathrin-coated vesicles (CCVs) assembly. Furthermore, regulates clathrin-coated vesicle size and maturation by directly sensing and driving membrane curvature. In addition to binding to clathrin, mediates the endocytosis of small R-SNARES (Soluble NSF Attachment Protein REceptors) between plasma membranes and endosomes including VAMP2, VAMP3, VAMP4, VAMP7 or VAMP8. In turn, PICALM-dependent SNARE endocytosis is required for the formation and maturation of autophagic precursors. Modulates thereby autophagy and the turnover of autophagy substrates such as MAPT/TAU or amyloid precursor protein cleaved C-terminal fragment (APP-CTF).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q13492}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q13492}. Golgi apparatus {ECO:0000250|UniProtKB:Q13492}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q13492}. Nucleus {ECO:0000250|UniProtKB:Q13492}. Note=Colocalized with clathrin in the Golgi area. Interaction with PIMREG may target PICALM to the nucleus in some cells. {ECO:0000250|UniProtKB:Q13492}.
Interaction partners:
- Clathrin heavy chain 1
- AP-2 complex subunit alpha-1
- Epidermal growth factor receptor substrate 15
- Cyclin-G-associated kinase
- AP-2 complex subunit alpha-2
- Epidermal growth factor receptor substrate 15-like 1
- Vesicle-associated membrane protein 2
- Disabled homolog 2
- Clusterin
- AP2-associated protein kinase 1
Sequence:
MSGQSLTDRITAAQHSVTGSAVSKTVCKATTHEIMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNSSWVVVFKSLITTHHLMVYGNERFIQYLASRNTLFNLSNFLDKSGLQGYDMSTFIRRYSRYLNEKAVSYRQVAFDFTKVKRGADGVMRTMNTEKLLKTVPIIQNQMDALLDFNVNSNELTNGVINAAFMLLFKDAIRLFAAYNEGIINLLEKYFDMKKNQCKEGLDIYKKFLTRMTRISEFLKVAEQVGIDRGDIPDLSQAPSSLLDALEQHLASLEGKKIKDSTAASRATTLSNAVSSLASTGLSLTKVDEREKQAALEEEQARLKALKEQRLKELAKKPHTSLTTAASPVSTSAGGIMTAPAIDIFSTPSSSNSTSKLPNDLLDLQQPTFHPSVHAMSAAPQGASTWGDPFSATLDAVEDAIPSLNPFLTKSSGDVHLPIASDVSTFTTRTPTHEMFVGFSPSPVAQPHSSAGLNVDFESVFGNKSTNVAVDSGGFDELGGLLKPTVASQNQSLPVAKLPPNKLVSDDLDSSLANLVGNLGIGNGTTKNDVSWSQPGEKKLTGGSNWQPKVAPTTAWSAATMNGMHFPQYAPPVMAYPATTPTGMIGYGIPPQMGSVPVMTQPTLIYSQPVMRPPNPFGPVSGAQIQFM
Protein: T. brucei spp.-specific protein (Q38CU8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MHSCWIGSLLLLVGLMFFSIVCRANGTEVKPLEESAEDICAAMKSLNTVNNTVQNIITTIRNHKAKLIRYLQDVETAFERTSSAAAAAKQYGGTFRTASVASKIANDAMSNSTRAMLDAETSHNTTLIIEAAANIEAQSARDNATAAAVALQAIWKTTVGTARLQANHTDCVYTPADQMLTSQKLNEHKEKLVVTDSKYNDEHKELKELWARSYLKLFLPLDQLHMLLQKLEWDVATTSEMETTAEKAADAAVAAQEDVEKAAELAAESATESVRAKRYSDRVARGNMKFKTIAGFHEEPLPEVVPRPGAKASAASDPLENEDGAFYVSRGIMPLSQAFFVIAFTI
Protein: Integrator complex subunit 5 (Int5) (Q6P9B9)
Organism: Homo sapiens (Human)
Function: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes (Probable). Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:23904267, ECO:0000269|PubMed:39032490}. Cytoplasm {ECO:0000269|PubMed:23904267}. Nucleus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Integrator complex subunit 10
- Integrator complex subunit 4
- Integrator complex subunit 8
- Integrator complex subunit 2
- Integrator complex subunit 14
- Integrator complex subunit 1
- Integrator complex subunit 12
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Integrator complex subunit 9
- DNA-directed RNA polymerase II subunit RPB1
Sequence:
MSALCDPPGAPGPPGPAPATHGPAPLSAQELSQEIKAFLTGVDPILGHQLSAREHARCGLLLLRSLPPARAAVLDHLRGVFDESVRAHLAALDETPVAGPPHLRPPPPSHVPAGGPGLEDVVQEVQQVLSEFIRANPKAWAPVISAWSIDLMGQLSSTYSGQHQRVPHATGALNELLQLWMGCRATRTLMDIYVQCLSALIGSCPDACVDALLDTSVQHSPHFDWVVAHIGSSFPGTIISRVLSCGLKDFCVHGGAGGGAGSSGGSSSQTPSTDPFPGSPAIPAEKRVPKIASVVGILGHLASRHGDSIRRELLRMFHDSLAGGSGGRSGDPSLQATVPFLLQLAVMSPALLGTVSGELVDCLKPPAVLSQLQQHLQGFPREELDNMLNLAVHLVSQASGAGAYRLLQFLVDTAMPASVITTQGLAVPDTVREACDRLIQLLLLHLQKLVHHRGGSPGEGVLGPPPPPRLVPFLDALKNHVGELCGETLRLERKRFLWQHQLLGLLSVYTRPSCGPEALGHLLSRARSPEELSLATQLYAGLVVSLSGLLPLAFRSCLARVHAGTLQPPFTARFLRNLALLVGWEQQGGEGPAALGAHFGESASAHLSDLAPLLLHPEEEVAEAAASLLAICPFPSEALSPSQLLGLVRAGVHRFFASLRLHGPPGVASACQLLTRLSQTSPAGLKAVLQLLVEGALHRGNTELFGGQVDGDNETLSVVSASLASASLLDTNRRHTAAVPGPGGIWSVFHAGVIGRGLKPPKFVQSRNQQEVIYNTQSLLSLLVHCCSAPGGTECGECWGAPILSPEAAKAVAVTLVESVCPDAAGAELAWPPEEHARATVERDLRIGRRFREQPLLFELLKLVAAAPPALCYCSVLLRGLLAALLGHWEASRHPDTTHSPWHLEASCTLVAVMAEGSLLPPALGNMHEVFSQLAPFEVRLLLLSVWGFLREHGPLPQKFIFQSERGRFIRDFSREGGGEGGPHLAVLHSVLHRNIDRLGLFSGRFQAPSPSTLLRQGT
Protein: Uncharacterized protein C1393.12 (O94724)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MNRRVTLGALAAAVGVGYYMTRHNRQASSRLEQKNAEIVRAVENEGQRFDKAVGETTEKAKSYLQSGKERVVDELDKPRENVKNVLSEAQAKGTEQAEALKKGTSKWF
Protein: Phosphoinositide phospholipase C (EC 3.1.4.11) (Q385H1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- inositol-polyphosphate 5-phosphatase
- 1-phosphatidylinositol 4-kinase
- 1-phosphatidylinositol 4-kinase
- Phosphatidylinositol 4-phosphate 5-kinase alpha, putative
- non-specific serine/threonine protein kinase
- Inositol/phosphatidylinositol phosphatase, putative
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Inositol-1-monophosphatase
- phosphatidylinositol 3-kinase
- 1-phosphatidylinositol-3-phosphate 5-kinase
Sequence:
MGGCTSRGLSEEKLACYSHRTGNLVDEHLSTGAVEAHELQPFFSSLLGAITDLLKCSREDAVEFLACASSANPRAAELFTSFCAANPLNLIKWDVNHAKFMMIWIKYDDDNSGDICVRELRKILKGLSFPERLSQKMIDELEATGGRANYKLMQGTFMSLTRLNELTYAMRNIVGPDRDVMTKAEFVTFLKETQGEGADGEELHVFLDAVGCTEEHPVHLDAFLSFLSDRRFNSIVNNRKVSSVYHDMTRPICEYFINSSHNTYLTGDQLLSKSSTDMYKRVLLDGCRCVELDCWDGRKGQPVVYHGYTRTSKLWFRDCISTIKKYAFVNSIYPVILSLEVHTSLRQQDRMAEILCETLGDMLFCSPWGAGEQTSFTFSPEALKGKILLKSKRATTPTDGVQVDDDDDEDEEADGVVENFVPPETARRCRGGGKTNSRGAEKKKKVSKVSEKLSRLISIESIGYKGVEDLSYLEMRQPYHCSSFTEGKAGKIASSNQEEFVAINNRCLSRIYPTGTRIGSSNFHPQTFWNCGCQLVALNWQNYKSYQLRLNRGFFSDNGNCGYLLKPTAVDIARARGPKRQSRLLTIEIISAFCLPRRKNASGSSIVDSRVAALIEGPGMEKSQRNTSPIHNNGFHPVWRGERLNNEFCWKVYEWELSTLVMQVYDEDTKSNNLLGEYVVPLRALKKGIRQVPLRDLKGSIIHGSFLMVQVSYQ
Protein: Prolyl endopeptidase (EC 3.4.21.-) (Q4QHU7)
Organism: Leishmania major
Interaction partners:
Sequence:
MSSDSSVAASAQPPIAAKKPHRVTFGYVEGEDRGPNPMNPPRYREDPYFWMRDDDRKDPAVIEHLNKEKVYFQARSADIAQLRDDIYAEHISHINEDDMSAPYVYGKYRYYTREVKGKPYKIYCRVFTDKEPGDVAAEEVIIDVNQVAEGKAFCDVMEVKPAPPEHDLVAFSVDMSGNEVYTIEFKRISDPSQTIADKVSGTNGEIVWGPDHTSLFYVTKDETLRENKVWRHVMGKLQSEDVCLYEEHNPLFSAFMYKAADTNTLCIGSQSPETAEVHLLDLRKGNAHNTLEIVRPREKGVRYDVQMHGTSHLVILTNEGGAVNHKLLIAPRGQPSDWSHVLVDHSEDVFMESIAVRSNYLVVAGRRAGLTRIWTMMADSQDGVFKAGTGLREVVMEEPIFTVHLVESQMLEYEEPTFRMEYSSLATPNTWFDVSPQDHSRTAVKVREVGGGFDAANYKVERRFATAPDQTKIPLSVVYHKDLDMSQPQPCMLYGYGSYGLSMDPQFSIQHLPYCDRGMIFAIAHIRGGSELGRAWYEIGAKYLTKRNTFSDFIAAAEFLVNAKLTTPSQLACEGRSAGGLLMGAVLNMRPDLFKVALAGVPFVDVMTTMCDPSIPLTTGEWEEWGNPNEYKYYDYMLSYSPMDNVRAQEYPNIMVQCGLHDPRVAYWEPAKWVSKLRECKTDNNEILLNIDMESGHFSAKDRYKFWKESAIQQAFVCKHLKSTVRLLVRR
Protein: Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform (PP2A B subunit isoform B'-beta) (PP2A B subunit isoform B56-beta) (PP2A B subunit isoform PR61-beta) (PP2A B subunit isoform R5-beta) (Q80W83)
Organism: Rattus norvegicus (Rat)
Function: As the regulatory component of the serine/threonine-protein phosphatase 2A (PP2A) holoenzyme, modulates substrate specificity, subcellular localization, and responsiveness to phosphorylation. The phosphorylated form mediates the interaction between PP2A and AKT1, leading to AKT1 dephosphorylation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q15173}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Protein phosphatase 2 scaffold subunit A alpha
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Shugoshin 1
- Protein phosphatase 1 regulatory subunit 1A
- Apoptosis regulator Bcl-2
- D
- Meiotic recombination protein REC8 homolog
- Ryanodine receptor 2
Sequence:
METKLPPASTPTSPSSPGLSPVPPPDKVDGFSRRSLRRARPRRSHSSSQFRYQSNQQELTPLPLLKDVPASELHELLSRKLAQCGVMFDFLDCVADLKGKEVKRAALNELVECVGSTRGVLIEPVYPDIIRMISVNIFRTLPPSENPEFDPEEDEPNLEPSWPHLQLVYEFFLRFLESPDFQPSVAKRYVDQKFVLMLLELFDSEDPREREYLKTILHRVYGKFLGLRAYIRKQCNHIFLRFIYELEHFNGVAELLEILGSIINGFALPLKTEHKQFLVRVLIPLHSVKSLSVFHAQLAYCVVQFLEKDATLTEHVIRGLLKYWPKTCTQKEVMFLGEMEEILDVIEPSQFVKIQEPLFKQVARCVSSPHFQVAERALYFWNNEYILSLIEDNCHTVLPAVFGTLYQVSKEHWNQTIVSLIYNVLKTFMEMNGKLFDELTASYKLEKQQEQQKAQERQELWRGLEELRLRRLQGTQGAKEAPVPRPTPQVAASGGQS
Protein: Rhomboid domain containing 1 (C9JQK8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MQRRSRGINTGLILLLSQIFHVGINNIPPVTLATLALNIWFFLNPQKPLYSSCLSVEKCYQQKDWQRLLLSPLHHADDWHLYFNMASMLWKGINLERRLGSRWFAYVITAFSVLTGVVYLLLQF
Protein: EF-hand domain-containing family member B (Cilia- and flagella-associated protein 21) (Q8N7U6)
Organism: Homo sapiens (Human)
Function: Cytosolic sensor for calcium, modulates the interaction of STIM1 and ORAI1 upon store depletion and the activation of store-operated Ca(2+) entry (SOCE) and NFAT translocation from cytosol to nucleus. Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:36191189}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q8CDU5}. Cytoplasm {ECO:0000305|PubMed:30481768}.
Interaction partners:
- WD repeat-containing protein 90
- Parkin coregulated gene protein
- Enkurin
- EF-hand domain-containing family member C2
- EF-hand domain-containing protein 1
- Cilia- and flagella-associated protein 20
- Cilia- and flagella-associated protein 45
- Tubulin alpha-1A chain
- Tubulin beta-4B chain
- Cilia- and flagella-associated protein 107
Sequence:
MNMEIGHPHEGKDDLGDKRVIMGTKFPMELGIRVGLGKEDSRCGESPVVSNKCEGRMAPPETKFPLSKGLEMGLERQNISRTVMQRGSLGVDSVSASQGTKPSLLPGRMGLENESLLAGYTHERIIQPPLGRVCGSSQAAGSRRAPLASGPEGVEELVGKPAFVMEPRQEMEKESTCVLMKPNTEIKLPVEVDIGLTQAEGPDETKNTEPQMGLVIEPPQCQFAQQHEQRKEAGNIESGVEPPDRIRPIYSGKFFDRTPCWPSAGKVIPVGYRVATCLTEKLPRLITPPEAKKYFNFRYPPAGVERVFYGRANDPQIAPYLTHGIRSKISVLANTLINPQPITTFQQKIKDKKESIYLSNRRAPLGKSHDQAPGLPKGMDTTNTTFGTAVIKEYSAKDVVNPPKSYEEVFKEGNEGHDLYVVSHNDYYAGEAKNRKYNPSSFHRCSVYGVPTPHFNDGRAMAKSLYWLHELQMKRGAKFVSKRADDFKEKFQHKLGRVLDPIAETMNVPPDCTFGACLRPEEYGVGDLIHNRLPDEYLRGKDRQRALIAAVRHHLKKVNYQKFDTLLAAFRHYDKKGDGMIDKDELQEACDQANLSLDDKLLDQLFDYCDVDNDGFINYLEFANFLNWKDKMLLKEYEERVIIKGRKPDCVNPTEANVEEPEQTLLIKPEDIVLKEAGSTEKTLRTLLRPSDKVSNYYKTTSSEINAIVGAIPSTCYPICGVPTIRSDIPAPRIRRISDRTNYGEEGSAYSLLYPTIFARKGVFERDFFKTRSKEEIAEILCNIGVKLSDEEFENVWNLASKKHHRGEVCVENIRNVLDELRHADRIKCKTLM
Protein: TNF receptor associated factor 7 (A0A8I6AMJ5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGPAHTNSIAGRLPPLAPLPIRHGMRRTAWAQPPDRLPPSVQPPINTPRRSDSAISVRSLHSESSMSLRSTFSLPEEEEEPEPLVFAEQPSVKLCCQLCCSVFKDPVITTCGHTFCRRCALKSEKCPVDNAKLTVVVNNIAVAEQIGELFIHCRHGCRAAGTGKPGVFEVDPRGCPFTIKLSARKDHESSCDYRPVRCPNNPSCPPLLKMNLEAHLKECEHIKCPHSKCTFIGNQDTYETHLETCRFEGLKEFLQQTDDRFHEMHVALAQKDQEIAFLRSMLGKLSEKIDQLEKSLELKFDVLDENQSKLSEDLMEFRRDASMLNDELSHINARLNMGILGSYDPQQIFKCKGTFVGHQGPVWCLCVYSMGDLLFSGSSDKTIKVWDTCTTYKCQKTLEGHDGIVLALCIQGGSADCTIIVWDIQNLQKVNTIRAHDNPVCTLVSSHNMLFSGSLKAIKVWDIVGTELKLKKELTGLNHWVRALVAAQSYLYSGSYQTIKIWDIRTLDCIHVLQTSGGSVYSIAVTNHHIVCGTYENLIHVWDIESKEQVRTLTGHVGTVYALAVISTPDQTKVFSASYDRSLRVWSMDNMICTQTLLRHQGSVTALAVSRGRLFSGAVDSTVKVWTC
Protein: Diphthamide biosynthesis protein 3 (Q9UT33)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. Dph1 and dph2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising dph3 and a NADH-dependent reductase, predominantly cbr1. Acts as an electron donor to reduce the Fe-S cluster in dph1-dph2 keeping the [4Fe-4S] clusters in the active and reduced state. Restores iron to dph1-dph2 iron-sulfur clusters which have degraded from [4Fe-4S] to [3Fe-4S] by donating an iron atom to reform [4Fe-4S] clusters, in a manner dependent on the presence of elongation factor 2 and SAM. Associates with the elongator complex and is required for tRNA Wobble base modifications mediated by the elongator complex. The elongator complex is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- 2-
- 2-
- RCC1 repeat-containing protein C10F6.04
- Elongator complex protein 3
- Diphthine methyl ester synthase
- Diphthamide biosynthesis protein 4
- Diphthine--ammonia ligase
- Diphthine methyltransferase
- Elongator complex protein 1
- Elongator complex protein 4
Sequence:
MSFYDEIELEDFTFDAGTNLYTFPCPCGDRFEISLEDLQLGEDVARCPSCSLIVRVIYDEDEFMEVDNDASTAPIIIAA
Protein: DMT family organic anion transporter (Eurofung) (Q5B8L7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
MSSSEEKVRTSGEVSRPEPTLPTVNPAVDKPEPPKPTFHPAVYVTSWIALSSSVILFNKHILDYAQFRFPIILTTWHLAFATFMTQVLARTTTLLDGRKTVKMTGRVYLRAIVPIGLFFSLSLICGNVTYLYLSVAFIQMLKATTPVAVLLATWGMGMAPVNLKVLTNVSVIVFGVIIASFGEIKFVFIGFLFQIAGIIFEATRLVMVQRLLSSAEYKMDPLVSLYYFAPVCAVMNGVTALFLEVPTLTMDHIYNVGVWTLLANAMVAFMLNVSVVFLIGKTSSLVMTLCGVLKDILLVVASMVIWNTPVTALQFFGYSIALIGLVYYKLGGDKIKEYTSQANRAWAEYGATHPAQRRFVIIGAALLSFFLLVGSMAPSYAPDSVANVKGMLGGASTGNA
Protein: Zcf2p (A0A1D8PDI4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Cysteine dioxygenase CDG1
- Sulfite efflux pump SSU1
Sequence:
MSEKIKREKPVKVRKHVSSACLECRRRHFKCDGKQPVCDRCQKSNKPCQYVASHRGGSRKKGVSTKKKPVTVNDINQGPEMPMFVADIEDFGKSKSTENSANDGNEIKSNDEMLEKLMTLPCAHDQNRCQDSNCPGKSAVRYMKSRPEKRGQLNESETHMMETLRKRIKLESTMSNIDCLFSDNNPPIDIRSFKELEMTTAVHDPSNYVDLTVLDKDVILKNYYETFHKAHPILPAREEMLIYMSNSSIEKELLPILSIVSDGETTSVYARAIDLVSDRLIQCVEVVKSFGYIDIVSLQVLTLVSFVAHVSSLHALSKNLRHFCIYLLQDLQINLLDAPSKHGSNDMTPESETNAPLKVFNSPRLSHVSRDSIDQCARRLFWELNFVDIITGSADGKTVSSFDKIESFVDFPTVPSRDEFDYKGRSEAGTLVTNAVKMNIEITNKRPYDILLTRLQASLSSWEMRLEDPSLFEAPPLIDKSGRVNEGVHQAILLFNYAKIFVHRPFSYLWKINSPQHPKCNGEAVDSTNVPPQLQANSRTTIETRKTIEGANSIVQVLMDTGASKVFQRTHFFACALALSSLVHLSAYIWVETTLAVDKAQAFGLNEEDLDVYTEYIKLALTAIYPISKHWQLSGKLAKHIRDSLTTLRPKLYSKLKDFLPQLEIGMEKMKIREGDSTGEDSSRSSALPMNAVSSSTTTTNYDGLQSQDNNNSTLSNRQSALDIHDGAIPGDNISGSYDFENLSWEPVSPISPSGCDWIDKGLLDFNFDPFPSTL
Protein: Tetratricopeptide repeat protein (B6GVA2)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Interaction partners:
Sequence:
MVSIEQVESPAAGKTSTAAEAPSGYVSDGYETASDSELNGAENGSNRESENTINTASSSSDGDFLKEKTQEQQPEVNQEQLNEKALAQANDAKVEGNALFKDGLYEEALSKYELALQVAADIPSSTEIRSICHANRAACFTKLGKHEETIKECTKALELNPTYIKALVRRAEAHEKLEHFEEAITDMTKILELEPSHDQARRTVILLKPLADEKREKMKEEMIGKLKEMGNSILGRFGMSVDNFKTVKDPNTGSYSVQFQK
Protein: At2g03850 (Late embryogenesis abundant protein (LEA) family protein) (Putative cold-regulated protein) (Q9SI55)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Late embryogenesis abundant domain-containing protein / LEA domain-containing protein
- Protein GOLVEN 6
- F12A21.10
- Protein ROOT INITIATION DEFECTIVE 3
Sequence:
MAMSISGAVFNGLGSSFLISRGKRSGVGLGVVAMRVGRKNVITSPKCKKSWVPTAVKGDGNSKLDPKWLDDASQKASDYVKEKGSEVGHASAQKGQDVNDHVDRAKYYMFEKASEAIDNVAEIAQFASEFVTEKGKETKKETASISEKAKDFIVEKAGEIIDIATDVSKKTAKYVGDKAKEVKEAIMPPKT
Protein: DNA photolyase (EC 4.1.99.3) (O93963)
Organism: Hypocrea atroviridis (Trichoderma atroviride)
Interaction partners:
Sequence:
MLARSVYTVTRSQITSTSYLPSLSSYSKFLQPKFTFSTMPPKGSKRETASPVGKANGVETKRVKHEANQDELHQPHPFAKDAEEHGIVLRRFYPHEMSTSRAYAYNSNEIERPMEGLVAALEETAGARKQAKVRHAVVHWFKMDLRHSDNRSLALASAKAKEAGVPLICVYIISPQDFEAHLTSPVRVDFMLRTLSVLKDDLAALDIPLHVETVDKRKDIPRRILELMEEWGSNHLFANMEYEVDELRRETRMIRQFAENNMSFEVVHDTCVVPPGELHSGTGKQYAVYTPWYRAWMAHIHENLDLLEIYDRPEKNPGATRRTFKTLFDCPIPDAPKNKQLNDEEKKRFHGLWPCGEHEAMSRLEKFCDEAVTSYHDRRNIPGDNGTSCLSVHLASGTISSRTCVRTARDRNKTKRLDGGHQGIHVWISEVAWRDFYKHVLVNWPYVCMNKPFKPEYANIEWSYNMDHFEAWCEGRTGFPIVDAAMRQLNHMGYMHNRCRMIVASFLSKDLLIDWRMGEKYFMEHLVDGDFASNNGGWGFSASVGVDPQPYFRVFNPLLQSEKFDPNGEYIRKWIPELKALSDKEIHDPYNRGAGTKAKKQGYPKQIVDHKGARERALSAYKDGLERGI
Protein: Cytochrome P450 709B3 (EC 1.14.-.-) (Q9T093)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in abscisic acid (ABA) and salt stress response. May regulate the salt stress response independently of well-characterized pathways. Does not function as cytokinin hydroxylase in yeast heterologous system (Probable).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Plant invertase/pectin methylesterase inhibitor superfamily protein
Sequence:
MELISTINLLTIVLLLFVVSKIWKACWILLLRPLMLSKRFKKQGISGPKYKILYGNLSEIKKMKKEADLCVLDPNSNDIFPRVFPQYHQWMSQYGDTFLFWTGTKPTIYISNHELAKQVLSSKFGFTIIPVKRPEVFILFGKGLSFIQGDDWIRHRRILNPAFSMDRLKAMTQPMGDCTLRIFEEWRKQRRNGEVLIKIEISKEFHKLTADIIATTAFGSSYAEGIELCRSQTELEKYYISSLTNVFIPGTQYLPTPTNLKLWELHKKVKNSIKRIIDSRLKSKCKTYGYGDDLLGVMLTAAKSNEYERKMRMDEIIEECKNFYYAGQGTTSILLTWTTMLLSLHQGWQEKLREEVFNECGKDKIPDTDTFSKLKLMNMVLMESLRLYGPVIKISREATQDMKVGHLEIPKGTSIIIPLLKMHRDKAIWGEDAEQFNPLRFENGISQATIHPNALLPFSIGPRACIAKNFAMVEAKTVLTMILQQFQLSLSPEYKHTPVDHFDLFPQYGLPVMLHPLG
Protein: Dynein light chain 1, cytoplasmic (Q22799)
Organism: Caenorhabditis elegans
Function: Acts as a non-catalytic accessory component of a dynein complex (By similarity). Part of a complex with bicd-1 and egal-1, which is recruited to the nuclear envelope by unc-83, where in turn, it recruits dynein to the nuclear surface and regulates nuclear migrations in hypodermal precursor cells. Probably within a dynein motor complex, plays a role in the cell fate specification of the germline and oogenesis. In particular, it inhibits germ cell proliferation. Regulates the function and localization of the RNA-binding protein fbf-2 in the germline. Plays a role in mitotic and meiotic processes. Involved in the pairing of homologous chromosomes. Independently of its dynein-mediated functions, plays a role in germ cell apoptosis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P63170}. Nucleus envelope {ECO:0000269|PubMed:27864381, ECO:0000305|PubMed:20005871}. Cytoplasmic granule {ECO:0000269|PubMed:27864381}. Note=Probably recruited to the nuclear envelope by unc-83 (PubMed:20005871). Localizes to perinuclear patches in the transition zone (PubMed:27864381). Localizes to P-granules in the mitotic region and transition zone (PubMed:27864381). {ECO:0000269|PubMed:27864381, ECO:0000305|PubMed:20005871}.
Interaction partners:
- WD_REPEATS_REGION domain-containing protein
- Dynein heavy chain, cytoplasmic
- Egalitarian protein homolog
- Dynein heavy chain linker domain-containing protein
- Dynein Heavy Chain
- Dynein light intermediate chain
- Dynein light chain roadblock
- Nsp1_C domain-containing protein
- F-actin-capping protein subunit beta
- DYnein Light chain
Sequence:
MVDRKAVIKNADMSDDMQQDAIDCATQALEKYNIEKDIAAYIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG
Protein: E3 ubiquitin-protein ligase RNF6 (EC 2.3.2.27) (Q9Y252)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase mediating 'Lys-48'-linked polyubiquitination of LIMK1 and its subsequent targeting to the proteasome for degradation. Negatively regulates axonal outgrowth through regulation of the LIMK1 turnover. Mediates 'Lys-6' and 'Lys-27'-linked polyubiquitination of AR/androgen receptor thereby modulating its transcriptional activity. May also bind DNA and function as a transcriptional regulator.
Subcellular location: Nucleus {ECO:0000269|PubMed:19345326}. Cytoplasm {ECO:0000269|PubMed:19345326}. Cell projection, axon {ECO:0000250|UniProtKB:Q9DBU5}. Nucleus, PML body {ECO:0000250|UniProtKB:Q9DBU5}. Note=Localizes to the PML nuclear bodies in Sertoli cells. {ECO:0000250|UniProtKB:Q9DBU5}.
Interaction partners:
- Phospholipid-transporting ATPase IB
- Deleted in lung and esophageal cancer protein 1
- Transducin-like enhancer protein 3
Sequence:
MNQSRSRSDGGSEETLPQDHNHHENERRWQQERLHREEAYYQFINELNDEDYRLMRDHNLLGTPGEITSEELQQRLDGVKEQLASQPDLRDGTNYRDSEVPRESSHEDSLLEWLNTFRRTGNATRSGQNGNQTWRAVSRTNPNNGEFRFSLEIHVNHENRGFEIHGEDYTDIPLSDSNRDHTANRQQRSTSPVARRTRSQTSVNFNGSSSNIPRTRLASRGQNPAEGSFSTLGRLRNGIGGAAGIPRANASRTNFSSHTNQSGGSELRQREGQRFGAAHVWENGARSNVTVRNTNQRLEPIRLRSTSNSRSRSPIQRQSGTVYHNSQRESRPVQQTTRRSVRRRGRTRVFLEQDRERERRGTAYTPFSNSRLVSRITVEEGEESSRSSTAVRRHPTITLDLQVRRIRPGENRDRDSIANRTRSRVGLAENTVTIESNSGGFRRTISRLERSGIRTYVSTITVPLRRISENELVEPSSVALRSILRQIMTGFGELSSLMEADSESELQRNGQHLPDMHSELSNLGTDNNRSQHREGSSQDRQAQGDSTEMHGENETTQPHTRNSDSRGGRQLRNPNNLVETGTLPILRLAHFFLLNESDDDDRIRGLTKEQIDNLSTRHYEHNSIDSELGKICSVCISDYVTGNKLRQLPCMHEFHIHCIDRWLSENCTCPICRQPVLGSNIANNG