wanglab/gogpt-training-data huggingface dataset:
Protein: Serpin B8 (Cytoplasmic antiproteinase 2) (CAP-2) (CAP2) (Peptidase inhibitor 8) (PI-8) (P50452)
Organism: Homo sapiens (Human)
Function: Has an important role in epithelial desmosome-mediated cell-cell adhesion.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MDDLCEANGTFAISLFKILGEEDNSRNVFFSPMSISSALAMVFMGAKGSTAAQMSQALCLYKDGDIHRGFQSLLSEVNRTGTQYLLRTANRLFGEKTCDFLPDFKEYCQKFYQAELEELSFAEDTEECRKHINDWVAEKTEGKISEVLDAGTVDPLTKLVLVNAIYFKGKWNEQFDRKYTRGMLFKTNEEKKTVQMMFKEAKFKMGYADEVHTQVLELPYVEEELSMVILLPDDNTDLAVVEKALTYEKFKAWTNSEKLTKSKVQVFLPRLKLEESYDLEPFLRRLGMIDAFDEAKADFSGMSTEKNVPLSKVAHKCFVEVNEEGTEAAAATAVVRNSRCSRMEPRFCADHPFLFFIRHHKTNCILFCGRFSSP
Protein: Apolipoprotein C-II (Apo-CII) (ApoC-II) (Apolipoprotein C2) [Cleaved into: Proapolipoprotein C-II (ProapoC-II)] (G3V8D4)
Organism: Rattus norvegicus (Rat)
Function: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P02655}.
Interaction partners:
- Apolipoprotein C-III
- Apolipoprotein C-I
- Lipoprotein lipase
- Apolipoprotein E
- Apolipoprotein A-II
- Apolipoprotein B-100
- Apolipoprotein A-V
- Apolipoprotein C-I-like.
- Apolipoprotein A-IV
- Apolipoprotein C-IV
Sequence:
MGSRFFLALFLALLVLGNEVQGTEEDDPGSSALLDTVQEHLFSYWNSAKAAAGELYQKTYLTSVDEKLRDMYSKSSAAMTTYAGIFTDQLLTLLKGE
Protein: ADAM metallopeptidase domain 22 (A0A8I6GKI4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MQAVAAAFFWLLCVLGTYPLARCGRAGDASLRELERGDGNRFLERQSTVPLRLIYRLGGEDETQHEQLNTRVRGDPGGRQPTHVDKASFRVDAFGTSFILDVLLNHELLSSGYVERHIEHGGKVVENKGGEHCYYQGQIRGNPASFVALSTCHGLHGMFYDGNHTYLIEPEENEMSQESQFHSVYKSRLLEFPLDDLPSEFQRINITAPQFTLKPRLKRRKRQLLRFPRNVEEETKYIELMIVNDHLMFKKHRLSVVYTNTYAKSVVNMADVIYKDQLKTRIVLVAMETWAADNKFAISENPLVTLREFMKYRRDFIKEKADAVHLFSGSQFESSRSGAAYIGGICSLLRGGGVNEFGKTDLMAVTLAQSLAHNIGIISDKRKLASGECKCEDTWSGCIMGDTGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKPSKLLDPPECGNGFIETGEECDCGTPAECALEGAECCKKCTLTQDSQCSDGLCCKKCKFQPLGTVCREAVNDCDIREICSGNSSQCAPNVHKMDGYSCDGTQGICFGGRCKTRDRQCKYIWGQKVTASDRYCYEKLNIEGTEKGNCGKDKDTWTQCNKRDVLCGFLLCTNIGNIPRLGELDGEITSTLVVQQGRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPMASFNFSTCLSNKAGTVCSGNGVCSNELKCVCNRHWTGADCGTHFPHNDDAKTGITLSGNGVAGTNIIIGIIAGTILVLALILGITAWGYKNYREQRSNGLSHSWSERIPDTKHISDICENGRPRSNSWQGNVGGNKKKIRGKRFRPRSNSTEREPQAPEPGHSLAQTSPGISPGGSDSPQTGSLDHRTLSPAKSPSSSTGSIASSRKYPYPMPPLPDEEKTVNRQSARLWETSI
Protein: Type VI secretion system spike protein VgrG3 (Muramidase Vgrg3C) (EC 3.2.1.-) (Q9KN42)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Function: Part of the type VI secretion system specialized secretion system, which delivers several virulence factors in both prokaryotic and eukaryotic cells during infection. Forms the spike at the tip of the elongating tube formed by haemolysin co-regulated protein Hcp. Allows the delivery of the TseL antibacterial toxin to target cells where it exerts its toxicity. Additionally, acts directly as an effector and targets the cell wall peptidoglycan layer of prey cells for degradation via its C-terminus. Toxicity is counteracted by a cognate immunity protein TsiV3.
Subcellular location: Secreted {ECO:0000269|PubMed:23341465}.
Interaction partners:
- Antitoxin protein TsiV3
- Type VI secretion system baseplate subunit TssG
- Type VI secretion system contractile sheath small subunit
- IraD/Gp25-like domain-containing protein
- Type IV / VI secretion system DotU domain-containing protein
- Type VI secretion system baseplate subunit TssF
- ImpA N-terminal domain-containing protein
- Type VI secretion system contractile sheath large subunit
- ClpB protein
- Hcp protein
Sequence:
MARLQFQLKVDGLEDESLVVRGFEGQESLSDSVWRCEPCYGFRYQVDLASALSNLTAEQFVDQTAHLTILRDGQVVQQINGIVRQLSKGDTGHRHTFYSLTLVPALERLSLRSNSRIFQQQSVPEIISILLQEMGIEDYAFALKRECAQREFCVQYRETDLQFLHRIAAEEGLVYSHLHEAQKHTLLFTDSSDSQPKLAKPVPYNALAGGEINLPYVVDLQFKTTAQVSHTELKDYSFKKPAYGFTQRTQGKDIAYQQPNYEHFDAPGRYKDDANGKAFSQIRLEYLRRDALLADAKSDEPLLLAGVRFDLQDHLDHAMNRDWLVVQANHQGTQPQALQEEGGSGATTYSNQLKLIPAHITWRARPCAKPQVDGPMIATVVGPQGEEIYCDNFGRVKVHFPWDRYSSSNEKSSCWVRVAQEWAGSQYGSMAIPRVGHEVIVSFLNGDPDQPIITGRTYHATNTAPYALPDHKTKTVLRTETHQGQGYNELSFEDQAGSEQILLHAQKDWDALIEHDHTEVIRHDQHLTVDNDRFTRIQRNQHLTVEGEVRSKIALDSSHEVGASLQHKVGQRIAVEAGKEISLKSGAKIVVEAGAELTLKAGGSFVKVDAGGVHLVGPAINLNAGGSAGSGSAYGGQLAAAPRMLAQAKPVAELVQPDIAASMQSGAARVIDVASLPTMMPSSANNTANDEPVAEEKTPERILKSDLLKPSDELEKLAKRQASAYRQGNHSDEVKLLQEALIKLGFDLGKAGADGDFGSKTKTAIEQFQKSYQPSHQTHPSYSIGAVDGIVGKGTLLALDEALMDGWVYENNIYQIWPLGKTSEKYESAGRGPGVISTGNGDYGGASYGCYQMSSNLGVVQKYIQSSKFKEFFSGLNPATKEFNVVWQDIASRYPQEFREEQHQFIKRTHYDIQIGHLRGKGLLFEHNRAAVHDLIWSTSVQFGGRTNLIFNALNGQNMESMTDKDIIILVQDYKLVNTERLFKSSPSWWSDLKKRAVSEKKALLELEIDGLEVDIK
Protein: Keratin, type II cytoskeletal 6A (Cytokeratin-6A) (CK-6A) (Cytokeratin-6D) (CK-6D) (Keratin-6A) (K6A) (Type-II keratin Kb6) (allergen Hom s 5) (P02538)
Organism: Homo sapiens (Human)
Function: Epidermis-specific type I keratin involved in wound healing. Involved in the activation of follicular keratinocytes after wounding, while it does not play a major role in keratinocyte proliferation or migration. Participates in the regulation of epithelial migration by inhibiting the activity of SRC during wound repair.
Interaction partners:
- Keratin, type I cytoskeletal 16
- Keratin, type II cytoskeletal 5
- Keratin, type I cytoskeletal 13
- Keratin, type II cytoskeletal 6B
- Cornifin-B
- Keratin, type I cytoskeletal 17
- Keratin, type I cytoskeletal 15
- Keratin, type I cytoskeletal 14
- Keratin, type I cuticular Ha1
- Cornifin-A
Sequence:
MASTSTTIRSHSSSRRGFSANSARLPGVSRSGFSSVSVSRSRGSGGLGGACGGAGFGSRSLYGLGGSKRISIGGGSCAISGGYGSRAGGSYGFGGAGSGFGFGGGAGIGFGLGGGAGLAGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPTIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQGTKTVRQNLEPLFEQYINNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGEGVGQVNISVVQSTVSSGYGGASGVGSGLGLGGGSSYSYGSGLGVGGGFSSSSGRAIGGGLSSVGGGSSTIKYTTTSSSSRKSYKH
Protein: Ap3d1 protein (Q4FZT4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
AQFVFTIQSIVMAQKLKGTLSFIAKDDEGATHEKLDFRLHFSCSSYLITTPCYSDAFAKLLESGDLSMNSIKVDGISISFQNLLAKICFYHHFSVVERVDSCASMYSRSIQGHHVCLLVKKGESSVSVDGKCSDATLLSSLLEEMKTTLSQC
Protein: Diphthamide biosynthesis protein 4 (Q9UUG3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P47138}. Nucleus {ECO:0000250|UniProtKB:P47138}.
Interaction partners:
- 2-
- Diphthine--ammonia ligase
- Diphthine methyl ester synthase
- Diphthamide biosynthesis protein 3
- 2-
- Diphthine methyltransferase
- Elongator complex protein 3
Sequence:
MNHYSVLNLKDGKTYTDDEIKEAYRKALLLFHPDKCKEKPSVVYTIDQVKEAYQVLSSEKDRQQYQIKQEEESSHYYSIVDLSEFEELDNGSYYYPCRCGDLGGYVVTEDDLENNRSVVPCMGCSLTIQVDYEIAESDS
Protein: Threonylcarbamoyl-AMP synthase (Q9SGI3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAVAKLHGGGMAAMRLLLLPSPMTHRRPSTLPSTASLSPRRYIVALAAKRSPKRLKYSTPRFTKEGELVYIEVDPCGVDSWKLQPVIDLLKQGAVGVIPTDTVYAIACDCKNHSAVERLRRIKKIESSKPLSILCRSLRDIDTFTMGFPRGDGHGHANVFRAVKQCLPGPYTFILTASKELPKQCVGYGTTSVKYASRKNVGVRISDDALCQAILQQMDAPLICTSVKGPKENEWMIDPTAIGDIYGPEGLDFVVDGGIRVAEPSTIVDMTGPYPKVIREGKGPILPWMVVEDDESSLRQDLMASGT
Protein: Histamine-gated chloride channel subunit (A1KYB3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVFQIIILVICTICMKHYAKGEFQQSLAITDILPEDIKRYDKMRPPKKEGQPTIVYFHVTVMGLDSIDENSMTYVADVFFAQTWKDHRLRLPENMTQEYRLLEVDWLKNMWRPDSFFKNAKSVTFQTMTIPNHYMWLYKDKTILYMVKLTLKLSCIMNFAIYPHDTQECKLQVESLSHTTDDLIFQWDPTTPLVVDENIELPQVALIRNETADCTQVYSTGNFTCLEVVFTLKRRLVYYVFNTYIPTCMIVIMSWVSFWIKPEAAPARVTLGVTSLLTLSTQHAKSQSSLPPVSYLKAVDAFMSVCTVFVFMALMEYCLINIVLSDTPIPKPMAYPPKPVAGDGPKKEGEGAPPGGSNSTASKQQATMLPLADEKIEKIEKIFDEMTKNRRIVTTTRRVVRPPLDADGPWIPRQESRIILTPTIAPPPPPPQPAAPEPELPKPKLTPAQERLKRAIYIDRSSRVLFPALFASLNGIYWCVFYEYL
Protein: Rifin (Q8IIY5)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKIHYINILLFELPLNILIYNQRNHKSTTHHTLKIPITRLLCECELYAPSNYDNDPEMKEVMEIFDRQTSERFHEYDERMKTTRQKCKDKCDKEIQKIILKDKLEKELNEKFLTLQTDIQNDAIPTCVCEKSLADKVEKGCLRCGSILGAAMPEVGSIGGGLLYALNAWKPKALEAAIAAAKELAITEATNAGVKTVVSEINKLLAKFKQHEILFELKPIVNKSNFSCGSSLFQRAEELASKSCVAQPNGSYTSFCNTILNGEKTTFKPFAQAGANTYEKTLTTETPVLQARYTAAVKTAYGGYQTAIIASIVAIVVIVLIMVIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: U6 snRNA-associated Sm-like protein LSm8 (Q9W087)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365048}.
Interaction partners:
- U6 snRNA-associated Sm-like protein LSm4
- U6 snRNA-associated Sm-like protein LSm6
- U6 snRNA-associated Sm-like protein LSm7
- U6 snRNA-associated Sm-like protein LSm5
- U6 snRNA-associated Sm-like protein LSm2
- U6 snRNA-associated Sm-like protein LSm3
- Probable small nuclear ribonucleoprotein G
- U4/U6 small nuclear ribonucleoprotein Prp31
- Probable small nuclear ribonucleoprotein Sm D2
- Precursor RNA processing 3, isoform A
Sequence:
MSGLESYINHTVSIITADGRNFIGTLKGFDQTINIIIDECHERVFSTTSGIEQIVLGLHIIRGDNIAVIGLIDETIDSRLDLANIRGEPLGPVVH
Protein: NADP-dependent malic enzyme (NADP-ME) (EC 1.1.1.40) (Malic enzyme 1) (P06801)
Organism: Mus musculus (Mouse)
Function: Catalyzes the oxidative decarboxylation of (S)-malate in the presence of NADP(+) and divalent metal ions, and decarboxylation of oxaloacetate.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P48163}.
Interaction partners:
- Pyruvate carboxylase, mitochondrial
- Malate dehydrogenase, mitochondrial
- Malate dehydrogenase, cytoplasmic
- Fumarate hydratase, mitochondrial
- Pyruvate kinase PKM
- L-lactate dehydrogenase A chain
- Pyruvate kinase PKLR
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- L-lactate dehydrogenase B chain
Sequence:
MEPRAPRRRHTHQRGYLLTRDPHLNKDLAFTLEERQQLNIHGLLPPCIISQELQVLRIIKNFERLNSDFDRYLLLMDLQDRNEKLFYSVLMSDVEKFMPIVYTPTVGLACQQYSLAFRKPRGLFISIHDKGHIASVLNAWPEDVVKAIVVTDGERILGLGDLGCNGMGIPVGKLALYTACGGVNPQQCLPITLDVGTENEELLKDPLYIGLRHRRVRGPEYDAFLDEFMEAASSKYGMNCLIQFEDFANRNAFRLLNKYRNKYCTFNDDIQGTASVAVAGLLAALRITKNKLSDQTVLFQGAGEAALGIAHLVVMAMEKEGLSKENARKKIWLVDSKGLIVKGRASLTEEKEVFAHEHEEMKNLEAIVQKIKPTALIGVAAIGGAFTEQILKDMAAFNERPIIFALSNPTSKAECSAEQCYKVTKGRAIFASGSPFDPVTLPDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTAEVISQQVSDKHLQEGRLYPPLNTIRGVSLKIAVKIVQDAYKEKMATVYPEPQNKEEFVSSQMYSTNYDQILPDCYPWPAEVQKIQTKVNQ
Protein: Homeobox protein CUP9 (P41817)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable DNA-binding protein which plays a role in protecting yeast cells against copper toxicity. May regulate the expression of important copper homeostatic genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- E3 ubiquitin-protein ligase UBR1
- Peptide transporter PTR2
- Protein SOK1
- AP-1-like transcription factor YAP6
- Transcriptional regulator NRG1
Sequence:
MNYNCEIQNRNSKNVDNQVSLPPIQVLFNSIEKRSMPELAFSNIEYSHGNLRSSTEEQNYPAPVLLPQHHSIAYPAINSGGTSTTATPTASTVETSKTSSSAMDTQSQYGSSKKSKSASDDAKPCYKSAPIYEIINKEKDAGAQYNRPFSDFVESKSRRKQNSGRRSNLPKETVQILNTWLLNHLNNPYPTQQEKRELLIKTGLTKIQLSNWFINVRRRKIFSDYYTLVNSIPNDNANNTPVERVQNVSAYHNTLSATNNTMYDATSTCSTDYELSKRFAHAPVTRRKKLIDRLEELKKLSNPDMN
Protein: PWWP domain-containing protein 2B (Q6NUJ5)
Organism: Homo sapiens (Human)
Function: Chromatin-binding protein that acts as an adapter between distinct nucleosome components (H3K36me3 or H2A.Z) and chromatin-modifying complexes, contributing to the regulation of the levels of histone acetylation at actively transcribed genes. Competes with CHD4 and MBD3 for interaction with MTA1 to form a NuRD subcomplex, preventing the formation of full NuRD complex (containing CHD4 and MBD3), leading to recruitment of HDACs to gene promoters resulting in turn in the deacetylation of nearby H3K27 and H2A.Z. Plays a role in facilitating transcriptional elongation through regulation of histone acetylation (By similarity). Negatively regulates brown adipocyte thermogenesis by interacting with and stabilizing HDAC1 at the UCP1 gene promoter, thereby promoting histone deacetylation at the promoter leading to the repression of UCP1 expression (By similarity).
Interaction partners:
- Bromodomain-containing protein 4
Sequence:
MEPRAGCRLPVRVEQVVNGALVVTVSCGERSFAGILLDCTKKSGLFGLPPLAPLPQVDESPVNDSHGRAPEEGDAEVMQLGSSSPPPARGVQPPETTRPEPPPPLVPPLPAGSLPPYPPYFEGAPFPHPLWLRDTYKLWVPQPPPRTIKRTRRRLSRNRDPGRLILSTIRLRPRQVLCEKCKSTLSPPEASPGPPAAPRARRRLGSGPDRELRKPEEPENGEPTAAATARRSKRERREEDRAPAEQVPRSPVIKISYSTPQGKGEVVKIPSRVHGSLEPFRPQQAPQDDGSQDPEVLDRESRDRPSCAPSASIPKLKLTRPVPAGADLPPPKIRLKPHRLGDSEHEPVYRAELVGELNGYLRDSSPAPCADGPAGGLADLSSGSSGEDDDFKSCPQGPQGREGLAFLVSCPEGRADCASESACSSDSLDEARSSGSEGTPADTGDLSPGHGASAPSVSREARQTVPPLTVRLHTQSVSECITEDGRTVAVGDIVWGKIHGFPWWPARVLDISLGQKEDGEPSWREAKVSWFGSPTTSFLSISKLSPFSEFFKLRFNRKKKGMYRKAITEAANAARHVAPEIRELLTQFET
Protein: Sperm-associated antigen 1 (HSD-3.8) (Infertility-related sperm protein Spag-1) (Q07617)
Organism: Homo sapiens (Human)
Function: May play a role in the cytoplasmic assembly of the ciliary dynein arms (By similarity). May play a role in fertilization. Binds GTP and has GTPase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11517287, ECO:0000269|PubMed:16983343}. Dynein axonemal particle {ECO:0000305}. Note=Colocalizes with tubulin.
Interaction partners:
- PIH1 domain-containing protein 2
- RuvB-like 2
- Dynein axonemal assembly factor 6
- Protein kintoun
- Dynein axonemal assembly factor 5
- PIH1 domain-containing protein 1
- Dynein axonemal assembly factor 11
- Dynein axonemal assembly factor 3
- Dynein axonemal intermediate chain 2
- Zinc finger MYND domain-containing protein 10
Sequence:
MTTKDYPSLWGFGTTKTFKIPIEHLDFKYIEKCSDVKHLEKILCVLRSGEEGYYPELTEFCEKHLQALAPESRALRKDKPAATAASFTAEEWEKIDGDIKSWVSEIKKEEDKMHFHETETFPAMKDNLPPVRGSNSCLHVGKEKYSKRPTKKKTPRDYAEWDKFDVEKECLKIDEDYKEKTVIDKSHLSKIETRIDTAGLTEKEKDFLATREKEKGNEAFNSGDYEEAVMYYTRSISALPTVVAYNNRAQAEIKLQNWNSAFQDCEKVLELEPGNVKALLRRATTYKHQNKLREATEDLSKVLDVEPDNDLAKKTLSEVERDLKNSEAASETQTKGKRMVIQEIENSEDEEGKSGRKHEDGGGDKKPAEPAGAARAAQPCVMGNIQKKLTGKAEGGKRPARGAPQRGQTPEAGADKRSPRRASAAAAAGGGATGHPGGGQGAENPAGLKSQGNELFRSGQFAEAAGKYSAAIALLEPAGSEIADDLSILYSNRAACYLKEGNCSGCIQDCNRALELHPFSMKPLLRRAMAYETLEQYGKAYVDYKTVLQIDCGLQLANDSVNRLSRILMELDGPNWREKLSPIPAVPASVPLQAWHPAKEMISKQAGDSSSHRQQGITDEKTFKALKEEGNQCVNDKNYKDALSKYSECLKINNKECAIYTNRALCYLKLCQFEEAKQDCDQALQLADGNVKAFYRRALAHKGLKNYQKSLIDLNKVILLDPSIIEAKMELEEVTRLLNLKDKTAPFNKEKERRKIEIQEVNEGKEEPGRPAGEVSMGCLASEKGGKSSRSPEDPEKLPIAKPNNAYEFGQIINALSTRKDKEACAHLLAITAPKDLPMFLSNKLEGDTFLLLIQSLKNNLIEKDPSLVYQHLLYLSKAERFKMMLTLISKGQKELIEQLFEDLSDTPNNHFTLEDIQALKRQYEL
Protein: Telomere repeat-binding factor 5 (MYB transcription factor) (F4IEY4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds preferentially double-stranded telomeric repeats.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000255|PROSITE-ProRule:PRU00837}. Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837}.
Interaction partners:
- At5g08780
- Winged helix-turn-helix transcription repressor DNA-binding protein
- Large ribosomal subunit protein uL13x
- At1g48620
- Histone H1.1
- At3g18035
- HMG-Y-related protein A
- Embryo defective 1703
- Uncharacterized protein At3g14900
- Ubiquitin carboxyl-terminal hydrolase family protein
Sequence:
MGNQKLKWTAEEEEALLAGIRKHGPGKWKNILRDPEFADQLIHRSNIDLKDKWRNLSVPPGTQSLTNKARPAKVKEEGDTPAADANDAVTIPRPIPTIPPPPGRRTLPSELIPDENTKNAPRYDGVIFEALSALADGNGSDVSSIYHFIEPRHEVPPNFRRILSTRLRRLAAQSKLEKVSTFKSIQNFYKIPDPSGTKIGVPKPKETHTKLRQANNQTSADSQQMIEEAAITAACKVVEAENKIDVAKLAAEEFEKMTKIAEENRKLLVIATEMHELCSCGETMLLA
Protein: Gem-associated protein 2 (Q9N405)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Survival motor neuron protein
- Probable small nuclear ribonucleoprotein Sm D2
- Probable small nuclear ribonucleoprotein Sm D1
- Probable small nuclear ribonucleoprotein-associated protein B
- Methylosome subunit pICln
- Probable small nuclear ribonucleoprotein F
- Probable small nuclear ribonucleoprotein G
- ATP-dependent RNA helicase
- Probable small nuclear ribonucleoprotein E
- Probable U2 small nuclear ribonucleoprotein A'
Sequence:
MDQEACLGPSDDFEADDVDMTSPAMSAAQYLRQMQAERRGTKNVVRIAQKSPDSTSPEAKKQKQWLESVGYQEVKKIETPSPLIPSEEWRQEKCRKFEETRAKMALKIEKFSPMRIDRLNSPEEEEWHEILLEKCLPEFQDIAGNFLNHTGTPPALRMVFSIPKRHLSQLIEYLVDWSIEEGLNRPIREWIYSLLAVIDLPLVQDVVSALRRLVKECRSLRSELSIDRKSEANEFSLFITIITIFFGQKDLADI
Protein: Mitosis inhibitor protein kinase SWE1 (EC 2.7.11.1) (Wee1 homolog) (P32944)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Protein kinase that acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylating and inhibiting the mitosis-promoting cyclin B-bound CDC28 at 'Tyr-19'. SWE1-mediated inhibition of CDC28 acts in a cell size or morphogenesis checkpoint to delay mitosis in response to defects in growth, actin organization or bud formation. Inhibits the activity of B-type cyclins in replication initiation strongly for CLB2, moderately for CLB3 and CLB4, and there is no apparent inhibition for CLB5 and CLB6, correlating with the normal expression timing of those cyclins. Hyperphosphorylation and degradation of SWE1 when all checkpoint requirement are met releases CLB2-CDC28 from inhibition and allows for progression through the cell cycle. SWE1-dependent CDC28 phosphorylation is also required for pachytene arrest upon activation of the recombination checkpoint during meiosis. Also involved in the regulation of nitrogen starvation- and short chain alcohol-induced filamentous growth, or filamentous differentiation in response to slowed DNA synthesis. Can act both on serines and on tyrosines.
Subcellular location: Bud neck. Nucleus. Note=When SWE1 first accumulates in G1, it is localized to the nucleus. After bud emergence, a subpopulation is recruited to the daughter side of the mother-bud neck through HSL1 and its adapter HSL7, where it is susceptible to hyperphosphorylation and degradation.
Interaction partners:
- Tyrosine-protein phosphatase CDC14
- Cyclin-dependent kinase 1
- G2/mitotic-specific cyclin-2
- G2/mitotic-specific cyclin-1
- Protein arginine N-methyltransferase HSL7
- Serine/threonine-protein kinase RAD53
- M-phase inducer phosphatase
- Protein phosphatase PP2A regulatory subunit B
- Nucleolar protein NET1
- Sister chromatid cohesion protein 1
Sequence:
MSSLDEDEEDFEMLDTENLQFMGKKMFGKQAGEDESDDFAIGGSTPTNKLKFYPYSNNKLTRSTGTLNLSLSNTALSEANSKFLGKIEEEEEEEEEGKDEESVDSRIKRWSPFHENESVTTPITKRSAEKTNSPISLKQWNQRWFPKNDARTENTSSSSSYSVAKPNQSAFTSSGLVSKMSMDTSLYPAKLRIPETPVKKSPLVEGRDHKHVHLSSSKNASSSLSVSPLNFVEDNNLQEDLLFSDSPSSKALPSIHVPTIDSSPLSEAKYHAHDRHNNQTNILSPTNSLVTNSSPQTLHSNKFKKIKRARNSVILKNRELTNSLQQFKDDLYGTDENFPPPIIISSHHSTRKNPQPYQFRGRYDNDTDEEISTPTRRKSIIGATSQTHRESRPLSLSSAIVTNTTSAETHSISSTDSSPLNSKRRLISSNKLSANPDSHLFEKFTNVHSIGKGQFSTVYQVTFAQTNKKYAIKAIKPNKYNSLKRILLEIKILNEVTNQITMDQEGKEYIIDYISSWKFQNSYYIMTELCENGNLDGFLQEQVIAKKKRLEDWRIWKIIVELSLALRFIHDSCHIVHLDLKPANVMITFEGNLKLGDFGMATHLPLEDKSFENEGDREYIAPEIISDCTYDYKADIFSLGLMIVEIAANVVLPDNGNAWHKLRSGDLSDAGRLSSTDIHSESLFSDITKVDTNDLFDFERDNISGNSNNAGTSTVHNNSNINNPNMNNGNDNNNVNTAATKNRLILHKSSKIPAWVPKFLIDGESLERIVRWMIEPNYERRPTANQILQTEECLYVEMTRNAGAIIQEDDFGPKPKFFI
Protein: Microsomal triglyceride transfer protein large subunit (P55157)
Organism: Homo sapiens (Human)
Function: Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces. Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B. May be involved in regulating cholesteryl ester biosynthesis in cells that produce lipoproteins (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16478722, ECO:0000269|PubMed:22236406, ECO:0000269|PubMed:23475612, ECO:0000269|PubMed:26224785}. Golgi apparatus {ECO:0000269|PubMed:16478722}. Note=Colocalizes with P4HB/PDI in the endoplasmic reticulum (PubMed:23475612, PubMed:26224785). {ECO:0000269|PubMed:23475612, ECO:0000269|PubMed:26224785}.
Interaction partners:
- Apolipoprotein B-100
- Protein disulfide-isomerase
- Apolipoprotein A-I
- Apolipoprotein A-IV
- MICOS complex subunit MIC26
- Apolipoprotein C-III
- Apolipoprotein A-II
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Hepatocyte nuclear factor 4-alpha
- Diacylglycerol O-acyltransferase 1
Sequence:
MILLAVLFLCFISSYSASVKGHTTGLSLNNDRLYKLTYSTEVLLDRGKGKLQDSVGYRISSNVDVALLWRNPDGDDDQLIQITMKDVNVENVNQQRGEKSIFKGKSPSKIMGKENLEALQRPTLLHLIHGKVKEFYSYQNEAVAIENIKRGLASLFQTQLSSGTTNEVDISGNCKVTYQAHQDKVIKIKALDSCKIARSGFTTPNQVLGVSSKATSVTTYKIEDSFVIAVLAEETHNFGLNFLQTIKGKIVSKQKLELKTTEAGPRLMSGKQAAAIIKAVDSKYTAIPIVGQVFQSHCKGCPSLSELWRSTRKYLQPDNLSKAEAVRNFLAFIQHLRTAKKEEILQILKMENKEVLPQLVDAVTSAQTSDSLEAILDFLDFKSDSSIILQERFLYACGFASHPNEELLRALISKFKGSIGSSDIRETVMIITGTLVRKLCQNEGCKLKAVVEAKKLILGGLEKAEKKEDTRMYLLALKNALLPEGIPSLLKYAEAGEGPISHLATTALQRYDLPFITDEVKKTLNRIYHQNRKVHEKTVRTAAAAIILNNNPSYMDVKNILLSIGELPQEMNKYMLAIVQDILRFEMPASKIVRRVLKEMVAHNYDRFSRSGSSSAYTGYIERSPRSASTYSLDILYSGSGILRRSNLNIFQYIGKAGLHGSQVVIEAQGLEALIAATPDEGEENLDSYAGMSAILFDVQLRPVTFFNGYSDLMSKMLSASGDPISVVKGLILLIDHSQELQLQSGLKANIEVQGGLAIDISGAMEFSLWYRESKTRVKNRVTVVITTDITVDSSFVKAGLETSTETEAGLEFISTVQFSQYPFLVCMQMDKDEAPFRQFEKKYERLSTGRGYVSQKRKESVLAGCEFPLHQENSEMCKVVFAPQPDSTSSGWF
Protein: EF-hand domain-containing protein (Q581Z7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}. Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}.
Interaction partners:
- Calcium uniporter protein C-terminal domain-containing protein
- Calcium uniporter protein C-terminal domain-containing protein
- Calcium uniporter protein C-terminal domain-containing protein
- Calcium uniporter protein C-terminal domain-containing protein
- Prohibitin
Sequence:
MLSIWRAVKVSFPQAGHCHSYSVTAMLWSRLWLREMCQRIVGDSRMGCTALTLCVACIGASSWGAATVLCHPLATPEYLIPYYLRSIKSRFRHYASVRSADDGAMLMTMEDFVRSVLVLRKDEPLGASSLEDMSDLFASLDADGNVCLNLTEYTFLMVLLTAKLKDIRMLFTIVDKDRVGTLGLSEFAGVLRGLGCTANEANSLTTGCKNGIVRRLFGDDGELRCSYDEMEGSINAINEAIWRAEFHLFDPNNVGCIGAEEFGKLLAKQMIGSNVPFYVVENIRRMRGINTTVTVDQWIGFHQVMREADTIGEAVRLFMESGLSLGKREFNRVVKAAGVRPFKEEELDLIMALFDRNGDGALDFDEFISLMKRKLSYQYSGSSANEPREVKHFPTRLVECVGETLRGSVG
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q8SWW8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MWCIVNLPNGTQQAVKWDPKANGQECLEKVCRAMNIICEMEYFGLEHWTPNQKESQTRQWINLRNRLSGDSGSSGSGIQLMLALRVKFWVPVHFILQESVRNLFYMQARRDLLEGRLTAPDWSGAAKLAALLCQADGLRFNESSLKADCPMRMRRELAQQQQQQQQQAQQHRLEQQRKEKEHVLSFKKRRLSKQKSMEHIEVCTLPAASTTSCSLQPSPSASASASASASASASASTSACSQTHSNSSSSSPSNSSSQTGLDERLASNPLRVYEEYFMQPSCEGEPPADYLRQIAVEHGKLAKLQMSLKTAKYWLLKSIQDLEGYGEELFSGVTTNESATRCDIAVGAHGITVCRGGEKQSIPFGAIAAAKSLRRTFKLEYVDDHNDRKELEIKLPKQPIAAGLYRSITERHAFYVCDKVRGVVTNQFTRDLKGTIASMFMENTELGKRYVFDIQHTCREVHDQARRTLHERGGDLVAEGAEGCSAVAGGLGASAVGEPGVSPWAMALTTGAGGSMAGKIDLAIREKEAREAAIERCVDTRISEAMQCKICMDRAINTVFNPCCHVIACAQCAARCSNCPNCRVKITSVVKIYLPPELRTSQTGSGATTTSSSSIMGDGQVEEQLLQQQLDEISAAPASLEAGADAGVGVGGMAVGAGAGAGATGPGGQPKVTTAA