wanglab/gogpt-training-data huggingface dataset:
Protein: Non-homologous end joining protein Ku (Q9I1W5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Stimulates rNTP addition to DSB and end joining (ligation) of linear DNA by LigD, on 3'-overhangs and probably also 5'-overhangs and blunt dsDNA breaks. Binds both ends of linear dsDNA protecting it from exonuclease activity.
Interaction partners:
- Multifunctional non-homologous end joining protein LigD
- DNA topoisomerase
- Uncharacterized protein
- Protein MgtC
Sequence:
MARAIWKGAISFGLVHIPVSLSAATSSQGIDFDWLDQRSMEPVGYKRVNKVTGKEIERENIVKGVEYEKGRYVVLSEEEIRAAHPKSTQTIEIFAFVDSQEIPLQHFDTPYYLVPDRRGGKVYALLRETLERTGKVALANVVLHTRQHLALLRPLQDALVLITLRWPSQVRSLDGLELDESVTEAKLDKRELEMAKRLVEDMASHWEPDEYKDSFSDKIMKLVEEKAAKGQLHAVEEEEEVAGKGADIIDLTDLLKRSLRSRAGGGKDKGSEKAGADAKGRAKSGASRSRRKA
Protein: GID complex subunit 8 (Dosage-dependent cell cycle regulator 1) (Glucose-induced degradation protein 8) (P40208)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium. Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1). Required also for cell cycle progression. Positively controls G1 and the timing of START.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- GID complex subunit 1
- GID complex subunit 7
- E3 ubiquitin-protein ligase RMD5
- GID complex substrate-recognition subunit 4
- GID complex subunit 5
- GID complex subunit 9
- GID complex substrate-recognition subunit 10
- GID complex associated protein 12
- Fructose-1,6-bisphosphatase
- Protein SSH4
Sequence:
MTISTLSNETTKSGSCSGQGKNGGKDFTYGKKCFTKEEWKEQVAKYSAMGELYANKTIHYPLKIQPNSSGGSQDEGFATIQTTPIEPTLPRLLLNYFVSMAYEDSSIRMAKELGFIRNNKDIAVFNDLYKIKERFHIKHLIKLGRINEAMEEINSIFGLEVLEETFNATGSYTGRTDRQQQQQQQQFDIDGDLHFKLLLLNLIEMIRSHHQQENITKDSNDFILNLIQYSQNKLAIKASSSVKKMQELELAMTLLLFPLSDSADSGSIKLPKSLQNLYSISLRSKIADLVNEKLLKFIHPRIQFEISNNNSKFPDLLNSDKKIITQNFTVYNNNLVNGSNGTKITHISSDQPINEKMSSNEVTAAANSVWLNQRDGNVGTGSAATTFHNLENKNYWNQTSELLSSSNGKEKGLEFNNYYSSEFPYEPRLTQIMKLWCWCENQLHHNQIGVPRVEN
Protein: DPEP2 neighbor protein (A0A0U1RQF7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTDRILYIVSNMSSVPWEGSAAAAVPATSPPTPGHYHVLYRGCGETQVGWHGETYCLVGGYRVHGDAPLATPTKAEAEKPAPRRAPKRRQATIESDKDLGCSSPKIRRLEHRGRRLTPQKLAG
Protein: Probable lipoprotein LppI (O53489)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MRIAALVAVSLLIAGCSREVGGDVGQSQTIAPPAPAPSAAPSTPPAAGAPITTIVSWIEAGHPVDPAAYHVATRDGVTTQLGDDVAFSASSGTVACMTDARHTSGTLACLVRLANPPPRPETAYGEWKGGWVDFDGIHLQVGSARADPGPFVYGNGPELANGDTLSIGDYRCRSYQAGLFCVNYAHQSAVRFASAGIEPFGCLKPAPPPDGVGVAFGC
Protein: ADP-ribosylation factor GTPase activating protein 3, isoform E (M9PGG0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASPAAGPSKQEIESVFSRLRAQPANKSCFDCAAKAPTWSSVTYGIFICIDCSAVHRNLGVHLTFVRSTNLDTNWTWLQLRQMQLGGNANAAQFFRAHNCSTTDAQVKYNSRAAQLYRDKLCAQAQQAMKTHGTKDPNPPTVAPVISVETQQGGAPSVNLLNSVVPAAVPSSIGARKVQPKKGGLGARKVGGLGATKVKTNFADIEARANAANEMKTSAAAAPVVKPQTAEDELETVASMRLAYQELSMQKTREEAKLKTMDPAKAKQMERLGMGFNLRGSDMAHSALGDMETIQQSAAPKAKLSLLESENFFTDFSLYGNSSSGGGGGGSSEKRESSVGGTSKLDKFELDALGYETIEPIGGSHSNITSMFSRSNDYDKPKTSAPVKKNSGSSQTHTKGGTSTDPVIAQQKFGNSKGFGSDQYFASEQSSADVSASLNRFQGSRAISSSDYFGDGSPGGTGGNRASSVNFSAPDLDVESVKESVRQGVHKVAGRLSNLANDVMTSWQDKYGY
Protein: UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase 3 (EC 2.4.2.-) (Rhamnogalacturonan xylosyltransferase 3) (Q9FXA7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of D-xylose from UDP-alpha-D-xylose onto L-fucose. Probably involved in the biosynthesis of rhamnogalacturonan II (RG-II) through xylosylation of the internal fucose moiety of the A-chain of RG-II, a structurally complex pectic polysaccharide of the primary cell wall. RG-II is essential for the cell wall integrity of rapidly growing tissues such as roots and pollen tube growth and elongation.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta
- AUGMIN subunit 6
- Xylogalacturonan beta-1,3-xylosyltransferase
- Xyloglucan 6-xylosyltransferase 1
- Galactan beta-1,4-galactosyltransferase GALS1
- Polygalacturonate 4-alpha-galacturonosyltransferase
- Cytochrome P450, family 77, subfamily A, polypeptide 9
- Probable arabinosyltransferase ARAD1
- Arabinosyltransferase RRA1
- Probable galacturonosyltransferase 7
Sequence:
MAQQSQRPISNRHISLLNRNGLILLLLLALFVILGVFLPLTKSSLFMFPNTTSSSLSPSSSLSVSDWRDYSLAQAVKFVAKNETVIVCAVSYPFLPFLNNWLISISRQKHQEKVLVIAEDYATLYKVNEKWPGHAVLIPPALDPQSAHKFGSQGFFNLTSRRPQHLLNILELGYNVMYNDVDMVWLQDPFDYLQGSYDAYFMDDMIAIKPLNHSHDLPPLSRSGVTYVCSCMIFLRSTDGGKLLMKTWVEEIQAQPWNNTQAKKPHDQPAFNRALHKTANQVKVYLLPQSAFPSGGLYFRNETWVNETRGKHVIVHNNYIIGYDKKMKRFQDFSLWLVDDHALESPLGKLEIYQEQNTTTEGKNLTKIVRKQRKNRGKKHKLP
Protein: Anillin isoform X1 (Anillin, actin-binding protein) (A0A286Y917)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Kinesin-like protein
- Epithelial cell-transforming 2
- Kinesin family member 11
- Actin alpha 1, skeletal muscle b.
- Rac GTPase-activating protein 1
- Uncharacterized protein.
- CD2-associated protein
- Rho-related GTP-binding protein RhoA-B
- Aurora kinase B
- Discs, large
Sequence:
MDPFTEKLLERTRARRENLQKKMAERPTAANRPMAKRTREPLTDTNSVLSEPTIEKALPSSKPSPFKRRCSDENTFLAGEENKQPVAPQMTDPMTDQKPPLAPTTVRPIPVEQRSAPDMLPTRPPPETEKMVVCPPQSPAKRTDNVLRQKGLDGARETQKEAPTTFPSSMRSRLQRLAGQRQNWDSNGATEAVSESVVVSPLKSHNLDHPPATPTNSEVPVGRKGRLANLAATIGSWEDDLGHPPIRRDNAQAQPGTAYVRPPVSTVTSNSEQLQSARPTSHRPVNRGQQPAVYSPVKSTSVVPPSPQKTEFPQARWAQAVPSPVSSPLKIPPSTQPSSPLKSVTASPSSPHRGYVSQSPLKSHGQVDKLNFGAALNSSPAKPVLAPKPSAADDAVSRVRFTKDATPTQHRGPAATPGGVKSFLERFGERCQERNQNTPSMLGGPGHTSAASTPATPKFKLLQERLGGAQATSTTAALTEKQKMEREAELAQIRNRFQKGNMLRGKEDISEVKDDTENKEIELSLQSQTSLPLHDNKPSVHVPEVFNSPSKSIGKGMSCASSSPAKEIELKVEMPTVEEPEDVQEVDVVREIEMNVDASVNSEVINELFDGVLEESDEDADEDPLNISSMSLLAPLAETVAAVIKSPERKPMTSTPANSFLVKSSTPENPSRPSKFQRTRMLRADSSDSIDVLDEQQNQKLLYSIDAYRSTRVKSEPERPHVKQVIVRKEDVSQRMEMNGSSSHINIKQKMKMLTNEMNLQQTVIHQASQALNCCTDEEHGKGSQVEAEAERLLIIATERRAALKAELDRLKAEGPTAQKKSASSVPVDIGLPASKGSISLLELRLPLKADFICSSANKPECGNHYFFVMIRAGPENTVATPLSSTRTGLSGDALTFTTTFTLSDVSNDFEIDIEVYCLVQKRELNPDKRKKASKSKAITPKRFLNISKSNLQTPVMASPGGPNAVRTSSFVLVGSHKLTLASIGKNKFPLEKIKYERSERELLSDMFHNKVPFLCPLEGHVYLKMQCEVGSRIEEKGFLTMFEDVSGFGAWHRRWCVLSGYCISYWTYPDDEKRKNPMGRINLANCTSRKVEPANREFCARPNTFELITVRPQREDDRETLVSRCKDTLCVTKNWLSADTKDERNLWMQKLNQILVDLRMWQPDSCYRPM
Protein: Coagulation factor XIII A chain (Coagulation factor XIIIa) (EC 2.3.2.13) (Protein-glutamine gamma-glutamyltransferase A chain) (Transglutaminase A chain) (Q8BH61)
Organism: Mus musculus (Mouse)
Function: Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P00488}. Secreted {ECO:0000250|UniProtKB:P00488}. Note=Secreted into the blood plasma. Cytoplasmic in most tissues, but also secreted in the blood plasma. {ECO:0000250|UniProtKB:P00488}.
Interaction partners:
- Coagulation factor XIII B chain
- Prothrombin
- Fibrinogen alpha chain
- von Willebrand factor
- Fibrinogen gamma chain
Sequence:
MSDTPASTFGGRRAVPPNNSNAAEVDLPTEELQGLVPRGVNLKDYLNVTAVHLFKERWDSNKIDHHTDKYDNNKLIVRRGQTFYIQIDFNRPYDPRKDLFRVEYVIGRYPQENKGTYIPVPVVKELQSGKWGAKVIMNEDRSVRLSVQSSPECIVGKFRMYVAVWTPYGILRTRRDPETDTYILFNPWCEEDAVYLDDEKEREEYVLNDIGVIFYGDFKDIKSRSWSYGQFEDGILDTCLYVMDKAEMDLSGRGNPIKVSRVGSAMVNAKDDEGVLVGSWDNVYAYGIPPSAWTGSVDILLEYRSSETPVRYGQCWVFAGVFNTFLRCLGIPARVITNYFSAHDNDANLQMDIFLEEDGNVSSKLTKDSVWNYHCWNEAWMTRPDLPVGFGGWQAVDSTPQENSDGMYRCGPASVQAVKHGHVCFQFDAPFVFAEVNSDLVYITAKQDGTHVVEAVDATHIGKLIVTKQIGGDGMQDITDTYKFQEGQEEERLALETALMYGAKKTLNTEGVVKSRSDVTMNFDVENAVLGKDFKVTITFQNNSSNLYTILAYLSGNITFYTGVSKKEFKKESFEETLDPFSSKKKEVLVRAGEYMSHLLEQGFLHFFVTARINESRDVLAKQKSIILTIPKITIKVRGAAMVGSDMVVTVEFTNPLKETLQNVWIHLDGPGVMRPKRKVFREIRPNTTVQWEEVCRPWVSGHRKLIASMTSDSLRHVYGELDLQIQRRPTM
Protein: Candida glabrata strain CBS138 chromosome M complete sequence (Q6FIJ0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome D complete sequence
- Nicotinamide-nucleotide adenylyltransferase
- Lysine--tRNA ligase
- Lysine--tRNA ligase
Sequence:
MAPLNVGVIGTGIFATDRHLPSYQEMSDDFKVVAAFNRTKSKALKFAELAGLPEEKVYDDLKGIVNDPEVQMLDMLLPAQFNLDTVKHAIGAGKPILLEKPIAATMAQAREVVKLADSVDIPIGIAENWLYLPCIDVAKPLLEKIGPIVAFTHNSTGPFVTQNKYLSTSWRQNPEHIGGFLSDGGVHQLALVTELVGEIACVSALTRQVRKESGTVDIVFSTVEMKDSDIIGTFTYGSAFGATDKSVFLKIYGRNGTVVVELSDKKKPVVKVRYGSSAEECSAEEVHDVPLDDTFGVNAEFQNFREAVTKKDKKLFRSTPRVAFHHLACVAAFLESSDKNGDHVKVETI
Protein: Uncharacterized protein C3orf62 (Q6ZUJ4)
Organism: Homo sapiens (Human)
Function: Essential for normal spermatogenesis and male fertility.
Interaction partners:
Sequence:
MHYIKTWSLLGEMSEKLRRCRKELTAAIDRAFEGVSYSQECTGQQRLELSAAPLSFSLPVHRLLCRRHPLAACSSAAPFAAVPCAPENENPAFATNHAPVNAKPHALCPERKPLTSKENVLMHSSILAPERESWRTAGEGENWRKENLRKDMERDLKADSNMPLNNSSQEVTKDLLDMIDHTSIRTIEELAGKIEFENELNHMCGHCQDSPFKEEAWALLMDKSPQKATDADPGSLKQAFDDHNIVETVLDLEEDYNVMTSFKYQIE
Protein: ATP-dependent RNA helicase MRH4, mitochondrial (EC 3.6.4.13) (Mitochondrial RNA helicase 4) (P53166)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-binding RNA helicase involved in mitochondrial RNA metabolism. Required for maintenance of mitochondrial DNA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:12702275, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Pre-mRNA-splicing factor SNU114
- Pre-mRNA-splicing factor CEF1
- ATP-dependent RNA helicase SUV3, mitochondrial
- Pre-mRNA-splicing factor 6
- Large ribosomal subunit protein uL3m
- ATP synthase subunit beta, mitochondrial
- Mitochondrial GTPase 1
- ATP synthase subunit gamma, mitochondrial
- rRNA methyltransferase 1, mitochondrial
- ATP-dependent helicase NAM7
Sequence:
MSLFFKPVISPQWSFPVLLKIGVRSYAGGPRTKHKGNSPLASVPTGSSNKNRKQKAKGKKGNKKNDPDQAFNFGEYGGLKKDVEMNMDSTNKLIQKISNFDQLLILPPVRDAVKEIISKESLKLQDSRKKTSENIIPSPIQTVAIKRISKNLMDPKLQIHAIAAETGSGKTMAYLIPLIDYLKRQELETPELWETLRKNVLIRSIILVPTHELVDQVYETVSKTKTLLGLNSFKWDKATSYRDLLENIKNRIDILVTTPGKLLNLFSIRMITRPDKVLSKVGFVVLDEADTLLDRSWLEETHSAIKRIPNINHLIFCSATIPQEFNKTMQRLFPTVVPIMTPRLHKLPFALDFKVINSALSPFKGSKIKALAQTLYAISNDDTEPGFEKRCIIFVNEKKNVPEIVNLLNKKFGHNAIGLTGEDTFEERSEKIMPFLSPPRPLSEVVAQSTSPPTSLKKFEIPDSNIVIGKLKNTNSNGTAPSNKSLHVLVTTDLMARGLNFKGVRNVVLYDVPKTSIDLIHRVGRTARMKQGGRVFMLTDSKTKSWAKALPKIIKKHQRLS
Protein: Arginine repressor (P0A6D0)
Organism: Escherichia coli (strain K12)
Function: Negatively controls the expression of the four operons of arginine biosynthesis in addition to the carAB operon. Predominantly interacts with A/T residues in ARG boxes. It also binds to a specific site in cer locus. Thus it is essential for cer-mediated site-specific recombination in ColE1. It is necessary for monomerization of the plasmid ColE1.
Subcellular location: Cytoplasm.
Interaction partners:
- N-acetyl-gamma-glutamyl-phosphate reductase
- Amino-acid acetyltransferase
- Acetylglutamate kinase
- Ornithine carbamoyltransferase subunit F
- Met repressor
- Argininosuccinate synthase
- Ornithine carbamoyltransferase subunit I
- Argininosuccinate lyase
- Trp operon repressor
- Tyrosine recombinase XerD
Sequence:
MRSSAKQEELVKAFKALLKEEKFSSQGEIVAALQEQGFDNINQSKVSRMLTKFGAVRTRNAKMEMVYCLPAELGVPTTSSPLKNLVLDIDYNDAVVVIHTSPGAAQLIARLLDSLGKAEGILGTIAGDDTIFTTPANGFTVKDLYEAILELFDQEL
Protein: Adenylate isopentenyltransferase 8, chloroplastic (AtIPT8) (EC 2.5.1.112) (Adenylate dimethylallyltransferase 8) (Cytokinin synthase 8) (Plant growth activator 22) (Q9LJL4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in cytokinin biosynthesis. Catalyzes the transfer of an isopentenyl group from dimethylallyl diphosphate (DMAPP) to ATP and ADP.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:14726522}.
Interaction partners:
- Cytokinin hydroxylase
- Cytokinin hydroxylase
- Isopentenyl-diphosphate Delta-isomerase I, chloroplastic
- Isopentenyl-diphosphate Delta-isomerase II, chloroplastic
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic
- Cytokinin dehydrogenase 1
- Histidine kinase 2
- Cytokinin dehydrogenase 5
- Histidine kinase 3
- Cytokinin dehydrogenase 3
Sequence:
MQNLTSTFVSPSMIPITSPRLRLPPPRSVVPMTTVCMEQSYKQKVVVIMGATGSGKSCLSIDLATRFSGEIVNSDKIQFYDGLKVTTNQMSILERCGVPHHLLGELPPDDSELTTSEFRSLASRSISEITARGNLPIIAGGSNSFIHALLVDRFDPKTYPFSSETSISSGLRYECCFLWVDVSVSVLFEYLSKRVDQMMESGMFEELAGFYDPRYSGSAIRAHGIHKTIGIPEFDRYFSLYPPERKQKMSEWDQARKGAYDEAVQEIKENTWRLAKKQIERIMKLKSSGWDIQRLDATPSFGRSSREIWDNTVLDESIKVVKRFLVKDKV
Protein: Protein zwilch homolog (hZwilch) (Q9H900)
Organism: Homo sapiens (Human)
Function: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex.
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000269|PubMed:20462495}.
Interaction partners:
- Centromere/kinetochore protein zw10 homolog
- Kinetochore-associated protein 1
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Outer kinetochore KNL1 complex subunit ZWINT
- Cell division cycle protein 20 homolog
- Mitotic checkpoint protein BUB3
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Separin
- Centromere-associated protein E
- Kinesin-like protein KIF11
Sequence:
MWERLNCAAEDFYSRLLQKFNEEKKGIRKDPFLYEADVQVQLISKGQPNPLKNILNENDIVFIVEKVPLEKEETSHIEELQSEETAISDFSTGENVGPLALPVGKARQLIGLYTMAHNPNMTHLKINLPVTALPPLWVRCDSSDPEGTCWLGAELITTNNSITGIVLYVVSCKADKNYSVNLENLKNLHKKRHHLSTVTSKGFAQYELFKSSALDDTITASQTAIALDISWSPVDEILQIPPLSSTATLNIKVESGEPRGPLNHLYRELKFLLVLADGLRTGVTEWLEPLEAKSAVELVQEFLNDLNKLDGFGDSTKKDTEVETLKHDTAAVDRSVKRLFKVRSDLDFAEQLWCKMSSSVISYQDLVKCFTLIIQSLQRGDIQPWLHSGSNSLLSKLIHQSYHGTMDTVSLSGTIPVQMLLEIGLDKLKKDYISFFIGQELASLNHLEYFIAPSVDIQEQVYRVQKLHHILEILVSCMPFIKSQHELLFSLTQICIKYYKQNPLDEQHIFQLPVRPTAVKNLYQSEKPQKWRVEIYSGQKKIKTVWQLSDSSPIDHLNFHKPDFSELTLNGSLEERIFFTNMVTCSQVHFK
Protein: Orotate phosphoribosyltransferase (EC 2.4.2.10) (Q5B0P6)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Dihydroorotate dehydrogenase
- Orotidine 5'-phosphate decarboxylase
- Got1 family protein
- Ribose-phosphate pyrophosphokinase
- ribose-phosphate diphosphokinase
Sequence:
MSAAPEQKAALLPLLISNKVLSFGTYTLKSGRESPYFFTSSLLHTAPLLRATSAAYASVLSAAPFVTTAADGTTTPNFDIIFGPAYKGIPICAAVVNELAVRDSLAGQAKGTWDNVSYSFNRKEAKDHGEGGNIVGAPLKGKRVVIVDDVITAGTALREAVGIIEKEGGIVSGVVVLLDREERVSESEAKSAVGCAQRDLGEKVPVRAVIGLHDLIEKLGSEIGEGEIQRLKDYRARYGAK
Protein: Polycomb group RING finger protein 5 (RING finger protein 159) (Q86SE9)
Organism: Homo sapiens (Human)
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity. Plays a redundant role with PCGF3 as part of a PRC1-like complex that mediates monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is required for normal silencing of one copy of the X chromosome in XX females (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:21282530, ECO:0000269|PubMed:25519132}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q3UK78}. Note=Recruited by the non-coding RNA Xist to specific nuclear foci that probably correspond to the inactivated X chromosome. {ECO:0000250|UniProtKB:Q3UK78}.
Interaction partners:
- E3 ubiquitin-protein ligase RING1
- E3 ubiquitin-protein ligase RING2
- RING1 and YY1-binding protein
- Autism susceptibility gene 2 protein
- Polycomb group RING finger protein 3
- YY1-associated factor 2
- Polycomb group RING finger protein 1
- Polycomb group RING finger protein 2
- Chromobox protein homolog 8
- Chromobox protein homolog 6
Sequence:
MATQRKHLVKDFNPYITCYICKGYLIKPTTVTECLHTFCKTCIVQHFEDSNDCPRCGNQVHETNPLEMLRLDNTLEEIIFKLVPGLREQELERESEFWKKNKPQENGQDDTSKADKPKVDEEGDENEDDKDYHRSDPQIAICLDCLRNNGQSGDNVVKGLMKKFIRCSTRVTVGTIKKFLSLKLKLPSSYELDVLCNGEIMGKDHTMEFIYMTRWRLRGENFRCLNCSASQVCSQDGPLYQSYPMVLQYRPRIDFG
Protein: Roundabout homolog 4 (Magic roundabout) (Q8WZ75)
Organism: Homo sapiens (Human)
Function: Receptor for Slit proteins, at least for SLIT2, and seems to be involved in angiogenesis and vascular patterning. May mediate the inhibition of primary endothelial cell migration by Slit proteins (By similarity). Involved in the maintenance of endothelial barrier organization and function.
Interaction partners:
- Slit homolog 3 protein
- Slit homolog 2 protein
- Slit homolog 1 protein
- Netrin receptor UNC5B
- Paxillin
- Transcription factor SOX-18
- Multimerin-2
- Roundabout homolog 1
- Claudin-5
- Cadherin-5
Sequence:
MGSGGDSLLGGRGSLPLLLLLIMGGMAQDSPPQILVHPQDQLFQGPGPARMSCQASGQPPPTIRWLLNGQPLSMVPPDPHHLLPDGTLLLLQPPARGHAHDGQALSTDLGVYTCEASNRLGTAVSRGARLSVAVLREDFQIQPRDMVAVVGEQFTLECGPPWGHPEPTVSWWKDGKPLALQPGRHTVSGGSLLMARAEKSDEGTYMCVATNSAGHRESRAARVSIQEPQDYTEPVELLAVRIQLENVTLLNPDPAEGPKPRPAVWLSWKVSGPAAPAQSYTALFRTQTAPGGQGAPWAEELLAGWQSAELGGLHWGQDYEFKVRPSSGRARGPDSNVLLLRLPEKVPSAPPQEVTLKPGNGTVFVSWVPPPAENHNGIIRGYQVWSLGNTSLPPANWTVVGEQTQLEIATHMPGSYCVQVAAVTGAGAGEPSRPVCLLLEQAMERATQEPSEHGPWTLEQLRATLKRPEVIATCGVALWLLLLGTAVCIHRRRRARVHLGPGLYRYTSEDAILKHRMDHSDSQWLADTWRSTSGSRDLSSSSSLSSRLGADARDPLDCRRSLLSWDSRSPGVPLLPDTSTFYGSLIAELPSSTPARPSPQVPAVRRLPPQLAQLSSPCSSSDSLCSRRGLSSPRLSLAPAEAWKAKKKQELQHANSSPLLRGSHSLELRACELGNRGSKNLSQSPGAVPQALVAWRALGPKLLSSSNELVTRHLPPAPLFPHETPPTQSQQTQPPVAPQAPSSILLPAAPIPILSPCSPPSPQASSLSGPSPASSRLSSSSLSSLGEDQDSVLTPEEVALCLELSEGEETPRNSVSPMPRAPSPPTTYGYISVPTASEFTDMGRTGGGVGPKGGVLLCPPRPCLTPTPSEGSLANGWGSASEDNAASARASLVSSSDGSFLADAHFARALAVAVDSFGFGLEPREADCVFIDASSPPSPRDEIFLTPNLSLPLWEWRPDWLEDMEVSHTQRLGRGMPPWPPDSQISSQRSQLHCRMPKAGASPVDYS
Protein: F-box C protein (O44714)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MDASYSSSRPKKLNYTSYTSLKSVLKFLSVKKREQIHIHIPELRSVNALLPYAHEEVILDKFEIMIQNRSYLFKKLAEKAPKPEGVARRRPEYEYAEYNRLLVMDLGPPSLFDMNDLHHLWRPMGNQGPDRLSFGDLDSLEKRRLRFRRENRLQDSSEHGRTGNCEITISEEDGTAITVTKEIPVDIAYEKIFDAFFSNGSRIKLLKVQSFPDFLMRKDLLTLKVREIDCSSTASIDILELAPFLDHSSLKKLTLNVTNTNVDLLMLPLVQNCPVLRIVEAGTFLSRMLKTTLLSALQNQKLEIFPDIVIIESFPQLVQSWATSSRPIGSLVQVGIREDYKEVLDILDFLKESHGAHPAIIKKLENTDFSNGLSMLIDGDLELAIYGGGKISEEGLTRPQPCKWSLCMEVMKRGDTIPR
Protein: Monocarboxylate 2-oxoacid-binding periplasmic protein all3028 (Extracellular solute-binding protein) (Extracytoplasmic solute receptor protein all3028) (TRAP transporter monocarboxylate 2-oxoacid-binding subunit P) (Q8YSQ6)
Organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system involved in the uptake of monocarboxylate 2-oxoacids. This protein specifically binds monocarboxylate 2-oxoacids including pyruvate, 2-oxobutyrate, 2-oxovalerate, 2-oxoisovalerate, 2-oxoisocaproate and 2-oxo-3-methylvalerate. Is not able to bind mannitol.
Subcellular location: Periplasm {ECO:0000250|UniProtKB:P44542}.
Interaction partners:
- Alr3027 protein
- Alr3026 protein
Sequence:
MKRREVLNTAAIATATTALVSCTQTNTSSVQAGLPNVRWRMTTSWPKSLGTFIGAETVAKRVAEMTNGRFKITPFAAGELVPGLQVLDAVQAGTVECGHTSSYYYIGKSPALAFATSVPFGLNAQQQYAWLYQGGGLAAIQKIYANFNVINFPAGSTGAQMGGWFKKEIKSVSDLKGLKMRIPGLGGQVMSRLGVNVQVLPGGEIYLALDRGAIDAAEWVGPYDDEKLGLNKAAQFYYYPGWWEPGPTLDVLVNLNAWNRLPKEYQEIFKTATVEANLTMLNQYDALNGEALTRLLAGGTKLVPYSQEIMQAAQKISFDIFEENASKDAAFKQVYEQWKAFRKQIFAWNRVNELSYENFASSSQ
Protein: Sorting nexin-16 (P57768)
Organism: Homo sapiens (Human)
Function: May be involved in several stages of intracellular trafficking. Plays a role in protein transport from early to late endosomes. Plays a role in protein transport to the lysosome. Promotes degradation of EGFR after EGF signaling. Plays a role in intracellular transport of vesicular stomatitis virus nucleocapsids from the endosome to the cytoplasm.
Subcellular location: Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Late endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm {ECO:0000250}. Lysosome {ECO:0000250}.
Interaction partners:
- F-BAR and double SH3 domains protein 2
Sequence:
MATPYVPVPMPIGNSASSFTTNRNQRSSSFGSVSTSSNSSKGQLEDSNMGNFKQTSVPDQMDNTSSVCSSPLIRTKFTGTASSIEYSTRPRDTEEQNPETVNWEDRPSTPTILGYEVMEERAKFTVYKILVKKTPEESWVVFRRYTDFSRLNDKLKEMFPGFRLALPPKRWFKDNYNADFLEDRQLGLQAFLQNLVAHKDIANCLAVREFLCLDDPPGPFDSLEESRAFCETLEETNYRLQKELLEKQKEMESLKKLLSEKQLHIDTLENRIRTLSLEPEESLDVSETEGEQILKVESSALEVDQDVLDEESRADNKPCLSFSEPENAVSEIEVAEVAYDAEED
Protein: Mitochondrial amidoxime-reducing component 1 (mARC1) (EC 1.7.-.-) (Molybdenum cofactor sulfurase C-terminal domain-containing protein 1) (MOSC domain-containing protein 1) (Moco sulfurase C-terminal domain-containing protein 1) (Q9CW42)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reduction of N-oxygenated molecules, acting as a counterpart of cytochrome P450 and flavin-containing monooxygenases in metabolic cycles. As a component of prodrug-converting system, reduces a multitude of N-hydroxylated prodrugs particularly amidoximes, leading to increased drug bioavailability. May be involved in mitochondrial N(omega)-hydroxy-L-arginine (NOHA) reduction, regulating endogenous nitric oxide levels and biosynthesis. Postulated to cleave the N-OH bond of N-hydroxylated substrates in concert with electron transfer from NADH to cytochrome b5 reductase then to cytochrome b5, the ultimate electron donor that primes the active site for substrate reduction.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q5VT66}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q5VT66}. Membrane {ECO:0000250|UniProtKB:Q5VT66}; Lipid-anchor {ECO:0000250|UniProtKB:Q5VT66}. Note=Mitochondrial import is mediated by AA 1-40 and requires ATP. {ECO:0000250|UniProtKB:Q5VT66}.
Interaction partners:
- Cytochrome b5 type B
- NADH-cytochrome b5 reductase 3
- Sulfite oxidase, mitochondrial
Sequence:
MGAGSWALTLFGFSAFRVPGQPRSTWLGVAALGLAAVALGTVAWRRARPRRRRRLQQVGTVAQLWIYPIKSCKGLSVSEAECTAMGLRYGHLRDRFWLVINEEGNMVTARQEPRLVLISLTCEDDTLTLSAAYTKDLLLPITPPATNPLLQCRVHGLEIQGRDCGEDAAQWVSSFLKMQSCRLVHFEPHMRPRSSRQMKAVFRTKDQVAYSDASPFLVLSEASLEDLNSRLERRVKATNFRPNIVISGCGVYAEDSWNEVLIGDVELKRVMACTRCLLTTVDPDTGISDRKEPLETLKSYRLCDPSEQALYGKLPIFGQYFALENPGTIRVGDPVYLLGQ