wanglab/gogpt-training-data huggingface dataset:
Protein: WD repeat protein iqw1 (O94527)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Ligand-dependent coactivator of nuclear receptors that may function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- DNA damage-binding protein 1
- Chromatin modification-related protein rik1
- Cullin-4
- Uncharacterized WD repeat-containing protein C17D11.08
- WD repeat-containing protein 21
- RING-box protein pip1
- Rik1-associated factor 1
- Uncharacterized WD repeat-containing protein C343.17c
- Histone-lysine N-methyltransferase, H3 lysine-9 specific
- Rik1-associated factor 2
Sequence:
MSGISLSLRQLDYRDWFQRKISRDIYGNSTWLTGIDLQKELTGHTGCVNTLDWSADGEFLLSGSDDTRLIVWDVFNEYKPRHLISTGHVQNIFSAKFVPYSNNRQILSASGDKLIKLFDLDSSKEGGMDHGMETQTRCWSCALDSVKNIVPCDNGHTFLVCSEDGTARQYDIREPHVCNQDLDCPSILVNYNPYRINLYTITMSPSNPYYFAIGGTHPYAFLYDRRMVKKSFRDDWTMNTSPEKDCRCVRKFSPDGSCNSQGILDRYITCCQFSAANPNELLVSWNSDYVYLFHVHEDKSYTPTFNKIEDSNKKPSKPSLLQTQPLKRKNYSPWYKNNFGASTPASRVSRNPYTAAQPRKHTFYQMYENIEKFFTTENGGLYESIVSGRLSHFSRSIQYVKDAIYFLENYNYIPDSNGLNHSIRVSALRYWRACVSILALMDDTVSLEPNTIIQAGWGWLYDFMNWVTRYLLGISDHWALQMSPPTNVARQNFVLCDPDEPSRVLFSNPSEMIRAFARIDTNDLSSVRRFFWIHKVLRGCLLLISSDIYWEQFQPWDSSTSDVTSSQRLDDENGFLTLLEPPVNYENEVESSSGENIVSMYTGHSDLNDDDDDYQDEESYSYASDDDDESDEDSDEGPTLLSLRMKKRKAVEPNVPVNTHVKSYYGHCNVESIKNVNFYGQNDEYVMSGSDDGRFFIWDKLNASILAIIHGDSEAVNVIEGHPRCPTLAVSGIDSTVKIFNTENTPPSGCSRNHTSNSYKIIATNEMNRQQGSRDSYITSRMLSHLAYRAHLDDGFGHEVLDTDACSIM
Protein: Glutathione S transferase D11, isoform B (EC 1.11.1.9, EC 2.5.1.18) (B7Z0S9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Glutathione S-transferase D4
- Glutathione S transferase E11, isoform A
- Glutathione S transferase E4
- Glutathione S-transferase S1
- Glutathione S transferase E2
- Glutathione S transferase E5
- Glutathione S transferase E8, isoform A
- Glutathione S transferase T1
- FI01423p
Sequence:
MSDTKRIVTEFVYCLLLRGGKMSPPVLYYLPPSPPCRSILLLAKMLDIDFELKIVNILEGEQLKPDFVAMNPQHCVPTMNDEGLVLWESRAILSYLVAAYGKSDQLYPTDIRVRALVDQRLQFDLGTLYMRLTDYYFPTMFIGAPLDEGKRAKLAEAVGWLNTILEGRQFSAADHFTIADLTLLVTVSQLEAFEFELRPYKHIRQWLDRCKDHMAPFDYEELNANKANMLADMFKAKMNQSAG
Protein: HSP90AB1 protein (Q6PK50)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEEDKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFEKKKKKK
Protein: Late cornified envelope protein 1B (Late envelope protein 2) (Small proline-rich-like epidermal differentiation complex protein 2A) (Q5T7P3)
Organism: Homo sapiens (Human)
Function: Precursors of the cornified envelope of the stratum corneum.
Interaction partners:
- Late cornified envelope protein 1C
- Late cornified envelope protein 1E
- Late cornified envelope protein 1A
- Late cornified envelope protein 2B
- Late cornified envelope protein 1D
- Late cornified envelope protein 2C
- Late cornified envelope protein 2A
- Late cornified envelope protein 1F
- Late cornified envelope protein 2D
- Loricrin
Sequence:
MSCQQNQQQCQPPPKCIPKCPPKCLTPRCPPKCPPKCPPVSSCCSVSSGGCCGSSSGGSCGSSSGGCCSSGGGGCCLSHHRRRRSHCHRPQSSGCCSQPSGGSSCCGGGSGQHSGGCC
Protein: Sm protein F (Q38DY4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR006609}.
Interaction partners:
- G10 protein
- Sm protein G
- Sm protein B
- Pre-mRNA-splicing factor Syf1-like N-terminal HAT-repeats domain-containing protein
- U5 small nuclear ribonucleoprotein component, putative
- U1 small nuclear ribonucleoprotein, putative
- Small nuclear ribonucleoprotein E
- PRP8 protein homologue
- PRP1 splicing factor N-terminal domain-containing protein
- Small nuclear ribonucleoprotein Sm D2
Sequence:
MDANVPAAFLASLVGNTVHVKSKWGPVYVGTLVSCDPYMNLQLRDAVEKAKQETELGDMLLRNNNVLYIREVPKE
Protein: Forkhead box protein A2-A (FoxA2-A) (FoxA2a) (Fork head domain-related protein 3) (xFD-3) (Hepatocyte nuclear factor 3-beta homolog A) (HNF-3-beta-A) (HNF3-beta homolog A) (HNF3-beta-A) (xHNF3-beta-A) (xbeta-1) (Q91765)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as a transcriptional activator during early development, limiting the extent of mesoderm formation in the gastrula. Binds to DNA via the target sequence 5'-GT[AC]AACA-3', with 5'-GTAAACA-3' being the preferred binding site.
Subcellular location: Nucleus {ECO:0000255, ECO:0000305}.
Interaction partners:
Sequence:
MLGAVKMEGHEATDWSSYYGEAEAYSSVGNMNAGLSMNPMNTYMSMSAMRTSANMTASSMNMSYVNTGMSPSLTGMSPGTGAMTGMGTGVPSMASHLSPSMIPMSAQTTAMNALAPYTNINSMSPIYGQSNINRSRDPKTYRRSYTHAKPPYSYISLITMAIQQSPNKMLTLSEIYQWIMDLFPFYRQNQQRWQNSIRHSLSFNDCFLKVPRSPDKPGKGSFWTLHPDSGNMFENGCYLRRQKRFKCEKKPSLREGGGKKLSEGASSVGSAANSSSESSVGNESPHSSSSPCQEQKRSLVDMKSSQGLSPKHATSPASQAQHLLSQHHSVLSHEAQSHLKPEHHYSFNHPFSINNLMSSEQQHHHHHHHNHHHHHKMDLKAYEQVMHYSSYGSPMAGSLAMSTVTNKSGLESSPITSDTSYYQGGYSRPIMNSS
Protein: Neuronal vesicle trafficking-associated protein 1 (M234) (Neuron-enriched endosomal protein of 21 kDa) (Neuron-specific protein family member 1) (p21) (Q62092)
Organism: Mus musculus (Mouse)
Function: Plays a role in the recycling mechanism in neurons of multiple receptors, including AMPAR, APP and L1CAM and acts at the level of early endosomes to promote sorting of receptors toward a recycling pathway. Regulates sorting and recycling of GRIA2 through interaction with GRIP1 and then contributes to the regulation of synaptic transmission and plasticity by affecting the recycling and targeting of AMPA receptors to the synapse. Is required for faithful sorting of L1CAM to axons by facilitating trafficking from somatodendritic early endosome or the recycling endosome (By similarity). In an other hand, induces apoptosis via the activation of CASP3 in response to DNA damage (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:P02683}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P02683}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P02683}. Endosome membrane {ECO:0000250|UniProtKB:P02683}. Cell projection, dendrite {ECO:0000250|UniProtKB:P02683}. Early endosome membrane {ECO:0000250|UniProtKB:P02683}. Late endosome membrane {ECO:0000269|PubMed:28874679}. Lysosome lumen {ECO:0000250|UniProtKB:P02683}. Recycling endosome membrane {ECO:0000250|UniProtKB:P02683}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P02683}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P02683}. Endosome, multivesicular body membrane {ECO:0000250|UniProtKB:P02683}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P42857}. Note=Endocytosed from the cell surface, thus enters into early endosomes, trafficks to late endosomes and degradates in lysosomes (By similarity). Endoplasmic reticulum targeting is essential for apoptosis (By similarity). Found in both stationary and motile endosomes (PubMed:28874679). A previous study supports a type I membrane protein topology (PubMed:12070131). {ECO:0000250|UniProtKB:P02683, ECO:0000250|UniProtKB:P42857, ECO:0000269|PubMed:12070131, ECO:0000269|PubMed:28874679}.
Interaction partners:
- Syntaxin-12
Sequence:
MVKLGNNFAEKGTKQPLLEDGFDTIPLMTPLDVNQLQFPPPDKVVVKTKTEYEPDRKKGKARPPKIAEFTVSITEGVTERFKVSVLVLFALAFLTCVVFLVVYKVYKYDRACPDGFVLKNTQCIPEGLESYYTEQDSSAREKFYTVINHYNVAKQSITRSVSPWMSVLSEEKLSEQETEAAEKSA
Protein: Peroxisomal N(1)-acetyl-spermine/spermidine oxidase (EC 1.5.3.13) (Polyamine oxidase) (Q6QHF9)
Organism: Homo sapiens (Human)
Function: Flavoenzyme which catalyzes the oxidation of N(1)-acetylspermine to spermidine and is thus involved in the polyamine back-conversion. Can also oxidize N(1)-acetylspermidine to putrescine. Substrate specificity: N(1)-acetylspermine = N(1)-acetylspermidine > N(1),N(12)-diacylspermine >> spermine. Does not oxidize spermidine. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs.
Subcellular location: Peroxisome {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Diamine acetyltransferase 1
- Thialysine N-epsilon-acetyltransferase
- Spermine synthase
- Spermidine synthase
- Ornithine decarboxylase
- Glycine N-acyltransferase-like protein 1
- Diamine oxidase [copper-containing]
- Antizyme inhibitor 2
Sequence:
MESTGSVGEAPGGPRVLVVGGGIAGLGAAQRLCGHSAFPHLRVLEATARAGGRIRSERCFGGVVEVGAHWIHGPSRGNPVFQLAAEYGLLGEKELSQENQLVETGGHVGLPSVSYASSGASVSLQLVAEMATLFYGLIDQTREFLHAAETPVPSVGEYLKKEIGQHVAGWTEDEETRKLKLAVLNSFFNLECCVSGTHSMDLVALAPFGEYTVLPGLDCTFSKGYQGLTNCMMAALPEDTVVFEKPVKTIHWNGSFQEAAFPGETFPVSVECEDGDRFPAHHVIVTVPLGFLREHLDTFFDPPLPAEKAEAIRKIGFGTNNKIFLEFEEPFWEPDCQLIQLVWEDTSPLEDAAPELQDAWFRKLIGFVVLPAFASVHVLCGFIAGLESEFMETLSDEEVLLCLTQVLRRVTGNPRLPAPKSVLRSRWHSAPYTRGSYSYVAVGSTGGDLDLLAQPLPADGAGAQLQILFAGEATHRTFYSTTHGALLSGWREADRLLSLWAPQVQQPRPRL
Protein: 26S proteasome non-ATPase regulatory subunit 12 homolog B (26S proteasome regulatory subunit RPN5b) (AtRPN5b) (26S proteasome regulatory subunit p55 homolog B) (Q8VWK0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins (By similarity). Acts redundantly with RPN5A.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19252082}. Nucleus {ECO:0000269|PubMed:19252082}.
Interaction partners:
- 26S proteasome regulatory subunit 6A homolog B
- 26S proteasome regulatory subunit 8 homolog A
- 26S proteasome non-ATPase regulatory subunit 1 homolog A
- 26S proteasome non-ATPase regulatory subunit 7 homolog A
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome non-ATPase regulatory subunit 7 homolog B
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- 26S proteasome regulatory subunit 4 homolog B
- 26S proteasome non-ATPase regulatory subunit 1 homolog B
- 26S proteasome non-ATPase regulatory subunit 3 homolog B
Sequence:
MEESRQLESSIDRLLNEEKQMRLAENVAGTRKAATEILKLCFEAKDWKLLNEQILNLSKKRGQLKQAVQSMVQQAMQYIDQTLDIETRIELIKTLNNVAAGKIYVEIERARLTKMLAKIKEEQGLIAEAADLMQEVAVETFGAMAKTEKIAFILEQVRLCLDQKDFVRAQILSRKINPRVFDADTTKEKKKPKEGENMVEEAPADIPTLLVLKRIYYELMIRYYSHNNEYIEICRSYKAIYDIPSVKENPEQWIPVLRKICWFLALAPHDPMQSSLLNATLEDKKLSEIPDFKMLLKQIVTMEVIQWTSLWNKYKDEFENEKNMIGGSLGDKAGEDLKLRIIEHNILVVSKYYSRITFKRLAELLCLTTEEAEKHLSEMVVSKALIAKIDRPSGIICFQIVKDSNEILNSWATNLEKLLDLVEKSCHQIHKETMVHKVALRA
Protein: Protein tyrosine phosphatase PRL-1 (EC 3.1.3.48) (Q4QEZ7)
Organism: Leishmania major
Function: Has protein tyrosine phosphatase activity and may act as a virulence factor to support intracellular survival in host macrophages.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28507071}. Mitochondrion matrix, kinetoplast {ECO:0000269|PubMed:28507071}. Secreted, extracellular exosome {ECO:0000269|PubMed:28507071}. Secreted {ECO:0000269|PubMed:28507071}. Note=Enriched around the kinetoplast. {ECO:0000269|PubMed:28507071}.
Interaction partners:
Sequence:
MEVNATLIDCCDPQKPSRVLFHFLILDAPSPSNLPTYIKELQHRGVRHLVRVCGPTYDATLVKSRGIDVHSWPFDDGAPPTRAVLDSWLKLLDTELARQQEDPSVPPPTIGVHCVAGLGRAPILVALALVEYGNVSALDAIALIREKRKGAINQTQMHWITKYKRRHQGAGCVIM
Protein: ADP-ribosylation factor like GTPase 13B (A0A8I5ZXD0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MFNLMANCCNLFKRWREPVRKVTLVMVGLDNAGKTATAKGIQGEHPEDVAPTVGFSKIDLRQGKFEVTIFDLGGGKRIRGIWKNYYAESYGVIFVVDSSDEDRMEETKETMSEVLRHPRISGKPILVLANKQDKEGALGEADVIECLSLEKLVNEHKCLCQIEPCSAVLGYGKKIDKSIKKGLYWLLHIIAKDFDALSERIQKDTTEQRALEEQEKCERAERVRKLREEREQEQTELDGTSGLAEMDSGPVLTNPFQPIAAVIIENEKKQEKEKKKKTAEKDSDVGHPEHKGEQEGAESQNEAGGCLRNPHRDVVNSYKEALSQQLDNEDELDQRVSEPGDNSKKKTKKLRMKRSHRVEPVNTDESAPKSPTPPPPPPPDFYGKPLPPLAVRQRPNGDAQDMIS
Protein: Uncharacterized protein (Q9CR07)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
IDLYTKIRKKASERELMIAGRIFGMVLIAVSILWVPLVQVSQNGQLFHYIGSVSSYLGPPLGAVFMLAIFFKRVNEQGAFWGLMVGLVVGLIRLIAEFVYGTGSCVAPSNCPKIICGVHYMYFAIILFFVSIIVILGVSFLTEPIPDVHLYRLCWSLWNNTEERIDLDAEELETQEEAGGALEEDSEQSRGCLKRACCLLCGLQNTGPKLTKEEEAALRQKFSDTSEKPLWRTVMNINAVLLLGVAVFVHAYFA
Protein: Uncharacterized helicase C17H9.02 (EC 3.6.4.-) (O13799)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- NURS complex subunit red1
- Uncharacterized protein C7D4.14c
- Uncharacterized RNA-binding protein C902.04
- NURS complex subunit pir2
- Zinc finger CCCH domain-containing protein C337.12
- Protein NRDE2 homolog
- Poly
- Ribosome biogenesis protein NOP53
- ATP-dependent RNA helicase mtr4
- RNA binding exosome specificity factor Mmi1
Sequence:
MSENSTDSKNFQFSEGSRESSNDELKVLLRDTETKEDEKSSFSNSEEESIIENLSDSSVNKEYAKNSLKLSDAVSESKYLNPLLKDKRHDRSFALHKVVVPDDYDYIPLNKHIPSDPPAKTYPFELDPFQSTAIKCVERMESVLVSAHTSAGKTVIAEYAIAQALKNRQRVIYTSPIKSLSNQKYRELLSEFGDVGLMTGDVSINPSASCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVHYMRDKDRGVVWEETLILLPDAIRFIFLSATLPNALQFARWISEIHKQPCHVVYTDYRPTPLQHFIYPQGADGIYMLVDEKNKFKTENFKKVLEVLDHSTRQENYSKSSKKVKKSSSLERIINMVLSNRYDPIIVFCFSKKECEINAHQFGKLDLNDTENKELVTEIFDSAINQLSEEDRGLRQFEEMRSLLLRGIGIHHSGLLPILKELVEILFQEGLVRILFATETFSIGLNMPARTVLFTKAQKFSGNNFRWLTSGEYMQMSGRAGRRGIDTKGLSIVILDQSIDEQAARCLMNGQADVLNSAFHLSYGMILNLMRIEEISPEDILKKSFYQFQNMESLPLIKEELMQLKNEETSINIPNETAVKEFHDLKLQLEKYGEEIQKVMTHPDNCLPYLQSGRLIQIKLGGIIFPWGVLVNVIKREFDPNTREQVAPHETYVLDVLLPISSNSMSNHKVNPSILVPPRPNETPLYEIVSVLLTAVCNISSIRIYMPRELNSNESKLRAYRRVNEVIEEFKEIPYLDPLEHMHIESSTLSLSLRKLEILEPKLFDSPYYKDSKHRAEYHEFRKKLNLRAQIKDISTKITNTEAIIQLRELKIRQRVLRRLGFCTLENVIDIKGRVACEITSGDELLLVELIFQGFFNQMPPEEIAAALSCFVYEDKSEVSTLNLKEPFKKMYLTIIEAAKRIATVSLESKLQFNESDYLHQFKPDIMEPVSLWINGASFQEICIVSKLYEGSIVRTFRRLDELLKQLEHAAIVLGNNELKEKSVLTEQKLHRDIIFSASLYL
Protein: D-arabitol-phosphate dehydrogenase (APDH) (EC 1.1.1.301) (Q8KQL2)
Organism: Enterococcus avium (Streptococcus avium)
Function: Involved in the arabitol catabolism via the arabitol phosphate route. Catalyzes only the transformation of D-arabitol 1-phosphate (Arb1P) and D-arabitol 5-phosphate (Arb5P) into D-xylulose 5-phosphate (Xlu5P) and ribulose 5-phosphate, respectively. It can use both NAD and NADP.
Interaction partners:
Sequence:
MSKTMKGVSKQAPGYDQMAFIDLSVPEATDDKVLIKVAYTGICGSDIHTFKGEYKNPTTPVVLGHEFSGQVVEVGANVPKVKVGDRVTSETTFYVCGECDYCKEKQYNLCPHRKGIGTQQNGSMANYVLAREESIHLLPDHLSYEGAAMSEPLACCVHAMYQKSHLELKDTIIIMGPGPIGLYLLQIAKEIGAFVIMTGITKDAHRLALAKKLGADVIVDTMKEDLAKVVNEITDGYGVDKVYDASGAVPAVNASLPLIRKQGQFIQVGLFANKMVDLDTESIIQREIEYIGSRSQNPYDWPIAIHLLAKGAINIDEMITKKYPLTEWREAFDKVMEGNEIKVMIESNPEEF
Protein: Exocyst complex component 3-like 2 (D3YUP5)
Organism: Mus musculus (Mouse)
Interaction partners:
- Exocyst complex component 4
- Exocyst complex component 5
- Exocyst complex component 2
- Exocyst complex component 8
- Exocyst complex component 7
- Exocyst complex component 1
- Exocyst complex component 6
- Exocyst complex component 1-like
- Exocyst complex component 6B
- 3',5'-cyclic-AMP phosphodiesterase 7B
Sequence:
MPILKSLGVGDPKVPRAGTLPLRSSRNPFEDTPTLEEEDAELGTLPNGTSCRRRATLEKLAGLAPFRLGWTSGRRAGSPGDGQVRSFLGRVLAPGIRRSSADFGLLNRLQGFRTHGDEEPAGEAARRLAFLRLGRGPKPRRASLAERLVPAGEAAPEPPPKVPEPPKIKEPLSVLEILGLIQRRELARADEHILELEAEAPTAEAEAGAGRRARDVALLYEALQRELWALVRESLASPGPGTGAVSQLGLVLLQEEAADARRGPGAARKLRTHWAEAVARAARERLEEAAAPGARGALAGQLEALRARLLEDVAAVRGRLAPAYPAGLRAGAVYLRGYHEALAEWLGAAARRRLPLADRYALLHWHNHVYPREILGLVDLVALENGELGPLLSAGTLRGLEDECVTDVKAQTRAALLRVLQEDEEQWGSMDYRPSNLAQDVCELLEEHTERAPHISQEFVERMAYCCLGGLAEFLQSFQQRVERFHENPGIRELPSDTYISRTISMVNCGPPLRSLAERLARVGPPESEPAREASAIALDRVTRLCHRVLAELLFQELQPHFNKLMRRKWLSSSEALDGIVGTLGAQALALRRMQDEPYQVLVAELHRRALVEYVRPLLRGRLRCRSARTRSRVAGRLREDAAQLQRLFRRLESQAYWLDQVVPHLAEILQLEDTPSIQVEVGVLVRDYPDIRRKHVAALLDIRGLRNTAARQEILAVARDLELSESGALPPSRDRAFFADIPVPRTSFCLGLPLLLGRLPVSRLARPNLACLPLRPRPPSPVRARADR
Protein: Synapsin-2 (Synapsin II) (Q64332)
Organism: Mus musculus (Mouse)
Function: Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. May play a role in noradrenaline secretion by sympathetic neurons.
Subcellular location: Synapse.
Interaction partners:
- Synaptosomal-associated protein 25
- Vesicle-associated membrane protein 2
- Syntaxin-1A
- Complexin-1
- Synaptosomal-associated protein 23
- Vesicle-associated membrane protein 4
- Beta-soluble NSF attachment protein
- Syntaxin-4
- Syntaxin-3
- Vesicle-associated membrane protein 8
Sequence:
MMNFLRRRLSDSSFIANLPNGYMTDLQRPEPQQPPPAPGPGAATASAATSAASPGPERRPPPAQAPAPQPAPQPAPTPSVGSSFFSSLSQAVKQTAASAGLVDAPAPSAASRKAKVLLVVDEPHTDWAKCFRGKKILGDYDIKVEQAEFSELNLVAHADGTYAVDMQVLRNGTKVVRSFRPDFVLIRQHAFGMAENEDFRHLVIGMQYAGLPSINSLESIYNFCDKPWVFAQMVAIFKTLGGEKFPLIEQTYYPNHREMLTLPTFPVVVKIGHAHSGMGKVKVENHYDFQDIASVVALTQTYATAEPFIDAKYDIRVQKIGNNYKAYMRTSISGNWKTNTGSAMLEQIAMSDRYKLWVDACSEMFGGLDICAVKAVHGKDGKDYIFEVMDCSMPLIGEHQVEDRQLITDLVISKMNQLLSRTPALSPQRPLTTQQPQSGTLKEPDSSKTPPQRPPPQGGPGQPQGMQPPGKVLPPRRLPSGPSLPSSSSSSSSSSSSSSAPQRPGGPTTTHGDASSSSNSLAEAQAPQAAPAQKPQPHPQLNKSQSLTNAFSFSESSFFRSSANEDEAKAETIRSLRKSFASLFSD
Protein: Beclin-1 [Cleaved into: Beclin-1-C 35 kDa; Beclin-1-C 37 kDa] (Q4A1L4)
Organism: Bos taurus (Bovine)
Function: Plays a central role in autophagy. Acts as core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2. Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis. May play a role in antiviral host defense (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O88597}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Endosome membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. Note=Interaction with ATG14 promotes translocation to autophagosomes. Expressed in dendrites and cell bodies of cerebellar Purkinje cells. {ECO:0000250|UniProtKB:O88597, ECO:0000250|UniProtKB:Q14457}.; SUBCELLULAR LOCATION: [Beclin-1-C 35 kDa]: Mitochondrion {ECO:0000250|UniProtKB:O88597, ECO:0000250|UniProtKB:Q14457}. Nucleus {ECO:0000250|UniProtKB:Q14457}. Cytoplasm {ECO:0000250|UniProtKB:Q14457}.; SUBCELLULAR LOCATION: [Beclin-1-C 37 kDa]: Mitochondrion {ECO:0000250|UniProtKB:O88597}.
Interaction partners:
- Activating molecule in BECN1-regulated autophagy protein 1
- Autophagy related 14
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- UV radiation resistance associated
- Apoptosis regulator Bcl-2
- Phosphoinositide 3-kinase regulatory subunit 4
- Nuclear receptor-binding factor 2
- ULK2 protein
- non-specific serine/threonine protein kinase
- RB1-inducible coiled-coil protein 1
Sequence:
MEGSKTSSSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLATAQLKPGETQEEEANSGEEPFIETRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLGLELKELALEEERLIQELEDVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQMQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK
Protein: XIAP associated factor 1 (D3ZPQ3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- E3 ubiquitin-protein ligase XIAP
Sequence:
MEDDFQVCRNCKRSVASSHFTLHEAHCLRFLVLCPECEEPIPESKMKEHVEAVHQQTKESQQDPAECKFCELAVQLSKLDVHEYHCGSRTEHCPHCNQRVILRVLAQHKDLCLSAKGKPKEGKRAVSPGRKTRCDICKQMIPEHKYASHMKQCSAPRTVTYLRDGRTVVLPSTLPLMNTGNQTSTVSKDVRPKTKNRNSSTKRETKDQSGAVDLPLKSRLQQRTALPKGEETAYDILRKCRQCRILLPLPILNEHQEKCLRLAQQKKLVRRASWILKSTSSQ
Protein: Baculoviral IAP repeat-containing protein 5 (Apoptosis inhibitor 4) (Apoptosis inhibitor survivin) (TIAP) (O70201)
Organism: Mus musculus (Mouse)
Function: Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis (By similarity). Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules (By similarity). Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis (By similarity). The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules (By similarity). May counteract a default induction of apoptosis in G2/M phase (By similarity). The acetylated form represses STAT3 transactivation of target gene promoters (By similarity). May play a role in neoplasia. Inhibitor of CASP3 and CASP7 (By similarity). Essential for the maintenance of mitochondrial integrity and function.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O15392}. Nucleus {ECO:0000250|UniProtKB:O15392}. Chromosome {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere {ECO:0000250|UniProtKB:O15392}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O15392}. Midbody {ECO:0000250|UniProtKB:O15392}. Note=Localizes at the centromeres from prophase to metaphase, at the spindle midzone during anaphase and a the midbody during telophase and cytokinesis. Accumulates in the nucleus upon treatment with leptomycin B (LMB), a XPO1/CRM1 nuclear export inhibitor (By similarity). Localizes on chromosome arms and inner centromeres from prophase through metaphase. Localizes to kinetochores in metaphase, distributes to the midzone microtubules in anaphase and at telophase, localizes exclusively to the midbody. Colocalizes with AURKB at mitotic chromosomes. Acetylation at Lys-129 directs its localization to the nucleus by enhancing homodimerization and thereby inhibiting XPO1/CRM1-mediated nuclear export (By similarity). {ECO:0000250|UniProtKB:E3SCZ8, ECO:0000250|UniProtKB:O15392}.
Interaction partners:
- Inner centromere protein
- Aurora kinase B
- Borealin
- Aurora kinase A
- Ubiquitin-conjugating enzyme E2 C
- G2/mitotic-specific cyclin-B1
- Cyclin-dependent kinase 1
- Diablo IAP-binding mitochondrial protein
- G2/mitotic-specific cyclin-B2
- Caspase-3
Sequence:
MGAPALPQIWQLYLKNYRIATFKNWPFLEDCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDNPIEEHRKHSPGCAFLTVKKQMEELTVSEFLKLDRQRAKNKIAKETNNKQKEFEETAKTTRQSIEQLAA
Protein: HTH-type transcriptional regulator PgrR (Regulator of PG recycling) (P77333)
Organism: Escherichia coli (strain K12)
Function: Regulates the expression of genes involved in peptidoglycan (PG) degradation. Could play a role in switch control between recycling and degradation of PG peptides. Negatively regulates the expression of the ycjY-ymjD-ymjC-mpaA operon by binding to the PgrR-box. In addition, other genes are predicted to be under the control of PgrR, including genes related to membrane formation and function.
Interaction partners:
- Uncharacterized protein YcjY
- Periplasmic murein peptide-binding protein MppA
- Hca operon transcriptional activator HcaR
Sequence:
MKREEIADLMAFVVVAEERSFTRAAARLSMAQSALSQIVRRIEERLGLRLLTRTTRSVVPTEAGEHLLSVLGPMLHDIDSAMASLSDLQNRPSGTIRITTVEHAAKTILLPAMRTFLKSHPEIDIQLTIDYGLTDVVSERFDAGVRLGGEMDKDMIAIRIGPDIPMAIVGSPDYFSRRSVPTSVSQLIDHQAINLYLPTSGTANRWRLIRGGREVRVRMEGQLLLNTIDLIIDAAIDGHGLAYLPYDQVERAIKEKKLIRVLDKFTPDLPGYHLYYPHRRHAGSAFSLFIDRLKYKGAV