wanglab/gogpt-training-data huggingface dataset:
Protein: Protein disulfide isomerase MPD2 (EC 5.3.4.1) (Q99316)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Non essential disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May be involved in glycosylation, prolyl hydroxylation and triglyceride transfer. Able to fold proteins by being directly oxidized by ERO1.
Subcellular location: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein disulfide-isomerase MPD1
- Protein disulfide-isomerase
- Protein disulfide-isomerase EUG1
- ER-retained PMA1-suppressing protein 1
- Tryptophan synthase
- Endoplasmic oxidoreductin-1
- Endoplasmic reticulum chaperone BiP
Sequence:
MKLHGFLFSVLSTCVVILPALAYSEAVTMVKSIEQYFDICNRNDSYTMIKYYTSWCQHCKTLAPVYEELGELYAKKANKDDTPINFLEVNCEFFGPTLCTDLPGFPIIELVKPRTKPLVLPKLDWSSMKFHERLWQRIKTWFNNPKYQLDTSRVVRFEGSRNLKSLSNFIDTVRSKDTEERFIEHIFDDSRNCNEELRSQQLLCKAGKEYYSDTLSKLYGDVNGLEKERRRLEALIKQNGDDLSKEVKEKLKIIRLQLSLLSHIEDQLEDTSSHDEL
Protein: receptor protein serine/threonine kinase (EC 2.7.11.30) (Q569A5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MVKQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDYLKSTTLDAKSMLKLAYSSVSGLCHLHTEIFSTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVKFISDTNEVDIPPNTRVGTKRYMPPEVLDESLNRTHFQSYIMADMYSFGLILWEIARRCVSGGIVEEYQLPYHDLVPSDPSYEDMREIVCMKKLRPSFPNRWSSDECLRQMGKLMTECWAHNPASRLTALRVKKTLAKMSESQDIKL
Protein: Pyruvate kinase PKM (EC 2.7.1.40) (Cytosolic thyroid hormone-binding protein) (CTHBP) (Opa-interacting protein 3) (OIP-3) (Pyruvate kinase 2/3) (Pyruvate kinase muscle isozyme) (Threonine-protein kinase PKM2) (EC 2.7.11.1) (Thyroid hormone-binding protein 1) (THBP1) (Tumor M2-PK) (Tyrosine-protein kinase PKM2) (EC 2.7.10.2) (p58) (P14618)
Organism: Homo sapiens (Human)
Function: Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.
Subcellular location: [Isoform M2]: Cytoplasm {ECO:0000269|PubMed:25263439, ECO:0000269|PubMed:26787900, ECO:0000269|PubMed:27573352, ECO:0000269|PubMed:32268273}. Nucleus {ECO:0000269|PubMed:17308100, ECO:0000269|PubMed:18191611, ECO:0000269|PubMed:22056988, ECO:0000269|PubMed:22901803, ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900, ECO:0000269|PubMed:27573352, ECO:0000269|PubMed:32268273}. Note=Translocates to the nucleus in response to various signals, such as EGF receptor activation or apoptotic stimuli (PubMed:17308100, PubMed:22056988, PubMed:24120661). Nuclear translocation is promoted by acetylation by EP300 (PubMed:24120661). Deacetylation by SIRT6 promotes its nuclear export in a process dependent of XPO4, thereby suppressing its ability to activate transcription and promote tumorigenesis (PubMed:26787900). {ECO:0000269|PubMed:17308100, ECO:0000269|PubMed:22056988, ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900}.; SUBCELLULAR LOCATION: [Isoform M1]: Cytoplasm {ECO:0000305}.
Interaction partners:
- L-lactate dehydrogenase A chain
- Alpha-enolase
- Catenin beta-1
- Hypoxia-inducible factor 1-alpha
- Gamma-enolase
- Beta-enolase
- Glucose-6-phosphate isomerase
- L-lactate dehydrogenase A-like 6A
- Fructose-bisphosphate aldolase A
- L-lactate dehydrogenase C chain
Sequence:
MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEASFKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
Protein: Eukaryotic peptide chain release factor GTP-binding subunit ERF3B (Eukaryotic peptide chain release factor subunit 3b) (eRF3b) (EC 3.6.5.-) (G1 to S phase transition protein 2 homolog) (Q8IYD1)
Organism: Homo sapiens (Human)
Function: Involved in translation termination in response to the termination codons UAA, UAG and UGA. May play a role as a potent stimulator of the release factor activity of ETF1. Exhibits GTPase activity, which is ribosome- and ETF1-dependent. May play a role in cell cycle progression. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Eukaryotic peptide chain release factor subunit 1
- Serine/threonine-protein kinase SMG1
- Polyadenylate-binding protein 1
- Eukaryotic peptide chain release factor GTP-binding subunit ERF3A
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
- Regulator of nonsense transcripts 1
- Bifunctional glutamate/proline--tRNA ligase
- GTP-binding protein 4
- Polyadenylate-binding protein-interacting protein 1
Sequence:
MDSGSSSSDSAPDCWDQVDMESPGSAPSGDGVSSAVAEAQREPLSSAFSRKLNVNAKPFVPNVHAAEFVPSFLRGPTQPPTLPAGSGSNDETCTGAGYPQGKRMGRGAPVEPSREEPLVSLEGSNSAVTMELSEPVVENGEVEMALEESWEHSKEVSEAEPGGGSSGDSGPPEESGQEMMEEKEEIRKSKSVIVPSGAPKKEHVNVVFIGHVDAGKSTIGGQIMFLTGMVDKRTLEKYEREAKEKNRETWYLSWALDTNQEERDKGKTVEVGRAYFETERKHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFETGFEKGGQTREHAMLAKTAGVKHLIVLINKMDDPTVNWSIERYEECKEKLVPFLKKVGFSPKKDIHFMPCSGLTGANIKEQSDFCPWYTGLPFIPYLDNLPNFNRSIDGPIRLPIVDKYKDMGTVVLGKLESGSIFKGQQLVMMPNKHNVEVLGILSDDTETDFVAPGENLKIRLKGIEEEEILPGFILCDPSNLCHSGRTFDVQIVIIEHKSIICPGYNAVLHIHTCIEEVEITALISLVDKKSGEKSKTRPRFVKQDQVCIARLRTAGTICLETFKDFPQMGRFTLRDEGKTIAIGKVLKLVPEKD
Protein: Potassium channel subfamily K member 2 (Outward rectifying potassium channel protein TREK-1) (TREK-1 K(+) channel subunit) (Two pore domain potassium channel TREK1) (Two pore potassium channel TPKC1) (K2P2.1) (O95069)
Organism: Homo sapiens (Human)
Function: Ion channel that contributes to passive transmembrane potassium transport. Reversibly converts between a voltage-insensitive potassium leak channel and a voltage-dependent outward rectifying potassium channel in a phosphorylation-dependent manner. In astrocytes, forms mostly heterodimeric potassium channels with KCNK1, with only a minor proportion of functional channels containing homodimeric KCNK2. In astrocytes, the heterodimer formed by KCNK1 and KCNK2 is required for rapid glutamate release in response to activation of G-protein coupled receptors, such as F2R and CNR1 (By similarity).
Subcellular location: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:10784345}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000269|PubMed:23169818}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 4]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q920B6}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000250|UniProtKB:Q920B6}. Cell projection, dendrite {ECO:0000250|UniProtKB:P97438}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P97438}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q920B6}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes at the Ranvier nodes of myelinated afferent nerves. {ECO:0000250|UniProtKB:Q920B6}.
Interaction partners:
- Potassium channel subfamily K member 1
- Potassium channel subfamily K member 10
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Keratin, type II cytoskeletal 2 oral
- Potassium channel subfamily K member 4
- Popeye domain-containing protein 2
- Popeye domain-containing protein 1
- Piezo-type mechanosensitive ion channel component 1
Sequence:
MLPSASRERPGYRAGVAAPDLLDPKSAAQNSKPRLSFSTKPTVLASRVESDTTINVMKWKTVSTIFLVVVLYLIIGATVFKALEQPHEISQRTTIVIQKQTFISQHSCVNSTELDELIQQIVAAINAGIIPLGNTSNQISHWDLGSSFFFAGTVITTIGFGNISPRTEGGKIFCIIYALLGIPLFGFLLAGVGDQLGTIFGKGIAKVEDTFIKWNVSQTKIRIISTIIFILFGCVLFVALPAIIFKHIEGWSALDAIYFVVITLTTIGFGDYVAGGSDIEYLDFYKPVVWFWILVGLAYFAAVLSMIGDWLRVISKKTKEEVGEFRAHAAEWTANVTAEFKETRRRLSVEIYDKFQRATSIKRKLSAELAGNHNQELTPCRRTLSVNHLTSERDVLPPLLKTESIYLNGLTPHCAGEEIAVIENIK
Protein: Ninja-family protein MODD (Protein MEDIATOR OF OSBZIP46 DEACTIVATION AND DEGRADATION) (Q10Q07)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Acts as negative regulator of abscisic acid (ABA) signaling and drought tolerance. Mediates deactivation and degradation of BZIP46, a positive regulator of ABA signaling and drought stress tolerance. Represses BZIP46 activity via interaction with the TPR3-HDAC1 corepressor complex and down-regulation of the histone acetylation level at BZIP46 target genes. Promotes BZIP46 degradation via interaction with the U-box type ubiquitin E3 ligase PUB70.
Subcellular location: Nucleus {ECO:0000269|PubMed:27468891}.
Interaction partners:
- bZIP transcription factor 46
- U-box domain-containing protein 70
Sequence:
MEGFSRDLLCGIGKGGDGPRGEVRPRVDMEAEEVELNLGLSLGGRFGLDRRGEKLARSSSVAAILAAPTEPSAPPSGLFRTSSLPTVAAAEAAKKQGVDELNCRRPSGGAEAEPAAARLPASGSPSSGSSDGEGRRLEVNMTDTLMRTSSLPAGIEDEWRKRKEAQSLKRLEVKRKRIERRNSLTSNISKEAVGQILEEMNAGAEKVESCDDVATGNKKTGGNVNHSSDRNRCTGLPPVHRATYTQQRGSLSGIPTKHIPAMKGSADAEEHNVPSAATEHRNGAAIATPPFSALAVRAVALASRGEQLRATGRVAARAKSMGDVERIMMQEMPCVCTKGLPNGKRVEGFLYKYRKGEEVRIVCVCHGSFLTPAEFVKHAGGGDVANPLRHIVVNPIPPSLY
Protein: Phosphodiesterase (EC 3.1.4.-) (A0A8I5Y879)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDEYVTIRKKHLQRPIFRLRCLVKQLEKGDVNVVDLKKNIEYAASVLEAVYIDETRRLLDTEDELSDIQTDSVPSEVRDWLASTFTRKMGMTKKKPEEKPKFRSIVHAVQAGIFVERMYRKNYHMVGLTYPAAVIVTLKEVDKWSFDVFALNEASGEHSLKFMIYELFTRYDLINRFKIPVSCLIAFAEALEVGYSKHKNPYHNLVHAADVTQTVHYIMLHTGIMHWLTELEILAMVFAAAVHDYEHTGTTNNFHIQTRSDVAILYNDRSVLENHHVSAAYRLMQEEEMNILVNLSKDDWRDLRNLVIEMVLATDMSGHFQQIKNIRSSLQQPEGIDRAKTMSLILHAADISHPAKTWKLHYRWTMALMEEFFLQGDKEAELGLPFSPLCDRKSTMVAQSQIGFIDFIVEPTFSLLTDSTEKIVIPLIEEASKPESSNYGASSSSTMIGFHVADALRRSNTKGCMSDGTYAPDYSLSAVDLKSFKNNLVDIIQQNKERWKELAAQGCC
Protein: Probable U2 small nuclear ribonucleoprotein B'' (U2 snRNP B'') (Q7LL14)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in pre-mRNA splicing. This protein is associated with snRNP U2. It binds stem loop IV of U2 snRNA (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Pre-mRNA-splicing factor cwf10
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein-associated protein B
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-splicing factor prp1
- Pre-mRNA-splicing factor cdc5
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein F
- Pre-mRNA-processing factor 19
Sequence:
MNQNTLYVNNLNDKINKNDLRTALYMLFSTYGTVVDIVALKTPKMRGQAHVVFFDPSAAAIAMKALKNFIFFGKEMKIQYAHSKSKIIERIVAENDSRGPLKRLRDEADLE
Protein: Glutamate receptor 2 (GluR-2) (AMPA-selective glutamate receptor 2) (GluR-B) (GluR-K2) (Glutamate receptor ionotropic, AMPA 2) (P42262)
Organism: Homo sapiens (Human)
Function: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system. It plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. Through complex formation with NSG1, GRIP1 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:23739980, ECO:0000269|PubMed:31300657}; Multi-pass membrane protein {ECO:0000269|PubMed:23739980}. Postsynaptic cell membrane {ECO:0000269|PubMed:23739980}; Multi-pass membrane protein {ECO:0000269|PubMed:23739980}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P23819}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23819}. Note=Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression (By similarity). Displays a somatodendritic localization and is excluded from axons in neurons (By similarity). {ECO:0000250|UniProtKB:P19491, ECO:0000250|UniProtKB:P23819}.
Interaction partners:
- PRKCA-binding protein
- Glutamate receptor 4
- Glutamate receptor 1
- Glutamate receptor-interacting protein 1
- Glutamate receptor 3
- Voltage-dependent calcium channel gamma-2 subunit
- Voltage-dependent calcium channel gamma-8 subunit
- Protein cornichon homolog 2
- Cadherin-2
- Protein cornichon homolog 3
Sequence:
MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDEMYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTTTIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLRNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKVAKNAQNINPSSSQNSQNFATYKEGYNVYGIESVKI
Protein: Foxo1-corepressor (FCoR) (EC 2.3.1.-) (Foxo1 CoRepressor) (P0DJI6)
Organism: Mus musculus (Mouse)
Function: Regulator of adipocytes that acts by repressing FOXO1 transcriptional activity. Acts by promoting acetylation of FOXO1, both by preventing the interaction between FOXO1 and SIRT1 deacetylase, and by mediating acetyltransferase activity in vitro. Regulates insulin sensitivity and energy metabolism.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:22510882}. Nucleus {ECO:0000269|PubMed:22510882}. Note=Imported into the nucleus following phosphorylation at Thr-93 upon treatment of cells with forskolin. Probably shuttles between the nucleus and the cytoplasm.
Interaction partners:
Sequence:
MGGPTRRHQEEGSAECLGGPSTRAAPGPGLRDFHFTTAGPSKADRLGDAAQIHRERMRPVQCGDGSGERVFLQSPGSIGTLYIRLDLNSQRSTCCCLLNAGTKGMC
Protein: Cold tolerance protein 1 (P25616)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Protein required for cold tolerance. Plays a role in the regulation of phosphate uptake.
Interaction partners:
- Protein PET18
- Putative uncharacterized protein YCL068C
- GTP-binding protein GTR2
Sequence:
MKTIIISDFDETITRVDTICTIAKLPYLLNPRLKPEWGHFTKTYMDGYHKYKYNGTRSLPLLSSGVPTIISQSNFNKLFADELKYQNHNRVVELNSVNEITKQQIFKSISLDQMKTFARDQNHEDCLLRDGFKTFCSSVVKNFESDFYVLSINWSKEFIHEVIGDRRLKNSHIFCNDLKKVSDKCSQSYNGEFDCRLLTGSDKVKILGEILDKIDSGCNKEGNSCSYWYIGDSETDLLSILHPSTNGVLLINPQENPSKFIKITEKIIGIPKDKISSFEADNGPAWLQFCEKEGGKGAYLVKSWDSLKDLIMQVTKM
Protein: Arylalkylamine N-acetyltransferase 1 (EC 2.3.1.87) (Dopamine N-acetyltransferase) (Q94521)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes N-acetylation of tryptamine, tyramine, dopamine, serotonin and octopamine. In astrocytes, regulates sleep homeostasis by limiting the accumulation of serotonin and dopamine in the brain upon sleep deprivation. Is not essential for sclerotization.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32955431}. Nucleus {ECO:0000269|PubMed:32955431}. Note=In astrocytes, is primarily cytoplasmic, but in neurons is also nuclear. {ECO:0000269|PubMed:32955431}.
Interaction partners:
- Aromatic-L-amino-acid decarboxylase
- monoamine oxidase
- Beta-alanyl-bioamine nonribosomal peptide synthetase ebony
- MIP05841p)
Sequence:
MEVQKLPDQSLISSMMLDSRCGLNDLYPIARLTQKMEDALTVSGKPAACPVDQDCPYTIELIQPEDGEAVIAMLKTFFFKDEPLNTFLDLGECKELEKYSLKPLPDNCSYKAVNKKGEIIGVFLNGLMRRPSPDDVPEKAADSCEHPKFKKILSLMDHVEEQFNIFDVYPDEELILDGKILSVDTNYRGLGIAGRLTERAYEYMRENGINVYHVLCSSHYSARVMEKLGFHEVFRMQFADYKPQGEVVFKPAAPHVGIQVMAKEVGPAKAAQTKL
Protein: Peptide hydrolase (EC 3.4.-.-) (Q6FSV1)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MKFSTIAVTAALVAYSNASVLPFYGEQQAFDLSALKETKETDWDSIISGVKDALSQGHSEQDAAEVYEDDDEDVSPCKKSFWSFLWKPHVPYLLKPIVESDKLQDKIELDDLNKTAHDLLKIAKKSKKKFGHPTRVIGSPGHGKTIDYILDAFDDMKDYYDVSVQEFDALAGKIRSYNLTDAKTGKTFKNTTAFALSPPVKPFVGRVIEIPNLGCHEKDFAAVHRKGSKHKHDIALIERGECPFGVKSDLAGKYGFHAVVIYDNEPLSLDGLKGTLGAPTNHTVSTIGVTYVTGKEIIAKLAFDPDYSLYFAMDSYVGKIKTKNIIADTKHGDENNIVGLGAHSDSVEEGPGLNDDGSGTISLLTVAKQLTHFKINNKVRFAWWAAEEEGLLGSNYYANSLSKEENLKLRVFMDYDMMASPNYEYEVYDANNTVNPPGSQELRDLYINYYKDQGLNYTLIPFDGRSDYVGFIENGIPAGGIATGAEKKNVFNGGVLDKCYHQLCDDISNLAWDAFLVNTKLIAHSVATYANSFEGFPERIGSNKTISALQAPSFPYRGSNLII
Protein: RAB11 family interacting protein 2 (A0A8I6AF99)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}. Recycling endosome {ECO:0000256|ARBA:ARBA00004172}.
Interaction partners:
Sequence:
MMLSEQAQKWFPTHVQVTVLQAKDLKPKGKSGTNDTYTIIQLGKEKYSTSVAEKTLEPVWKEEASFELPGLLMQGNPEKYILFLIVMHRSLVGLDKFLGQVAINLNDIFEDKQRRKTEWFRLESKQGKRIKNRGEIKVNIQFMRNNMTASMFDLSMKDKTRSPFAKLKDKMKGRKSDGVFSDTSSAIVPSTHMPDANPEFSSGEMQMKSKPKKPFLLGPQRLSSAHSMSDLTGSHLSSEKLKSSTVGPTHLLSHQINSFGVVPESGSLKSPHRRTLSFDTSKLNQPGSIVDEGEHCFGRQSDPFTNVTASLPQKFATLPRKKNPFEESSEPWDSSTNLFSKPIEVRKESKREKREKVSLFERVTGKRDSRRSDKLNNGGSDSPCDLKSPSAFNENRQDYFEYESTNPFTAKFRASTIMPSSSFHMNPTSSDDLRKIPDSNPFDATAGYRSLTYEEVLQELVKHKELLRRKDTHIRELEDYIDNLLVRVMEETPSILRVPYEPSRKAGKFTNS
Protein: Omega-conotoxin CVIA (P58917)
Organism: Conus catus (Cat cone)
Function: Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels. This toxin blocks N-type calcium channels (Cav2.2/CACNA1B). Shows a weak voltage-dependent reversibility. It is noteworthy that ancillary subunits beta modulate recovery from this toxin block. Cav2.2/CACNA1B expressed with the ancillary subunit CACNB2a (isoform 2a) shows a low recovery from this toxin block, whereas Cav2.2/CACNA1B expressed with CACNB3 does not exhibit recovery at all.
Subcellular location: Secreted {ECO:0000269|PubMed:10938268}.
Interaction partners:
Sequence:
MKLTCVVIVAMLLLTACQLITANDSRGTQKHRALRSDTKLSMSTRCKSTGASCRRTSYDCCTGSCRSGRCG
Protein: Iron-containing hydrogenase, putative (Q389R3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Probable cytosolic iron-sulfur protein assembly protein CIAO1 homolog
- Cytochrome oxidase assembly protein, putative
- Adrenodoxin, putative
- Electron transfer protein, putative
Sequence:
MSANNFSASLMLAGMDYIAPSEACILPTKLQGGTSDDSVKRHGAGNEAVKITLQDCLACSGCVTTAETILITSQSREELLKDRALDPTRPFFVTISDQSAASIAAFLKTDVQRAFHIVSGFFRAVLNARYVSDLHWALRISVEKTAEEYCRRVRCERERLPLIVSACPGWVCYCEKQGAAILPLLCPVMSPQGIAGCYSKTLIPQMCHVSVQPCFDRKLEAARDGSSVSGERYTDFVLSTQELLDWMLEVDPSLPWQAPLDSDLEPLPILPPEEPKRSFAATMEGSGGYHRYAMHRAACELHGLELAPRDIHYEMKRNANHHLTTSPSNPGEVFCVAYGFQQIQNTVRGIKRKLASVASYTFIELMACPEGCLNGGGQARNGTTQSHVETTAAAKSAFISYISGSQPTMEVRGGMEGTSVASNRDVGDGPPPFSLAAFAEVEKQVGSSLWSCTFTDRQREFEATLNTGGVHSLKW
Protein: Small kinetochore-associated protein (SKAP) (Kinetochore-localized astrin-binding protein) (Kinastrin) (Kinetochore-localized astrin/SPAG5-binding protein) (TRAF4-associated factor 1) (Q9Y448)
Organism: Homo sapiens (Human)
Function: Essential component of the mitotic spindle required for faithful chromosome segregation and progression into anaphase. Promotes the metaphase-to-anaphase transition and is required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture. The astrin (SPAG5)-kinastrin (SKAP) complex promotes stable microtubule-kinetochore attachments. Required for kinetochore oscillations and dynamics of microtubule plus-ends during live cell mitosis, possibly by forming a link between spindle microtubule plus-ends and mitotic chromosomes to achieve faithful cell division. May be involved in UV-induced apoptosis via its interaction with PRPF19; however, these results need additional evidences.
Subcellular location: Nucleus {ECO:0000269|PubMed:24718257}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19667759, ECO:0000269|PubMed:21402792, ECO:0000269|PubMed:22110139, ECO:0000269|PubMed:23035123}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:19667759}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:29180244}. Note=Colocalizes with microtubules around centrosomes in prophase and with the mitotic spindle at prometaphase and metaphase. From late prometaphase to anaphase, is highly concentrated on kinetochores. Located at the kinetochore-microtubule interface. The astrin (SPAG5)-kinastrin (SKAP) complex localizes to the microtubule plus ends (PubMed:23035123). {ECO:0000269|PubMed:19667759, ECO:0000269|PubMed:21402792, ECO:0000269|PubMed:22110139, ECO:0000269|PubMed:23035123}.
Interaction partners:
- Sperm-associated antigen 5
- Centromere-associated protein E
- Kinetochore protein Nuf2
- Charged multivesicular body protein 1b
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Cell division cycle-associated protein 3
- Pre-mRNA-processing factor 19
- SKA complex subunit 1
- Kinesin-like protein KIF20A
- STAM-binding protein
Sequence:
MAAPEAPPLDRVFRTTWLSTECDSHPLPPSYRKFLFETQAADLAGGTTVAAGNLLNESEKDCGQDRRAPGVQPCRLVTMTSVVKTVYSLQPPSALSGGQPADTQTRATSKSLLPVRSKEVDVSKQLHSGGPENDVTKITKLRRENGQMKATDTATRRNVRKGYKPLSKQKSEEELKDKNQLLEAVNKQLHQKLTETQGELKDLTQKVELLEKFRDNCLAILESKGLDPALGSETLASRQESTTDHMDSMLLLETLQEELKLFNETAKKQMEELQALKVKLEMKEERVRFLEQQTLCNNQVNDLTTALKEMEQLLEM
Protein: Nudix hydrolase 13, mitochondrial (AtNUDT13) (EC 3.6.1.-) (Q52K88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates the hydrolysis of some nucleoside diphosphate derivatives. Can use diadenosine 5',5'''-P(1)P(6) hexaphosphate (Ap(6)A), diadenosine 5',5'''-P(1)P(5) pentaphosphate (Ap(5)A) and adenosine tetraphosphate (p(4)A) as substrates, but not diadenosine 5',5'''-P(1)P(4) tetraphosphate (Ap(4)A), diadenosine 5',5'''-P(1)P(3) triphosphate (Ap(3)A), deoxyribonucleoside triphosphates, ribonucleoside triphosphates, diphosphoinositol pentakisphosphate (PP-InsP(5)) and 5-phospho-alpha-D-ribosyl diphosphate (PRPP).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:17824959}.
Interaction partners:
- Nudix hydrolase 15, mitochondrial
- Nudix hydrolase 11
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic
- Nudix hydrolase 1
- Nudix hydrolase 14, chloroplastic
- mRNA-decapping enzyme-like protein
- Nudix hydrolase 19, chloroplastic
- Nudix hydrolase 8
- Small polypeptide DEVIL 19
- D-aminoacyl-tRNA deacylase
Sequence:
MSNLSARTGRDHQRYDNNFRLVSGCIPYRLVKDEEEDSTSVDFENKLQVLMISSPNRHDLVFPKGGWEDDETVLEAASREAMEEAGVKGILREDPLGVWEFRSKSSSVEADCCLGGGCKGYMFALEVKEELAIWPEQDDRERRWLNVKEALELCRYEWMQSALEEFLRVMAEEGSTKEDSLAISSISNRGERQIDPRYCFVV