wanglab/gogpt-training-data huggingface dataset:
Protein: AP-3 complex subunit delta (Adaptor-related protein complex 3 subunit delta) (Delta-adaptin) (Q54WN0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Part of the AP-3 complex, an adaptor-related complex which is essential for the compartmentalization of the endocytic pathway.
Subcellular location: Endosome membrane {ECO:0000250}.
Interaction partners:
- AP-3 complex subunit beta
- AP-3 complex subunit mu
- AP-3 complex subunit sigma
- AP-2 complex subunit mu
- AP-2 complex subunit sigma
- Arpin
- AP-1 complex subunit beta
- AP-1 complex subunit mu
- AP-2 complex subunit alpha-2
- Epidermal growth factor receptor substrate 15 homolog
Sequence:
MFERTLVDLIRGIRNHKKNETKFINQCINEIKEELKGDMQKKTVAVQKLTYIQMLGFDISWASFKIVEVMSCNKFSSKRIGYLAASQSFNEGTDVIVLATHQIRKDFLSSNQSEAYLALNCLSNICTTDLARELANDILTLLSTQKTHILKRAITVLYKIFLRYPESLRPAFPKLREKLDDPEPSVVSCSVNVICELARRNPKNYLPLAPVLFRILTNTTNNYWMLIKIVKLFAALTPHEPRLGKKLIDPLTNIINSSPSVSLLYECIQTCITGMSDHIPLMKLCISKLRTLIEHNDQNLKYLGLLALNNIMKIHPKAVSEHRDLVLNCLEDDDISIRLRALDLLPGMTSKKNIGDIVFKLLDHLDNAEGQYKEQIIEKIIELCSMGTYQFITDFEWYINILVKLSQIQDSIHGKLIASQLLDVVIRVKIVRAYSTRQMIELLKNPKLMSNPTEGGMCEVLYAAAWIVGEFSGYVNRPIDALEAFLQPRVCVLPSHIQSVYMLNSLKVFSHACAKANGDKIPSLDDDDEEEEAQEEEDQNEITHEIVQECLEIIKSRLTIFTHSIYLNVQERACLINELLSFYTVTKEQGNNISKELISLFTEQLNPVGPKAQKKVPIPEGLDLDEWINDPKHQEPIEEDEDDDIFNTSTSSHQKKHHKHHRGGYDGDDDEDDETNSSHSGHSSSNFNRHPIDIQRQKEERLRKQANNPYMLGGKVSKKLSTNDPENIPVVQLTGDLGHLHVGASSNRPMPSKGSKKTKKHYTIDTTTEMPEGAKESDDEDEKDNKYKNDALSNINLSEPLTASDVLHTSRHRTDIIKEKEREMAMLAKKNAKLSPKSPPSTANYSEVTSPEIAPAKKATKKAAAGSNPPPPPTAKKSSKKPAATSSTTTTTKSTQAAAAVVAPPPVIVKKVLKTILDDDNFKITCEILKVSPSNETDNNQIKLTMKVQNKTDEDMSDVSISLKNPAEQCVSIKNSGEIGVLEADASTTHTELLNVVNVLNSQELQFTLLASPSSSPSITNQLSIDLPFSFFIVATKLPKDKFAEILQKSGQVSAMDSTKITGQSLTMPLVIEKLAQQLSIEVVQAHPNGQTASFYAKTTQNHHIAMLVKEKDGNISFDIKSPQSLLNQILVKEIAQLTFSSK
Protein: Meiotic coiled-coil protein 3 (Meiotically up-regulated gene 7 protein) (Q9UTR7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Meiotically up-regulated gene 5 protein
- Reduced meiotic recombination protein C1442.04c
- Meiotic coiled-coil protein 4
- Meiotic expression up-regulated protein 23
Sequence:
MTKETHENHLRTHNGIFPVSLLSTQARQLLNFKLKSPSYYLLNSFKLLVKSEGNNQSTTADVTLTKSPNAYHASSAREEKDLQVSRRDTCFYCSRKIIKCICNEEHVGIESVQLKLILLLCQNLPNVTTNAKKYFSSLADGHNFTLTLYKFSLDNQTFSQLLSRFKSFATLTELLQVHNVMLQVNFSFQARQLNTEIQLRRCHSLEKTWKFLFGDYELPDVLKDMESSNSDWSDTSLKRIAYLCSLVEELKLHSSIMNDKYVCLVSKHNNALEDKFNSEAARQLLQKSLSIVASNLKQAENKTISYEEKLSIAQNSINEIQTQNRDLKLETEKLQDQIKALLERNQSLQEALETVKNDEKNLREMNANYETEMKEARQKLNNKEALISHYDDDFRAKELKISRLSESLREKAGLLEFQSSVSEQRDLLYQEQIQSSIKDMENVFRKNEYLMEELNELKNNLEVESSKVLRLDEEMKCLKDEQLSQFDTVFSLTDERDGLQKDLKNTKGNLDDEIGRSAFLKSQIRDQELTIEKLHDSLETLSQTNNSLQCEISEKNAELNSVNSKLSEGRAHLETANKENEILKQQLELSESKLASLLNSYQSFINKKEHLYSFLQLVEPSFAKSDSSNATESQISESVRKGISIFNLLFIVYKNVCSQAGINPSTKLEDLDEHTLSDELTYITKKFVQKDQEYQTKEIELRNYKITLQSLLEDKLIGVNTDCRSPSCSDFEQLGQESENNTSISGRVSKLVKSFNDSSSISNNTKISITKSPSGEKVSVFKEMSDIALRDMDKNRKLLGENVDVRNIVVQKDESLNIDLQNNAVVPELHFKEGMVYDSLENAYTYLAESKRMLANELQMKQEDLEKVILELEAYKEIFLEEKQIPCEEFMPGKNAKSEKSLRSVFQEQLMRETKRVRKLEKVNSELKLHCFELSERLREREHTLQQTFGDK
Protein: Pumilio homolog 1 (Q5T1Z8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, P-body {ECO:0000256|ARBA:ARBA00004201}. Cytoplasmic granule {ECO:0000256|ARBA:ARBA00004463}.
Interaction partners:
Sequence:
MPLPPPGPGPEPIPGCTAPTQSPVGRHVVGVKGVGGMSVACVLKRKAVLWQDSFSPHLKHHPQEPANPNMPVVLTSGTGSQAQPQPAANQALAAGTHSSPVPGSIGVAGRSQDDAMVDYFFQRQHGEQLGGGGSGGGGYNNSKHRWPTGDNIHAEHQVRSMDELNHDFQALALEGRAMGEQLLPGKKFWETDESSKDGPKGIFLGDQWRDSAWGTSDHSVSQPIMVQRRPGQSFHVNSEVNSVLSPRSESGGLGVSMVEYVLSSSPGDSCLRKGGFGPRDADSDENDKGEKKNKGTFDGDKLGDLKEEGDVMDKTNGLPVQNGIDADVKDFSRTPGNCQNSANEVDLLGPNQNGSEGLAQLTSTNGAKPVEDFSNMESQSVPLDPMEHVGMEPLQFDYSGTQVPVDSAAATVGLFDYNSQQQLFQRPNALAVQQLTAAQQQQYALAAAHQPHIGLAPAAFVPNPYIISAAPPGTDPYTAGLAAAATLGPAVVPHQYYGVTPWGVYPASLFQQQAAAAAAATNSANQQTTPQAQQGQQQVLRGGASQRPLTPNQNQQGQQTDPLVAAAAVNSALAFGQGLAAGMPGYPVLAPAAYYDQTGALVVNAGARNGLGAPVRLVAPAPVIISSSAAQAAVAAAAASANGAAGGLAGTTNGPFRPLGTQQPQPQPQQQPNNNLASSSFYGNNSLNSNSQSSSLFSQGSAQPANTSLGFGSSSSLGATLGSALGGFGTAVANSNTGSGSRRDSLTGSSDLYKRTSSSLTPIGHSFYNGLSFSSSPGPVGMPLPSQGPGHSQTPPPSLSSHGSSSSLNLGGLTNGSGRYISAAPGAEAKYRSASSASSLFSPSSTLFSSSRLRYGMSDVMPSGRSRLLEDFRNNRYPNLQLREIAGHIMEFSQDQHGSRFIQLKLERATPAERQLVFNEILQAAYQLMVDVFGNYVIQKFFEFGSLEQKLALAERIRGHVLSLALQMYGCRVIQKALEFIPSDQQVINEMVRELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFALSTHPYGCRVIQRILEHCLPDQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVAEIRGNVLVLSQHKFASNVVEKCVTHASRTERAVLIDEVCTMNDGPHSALYTMMKDQYANYVVQKMIDVAEPGQRKIVMHKIRPHIATLRKYTYGKHILAKLEKYYMKNGVDLGPICGPPNGII
Protein: Mitochondrial fission regulator 1 (Chondrocyte protein with a poly-proline region) (Q15390)
Organism: Homo sapiens (Human)
Function: May play a role in mitochondrial aerobic respiration. May also regulate mitochondrial organization and fission (By similarity).
Subcellular location: Mitochondrion {ECO:0000250}. Note=May be associated with the inner and the outer mitochondrial membrane. {ECO:0000250}.
Interaction partners:
- BPI fold-containing family A member 2
- Ras GTPase-activating protein 1
- Gem-associated protein 5
Sequence:
MLGWIKRLIRMVFQQVGVSMQSVLWSRKPYGSSRSIVRKIGTNLSLIQCPRVQFQINSHATEWSPSHPGEDAVASFADVGWVAKEEGECSARLRTEVRSRPPLQDDLLFFEKAPSRQISLPDLSQEEPQLKTPALANEEALQKICALENELAALRAQIAKIVTQQEQQNLTAGDLDSTTFGTIPPHPPPPPPPLPPPALGLHQSTSAVDLIKERREKRANAGKTLVKNNPKKPEMPNMLEILKEMNSVKLRSVKRSEQDVKPKPVDATDPAALIAEALKKKFAYRYRSDSQDEVEKGIPKSESEATSERVLFGPHMLKPTGKMKALIENVSDS
Protein: RNase adapter protein RapZ (P0A894)
Organism: Escherichia coli (strain K12)
Function: Modulates the synthesis of GlmS, by affecting the processing and stability of the regulatory small RNA GlmZ. When glucosamine-6-phosphate (GlcN6P) concentrations are high in the cell, RapZ binds GlmZ and targets it to cleavage by RNase E. Consequently, GlmZ is inactivated and unable to activate GlmS synthesis. Under low GlcN6P concentrations, RapZ is sequestered and inactivated by an other regulatory small RNA, GlmY, preventing GlmZ degradation and leading to synthesis of GlmS. Displays ATPase and GTPase activities in vitro. Can also hydrolyze pNPP.
Interaction partners:
- Phosphocarrier protein NPr
- Glutamine--fructose-6-phosphate aminotransferase
- Ribonuclease E
- Ribosome hibernation promoting factor
- Nitrogen regulatory protein
- Putative gluconeogenesis factor
- RNA polymerase sigma-54 factor
- Ribonuclease G
- Phosphoglucosamine mutase
- RNA-binding protein Hfq
Sequence:
MVLMIVSGRSGSGKSVALRALEDMGFYCVDNLPVVLLPDLARTLADREISAAVSIDVRNMPESPEIFEQAMSNLPDAFSPQLLFLDADRNTLIRRYSDTRRLHPLSSKNLSLESAIDKESDLLEPLRSRADLIVDTSEMSVHELAEMLRTRLLGKRERELTMVFESFGFKHGIPIDADYVFDVRFLPNPHWDPKLRPMTGLDKPVAAFLDRHTEVHNFIYQTRSYLELWLPMLETNNRSYLTVAIGCTGGKHRSVYIAEQLADYFRSRGKNVQSRHRTLEKRKP
Protein: PHD finger-like domain-containing protein 5A (PHF-5) (G5EBY6)
Organism: Caenorhabditis elegans
Interaction partners:
- PSP proline-rich domain-containing protein
- Splicing factor 3B subunit 3
- Splicing factor 3B subunit 6-like protein
- Splicing factor 3B subunit 1 domain-containing protein
- Splicing factor 3B subunit 4
- Protein moa-2
- Splicing factor 3A subunit 2
- RRM domain-containing protein
- Probable small nuclear ribonucleoprotein G
- Protein BUD31 homolog
Sequence:
MAKHHPDLIFCRKQPGIAIGRLCEKCDGRCVICDSHVRPCTLVRICEECNYGSYQGRCVICGGAGVSDAYYCKECTILEKDRDGCPKIVNLGSAKTDLFYERKKFGSKKS
Protein: Sperm flagellar protein 1 (Q9Y4P9)
Organism: Homo sapiens (Human)
Function: Microtubule-associated protein involved in the stabilization of microtubules along the axis of migration during radial intercalation. Promotes the establishment and stabilization of an axis of microtubules required for the active migration of cells into the outer epithelium (By similarity). Microtubule-associated protein that promotes microtubule bundling and stabilizes microtubules against depolymerization in response to cold shock (By similarity). Essential for ciliary central apparatus formation which requires both its microtubule-binding and bundling activities and for ciliary localization of HYDIN and SPAG6 in ependymal cilia (By similarity). Binds actin in intestinal epithelial cells (IECs), essential for IECs survival and contributes to formation of filopodia and lamellipodia in migrating IECs. Regulates planar cell polarity signaling pathway and asymmetric microtubule accumulation in ciliated epithelia (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:31473225}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q99JL1}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q0IH24}. Apical cell membrane {ECO:0000269|PubMed:31473225}. Basolateral cell membrane {ECO:0000269|PubMed:31473225}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:31473225}. Cell projection, microvillus {ECO:0000269|PubMed:31473225}. Cell projection, lamellipodium {ECO:0000269|PubMed:31473225}. Cell projection, filopodium {ECO:0000269|PubMed:31473225}. Note=Present in the tails of developing and epididymal sperm, internal to the fibrous sheath and around the outer dense fibers of the sperm flagellum. Also found at the apical tip of cilia (By similarity). Colocalizes with TJP1 and CGN at sites of cell-cell contact in intestinal epithelial cells (PubMed:31473225). {ECO:0000250|UniProtKB:Q0IH24, ECO:0000269|PubMed:31473225}.
Interaction partners:
- Microtubule-associated protein RP/EB family member 3
- Microtubule-associated protein RP/EB family member 1
- Calponin-1
Sequence:
MASSVDEEALHQLYLWVDNIPLSRPKRNLSRDFSDGVLVAEVIKFYFPKMVEMHNYVPANSLQQKLSNWGHLNRKVLKRLNFSVPDDVMRKIAQCAPGVVELVLIPLRQRLEERQRRRKQGAGSLQELAPQDGSGYMDVGVSQKARGEGVPDPQGGGQLSWDRPPAPRPPAYNRALQGDPSFVLQIAEKEQELLASQETVQVLQMKVRRLEHLLQLKNVRIEDLSRRLQQAERKQR
Protein: Laminin subunit beta-2 (Laminin-11 subunit beta) (Laminin-14 subunit beta) (Laminin-15 subunit beta) (Laminin-3 subunit beta) (Laminin-4 subunit beta) (Laminin-7 subunit beta) (Laminin-9 subunit beta) (S-laminin subunit beta) (S-LAM beta) (Q61292)
Organism: Mus musculus (Mouse)
Function: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane.
Interaction partners:
- Laminin subunit gamma-2
- Laminin subunit gamma-1
- Laminin subunit alpha-3
- Laminin subunit alpha-5
- Laminin subunit gamma-3
- Laminin subunit alpha-1
- Peripheral myelin protein 22
- Laminin subunit alpha-2
- Laminin subunit beta-1
- Laminin subunit alpha-4
Sequence:
MEWASGEPGRGRQGQPLPWELRLGLLLSVLAATLAQAPSLDVPGCSRGSCYPATGDLLVGRADRLTASSTCGLHSPQPYCIVSHLQDEKKCFLCDSRRPFSARDNPNSHRIQNVVTSFAPQRRTAWWQSENGVPMVTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWHVYRYFSYDCGADFPGIPLAPPRRWDDVVCESRYSEIEPSTEGEVIYRVLDPAIPIPDPYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIREKYYYALYELVIRGNCFCYGHASQCAPAPGAPAHAEGMVHGACICKHNTRGLNCEQCQDFYQDLPWHPAEDGHTHACRKCECNGHTHSCHFDMAVYLASGNVSGGVCDGCQHNTAGRHCEFCRPFFYRDPTKDMRDPAVCRPCDCDPMGSQDGGRCDSHDDPVLGLVSGQCRCKEHVVGTRCQQCRDGFFGLSASDPRGCQRCQCNSRGTVPGSSPCDSSSGTCFCKRLVTGHGCDRCLPGHWGLSHDLLGCRPCDCDVGGALDPQCDEATGQCRCRQHMIGRRCEQVQPGYFRPFLDHLTWEAEAAQGQGLEVVERLVTNRETPSWTGPGFVRLREGQEVEFLVTSLPRAMDYDLLLRWEPQVPEQWAELELMVQRPGPVSAHSPCGHVLPKDDRIQGMLHPNTRFLVFPRPVCLEPGISYKLKLKLIGTGGRAQPETSYSGLLIDSLVLQPHVLVLEMFSGGDAAALERRTTFERYRCHEEGLMPSKAPLSETCAPLLISVSALIYNGALPCQCDPQGSLSSECSPHGGQCRCKPGVVGRRCDVCATGYYGFGPAGCQACQCSPDGALSALCEGTSGQCPCRPGAFGLRCDHCQRGQWGFPNCRPCVCNGRADECDTHTGACLGCRDYTGGEHCERCIAGFHGDPRLPYGGQCRPCPCPEGPGSQRHFATSCHRDGYSQQIVCQCREGYTGLRCEACAPGHFGDPSKPGGRCQLCECSGNIDPMDPDACDPHTGQCLRCLHNTEGPHCGYCKPGFHGQAARQSCHRCTCNLLGTDPRRCPSTDLCHCDPSTGQCPCLPHVQGLNCDHCAPNFWNFTSGRGCQPCACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELYWGDPGLQCRACDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGVFPACHPCHACFGDWDRVVQDLAARTRRLEQWAQELQQTGVLGAFESSFLNMQGKLGMVQAIMSARNASAASTAKLVEATEGLRHEIGKTTERLTQLEAELTAVQDENFNANHALSGLERDGLALNLTLRQLDQHLEILKHSNFLGAYDSIRHAHSQSTEAERRANASTFAVPSPVSNSADTRRRTEVLMGAQKENFNRQHLANQQALGRLSAHAHTLSLTGINELVCGAPGDAPCATSPCGGAGCRDEDGQPRCGGLGCSGAAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAHRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIWGAVVDTQNTEQTLQRVQERMAGAEKSLNSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALEGKAAQLDGLEARMRSVLQAINLQVQIYNTCQ
Protein: PHD finger protein ALFIN-LIKE 7 (Protein AL7) (Q8LA16)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:19154204}.
Interaction partners:
- PHD finger family protein / SWIB complex BAF60b domain-containing protein / GYF domain-containing protein
- Cysteine/Histidine-rich C1 domain family protein
- PHD finger protein MALE MEIOCYTE DEATH 1
- Protein TRAUCO
- Protein RBL
- GMP synthase
- Multiple organellar RNA editing factor 1, mitochondrial
- Chromatin remodeling protein SHL
- 12S seed storage protein CRB
- Putative E3 ubiquitin-protein ligase RING1a
Sequence:
MEGIQHPIPRTVEEVFSDFRGRRAGLIKALSTDVQKFYHQCDPEKENLCLYGLPNETWEVNLPVEEVPPELPEPALGINFARDGMQEKDWISLVAVHSDSWLISVAFYFGARFGFGKNERKRLFQMINDLPTIFEVVTGNAKQSKDQSANHNSSRSKSSGGKPRHSESHTKASKMSPPPRKEDESGDEDEDDEQGAVCGACGDNYGGDEFWICCDACEKWFHGKCVKITPAKAEHIKHYKCPSCTTSKKMKA
Protein: Xylose import ATP-binding protein XylG (EC 7.5.2.10) (P37388)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex XylFGH involved in xylose import. Responsible for energy coupling to the transport system (Probable). The XylFGH system can also transport ribose in absence of xylose.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01722}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01722}.
Interaction partners:
- D-xylose-binding periplasmic protein
- Xylose transport system permease protein XylH
- Probable ABC transporter permease protein YphD
- Ribose import permease protein RbsC
- Autoinducer 2 import system permease protein LsrC
- D-allose transport system permease protein AlsC
- L-arabinose transport system permease protein AraH
- Galactofuranose transporter permease protein YtfT
- Galactose/methyl galactoside import permease protein MglC
- Inner membrane ABC transporter permease protein YjfF
Sequence:
MPYLLEMKNITKTFGSVKAIDNVCLRLNAGEIVSLCGENGSGKSTLMKVLCGIYPHGSYEGEIIFAGEEIQASHIRDTERKGIAIIHQELALVKELTVLENIFLGNEITHNGIMDYDLMTLRCQKLLAQVSLSISPDTRVGDLGLGQQQLVEIAKALNKQVRLLILDEPTASLTEQETSILLDIIRDLQQHGIACIYISHKLNEVKAISDTICVIRDGQHIGTRDAAGMSEDDIITMMVGRELTALYPNEPHTTGDEILRIEHLTAWHPVNRHIKRVNDVSFSLKRGEILGIAGLVGAGRTETIQCLFGVWPGQWEGKIYIDGKQVDIRNCQQAIAQGIAMVPEDRKRDGIVPVMAVGKNITLAALNKFTGGISQLDDAAEQKCILESIQQLKVKTSSPDLAIGRLSGGNQQKAILARCLLLNPRILILDEPTRGIDIGAKYEIYKLINQLVQQGIAVIVISSELPEVLGLSDRVLVMHEGKLKANLINHNLTQEQVMEAALRSEHHVEKQSV
Protein: Proteasome subunit beta type-5 (EC 3.4.25.1) (Macropain subunit PRE2) (Multicatalytic endopeptidase complex subunit PRE2) (Proteasome component PRE2) (Proteinase YSCE subunit PRE2) (P30656)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. This unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Probable proteasome subunit alpha type-7
- Proteasome subunit beta type-3
- Proteasome subunit alpha type-1
- Proteasome subunit alpha type-6
- 26S proteasome regulatory subunit 6A
- Proteasome subunit beta type-7
- 26S proteasome regulatory subunit 7 homolog
- 26S proteasome regulatory subunit RPN2
- 26S proteasome regulatory subunit 8 homolog
- Proteasome subunit beta type-1
Sequence:
MQAIADSFSVPNRLVKELQYDNEQNLESDFVTGASQFQRLAPSLTVPPIASPQQFLRAHTDDSRNPDCKIKIAHGTTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRSILAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKVKEEEGSFNNVIG
Protein: Inner membrane ABC transporter permease protein YdcV (P0AFR9)
Organism: Escherichia coli (strain K12)
Function: Involved in natural transformation. Probably part of the ABC transporter complex YdcSTUV. Probably responsible for the translocation of the substrate across the membrane. During natural transformation, may serve as the channel for dsDNA uptake (Probable).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Inner membrane ABC transporter permease protein YdcU
- Uncharacterized ABC transporter ATP-binding protein YdcT
- Bifunctional polyhydroxybutyrate synthase / ABC transporter periplasmic binding protein
- Spermidine/putrescine transport system permease protein PotB
- Spermidine/putrescine-binding periplasmic protein
- Putrescine-binding periplasmic protein PotF
- Gamma-aminobutyraldehyde dehydrogenase
- Putrescine transport system permease protein PotH
- Putrescine transport ATP-binding protein PotG
- Spermidine/putrescine import ATP-binding protein PotA
Sequence:
MHSERAPFFLKLAAWGGVVFLHFPILIIAAYAFNTEDAAFSFPPQGLTLRWFSVAAQRSDILDAVTLSLKVAALATLIALVLGTLAAAALWRRDFFGKNAISLLLLLPIALPGIVTGLALLTAFKTINLEPGFFTIVVGHATFCVVVVFNNVIARFRRTSWSLVEASMDLGANGWQTFRYVVLPNLSSALLAGGMLAFALSFDEIIVTTFTAGHERTLPLWLLNQLGRPRDVPVTNVVALLVMLVTTLPILGAWWLTREGDNGQ
Protein: RE37920p (Q8MS24)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPRNITSLVGKSAYLGCRVKHLGNKTVAWIRHRDLHILTVGTYTYTTDQRFQTSYHRDIDEWTLQIKWAQQRDAGVYECQISTQPVRSYSVNLNIVDLIDAETSDIMQQYYNDDAFYIAENRVYQSSNDEFAGMFGPIQTVAVPTATILGGPDLYVDKGSTINLTCIIKFSPEPPTHIFWYHQDKVLSEETSGGRLKFKTIKSEETKSILLIYDADLLHSGKYSCYPSNTEIASIRVHVLQGERPEAMQTNAAPAAVALACWSCHFGQATQAVRVISTMVAALVLLEACSSLLLQSGGGGGCPGGGSPAGGMPTRVREIREKPLTNSLFDPKIPSTTSAERVNNGSRNAR
Protein: Zinc finger-containing ubiquitin peptidase 1 (EC 3.4.19.12) (Lys-63-specific deubiquitinase ZUFSP) (Zinc finger with UFM1-specific peptidase domain protein) (A0A0S2Z644)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLSCNICGETVTSEPDMKAHLIVHMESEIICPFCKLSGVNYDEMCFHIETAHFEQNTLERNFERINTVQYGTSDNKKDNTLQCGMEVNSSILSGCASNHPKNSAQNLTKDSTLKHEGFYSENLTESRKFLKSREKQSSLTEIKGSVYETTYSPPECPFCGKIEEHSEDMETHVKTKHANLLDIPLEDCDQPLYDCPMCGLICTNYHILQEHVDLHLEENSFQQGMDRVQCSGDLQLAHQLQQEEDRKRRSEESRQEIEEFQKLQRQYGLDNSGGYKQQQLRNMEIEVNRGRMPPSEFHRRKADMMESLALGFDDGKTKTSGIIEALHRYYQNAATDVRRVWLSSVVDHFHSSLGDKGWGCGYRNFQMLLSSLLQNDAYNDCLKGMLIPCIPKIQSMIEDAWKEGFDPQGASQLNNRLQGTKAWIGACEVYILLTSLRVKCHIVDFHKSTGPLGTHPRLFEWILNYYSSEGEGSPKVVCTSKPPIYLQHQGHSRTVIGIEEKKNRTLCLLILDPGCPSREMQKLLKQDIEASSLKQLRKSMGNLKHKQYQILAVEGALSLEEKLARRQASQVFTAEKIP
Protein: Serine/threonine-protein phosphatase 5 (PP5) (EC 3.1.3.16) (Protein phosphatase T) (PPT) (Q60676)
Organism: Mus musculus (Mouse)
Function: Serine/threonine-protein phosphatase that dephosphorylates a myriad of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT. Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian rhythms, in response to steroid and thyroid hormones, calcium, fatty acids, TGF-beta as well as oxidative and genotoxic stresses (By similarity). Participates in the control of DNA damage response mechanisms such as checkpoint activation and DNA damage repair through, for instance, the regulation ATM/ATR-signaling and dephosphorylation of PRKDC and TP53BP1. Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress (By similarity). Plays a positive role in adipogenesis, mainly through the dephosphorylation and activation of PPARG transactivation function. Also dephosphorylates and inhibits the anti-adipogenic effect of NR3C1. Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E. May modulate TGF-beta signaling pathway by the regulation of SMAD3 phosphorylation and protein expression levels. Dephosphorylates and may play a role in the regulation of TAU/MAPT (By similarity). Through their dephosphorylation, may play a role in the regulation of ions channels such as KCNH2 (By similarity). Dephosphorylate FNIP1, disrupting interaction with HSP90AA1/Hsp90 (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:21994940}. Cytoplasm {ECO:0000269|PubMed:21994940}. Cell membrane {ECO:0000250|UniProtKB:P53041}. Note=Predominantly nuclear. But also present in the cytoplasm. Translocates from the cytoplasm to the plasma membrane in a RAC1-dependent manner. {ECO:0000250|UniProtKB:P53041}.
Interaction partners:
- Heat shock protein HSP 90-beta
- Hsp90 co-chaperone Cdc37
- Heat shock protein HSP 90-alpha
- Prostaglandin E synthase 3
- Mitogen-activated protein kinase kinase kinase 5
- Hamartin
- Serine/threonine-protein kinase B-raf
- Stress-induced-phosphoprotein 1
- Heat shock cognate 71 kDa protein
- E3 ubiquitin-protein ligase CHIP
Sequence:
MAMAEGERTECAETPRDEPPADGTLKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPNDKDAKMKYQECSKIVKQKAFERAIAGDEHRRSVVDSLDIESMTIEDEYSGPKLEDGKVTITFMKDLMQWYKDQKKLHRKCAYQILVQVKEVLCKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSVSKRGVSCQFGPDVTKAFLEENQLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYANTLLQLGMM
Protein: Growth-regulating factor 6 (AtGRF6) (Transcription activator GRF6) (Q9ZQ12)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that plays a role in the regulation of cell expansion in leaf and cotyledons tissues.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU01002}.
Interaction partners:
- DNA binding protein
- Di-glucose binding protein with Leucine-rich repeat domain-containing protein
- Uncharacterized protein At2g04870
- GRF1-interacting factor 1
- 14-3-3-like protein GF14 omega
- Formin-like protein 12
- Axial regulator YABBY 3
Sequence:
MATRIPFTESQWEELENQALVFKYLAANMPVPPHLLFLIKRPFLFSSSSSSSSSSSFFSPTLSPHFGWNVYEMGMGRKIDAEPGRCRRTDGKKWRCSKEAYPDSKYCERHMHRGKNRSSSRKPPPTQFTPNLFLDSSSRRRRSGYMDDFFSIEPSGSIKSCSGSAMEDNDDGSCRGINNEEKQPDRHCFILGTDLRTRERPLMLEEKLKQRDHDNEEEQGSKRFYRFLDEWPSSKSSVSTSLFI
Protein: C-X-C motif chemokine 2 (Cytokine-induced neutrophil chemoattractant 3) (CINC-3) (Macrophage inflammatory protein 2) (MIP2) (P30348)
Organism: Rattus norvegicus (Rat)
Function: Chemotactic for human polymorphonuclear leukocytes but does not induce chemokinesis or an oxidative burst. Contributes to neutrophil activation during inflammation.
Subcellular location: Secreted.
Interaction partners:
- C-X-C chemokine receptor type 2
- C-X-C chemokine receptor type 1
- Growth-regulated alpha protein
- Interleukin-1 beta
- Transcription factor Jun
- C-X-C motif chemokine 3
- Nuclear factor NF-kappa-B p105 subunit
- Transcription factor p65
- C-X-C chemokine receptor type 4
- C-C chemokine receptor type 5
Sequence:
MAPPTRQLLNAVLVLLLLLATNHQGTGVVVASELRCQCLTTLPRVDFKNIQSLTVTPPGPHCAQTEVIATLKDGHEVCLNPEAPLVQRIVQKILNKGKAN