wanglab/gogpt-training-data huggingface dataset:
Protein: WD repeat domain 27 (WD repeat-containing protein 27 isoform X1) (B8JJR1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MADVTSEQYFIERFSVTCSKPVSHLQLACCPSHCAIPWKDKNIRIYENKINNLEPPLELTGHHGDVSAMVFGTERDQPILCSASEDYVIVWDINRCYRQIKEGGIASGRVVGTLLGRVVYLSLCPMSAKVAACSGSRVVLLNAEREEVLGVLKAHLGPVTASEFCPWDVNLLISISEDRTFKIWDVKKGGILFESAVLSAYPLLSLSFMKQNGQFITGSGDGQLWCYTLPVDHKCRLVTKLDLSKLEQKHERNLRMISPPQSRTDGTARCDERGAVETAKPVLRIWPQTPKINHASLQQRGSYVWIGSSDGLCLLDLDTSELLSFLPLKGDLSISIAGSWVISEGLDGSMRCLVSSLFETSVVLLVVNGVRLDELCLRMAKSFSVEEQLSVMPSSPLMTTSPLKAELAKKGPKPQRKGGVNYQTSVKDQALVFHTQVKSSGYNTAPHRTMFRPKTNIKKKSSSITKTSTTMNDLLSEYPSHSEAPSVSFAHLMVSTSPTTMNALQYSGDGKQIVCGLGDGSVLLYNSSLTGNPDVYTGHSKAVNTVCWSHSKRWFLSTSEDPTLCIWTTSASEPVLTMREDQFAKPIRSAQFYYLDKFLLLASGSNLMLYLYHLDNTKDDIKRYKQRSKFKLTGKFSMKSGTDITSISAVNDFYSYIVLAAGADRTIQVFDMNRGSLVTQIPDAHCRAVHHLAQNQGSSFCTQAVQAYNLFLSSALTDGLKLWDLRTARCVRRYESHVNRCLHCTAAFSPCGRFIATGSEDHSAYIYDTRSSIFLHKLQRHSETVLNVAFNPAKPELLTGTLDGKLALFHPSECLLP
Protein: Enlarged germline granules protein 1 (D3YT16)
Organism: Caenorhabditis elegans
Function: Plays a role in modulating RNAi activity and P-granule accumulation in the germline. May function in association with CSR-1 complex components such as drh-3 to regulate RNA transcript accumulation in germ cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28182654}. Cytoplasmic granule {ECO:0000269|PubMed:28182654}. Note=Mainly localizes to the rachis, which is the central core of the cytoplasm connecting developing oocytes in the syncytial gonad (PubMed:28182654). Within the rachis, partially co-localizes with the P-body component cgh-1 (PubMed:28182654). Localizes to foci next to P-granules, but does not co-localize with P-granules (PubMed:28182654). {ECO:0000269|PubMed:28182654}.
Interaction partners:
- ATP-dependent RNA helicase glh-3
- Protein PAT1 homolog 1
Sequence:
MSNGKRGRKAKPTNKEKDMIFTPGCVDCHMNHLPFQCPRPVMTKKLPEWEKKSIGMGKLKNPLDSKVKMYSEPARQTTWKEKLSQLNHENMSYNAHNKRSSRQRGNSYRLPQQNIPPPSHHQSSQVMRGFQNAPFQMQPHYNNERKPQSRRNDTMRASKSAYAAATAPVKKHVRPANEQHMRKLNDLLRPFSYGSDDLYEETQPFVKETSLANVDIQICQTRPKVPPGKMWIFESRTIYDENGNCVSAREGAMEVSLASRMHNEPIVIVSMNDSMCF
Protein: DNA-directed RNA polymerase subunit 12-like protein (Q9C8M4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase subunit 10-like protein
- DNA-directed RNA polymerase subunit
- DNA binding / DNA-directed RNA polymerase
- DNA-directed RNA polymerases II and V subunit 8A
- DNA-directed RNA polymerases II and V subunit 6B
- DNA-directed RNA polymerases II, IV and V subunit 10
- DNA-directed RNA polymerases II, IV and V subunit 6A
- DNA-directed RNA polymerases II, IV and V subunit 11
- DNA-directed RNA polymerases II, IV and V subunit 8B
- DNA-directed RNA polymerase III subunit 2
Sequence:
MDLQQSETDDKQPEQLVIYVCGDCGQENILKRGDVFQCRDCGFRILYKKRILDKKETRIGV
Protein: Terpene synthase 1 (EC 4.2.3.-) (EC 4.2.3.106) (EC 4.2.3.46) (Q55E23)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into the sesquiterpene (E,E)-alpha-farnesene. Is also able to convert geranyl diphosphate (GPP) into a mixture of monoterpenes including (Z)-beta-ocimene; (E)-beta-ocimene and allo-ocimene.
Interaction partners:
- Alpha,alpha-trehalose-phosphate synthase B
- Uncharacterized protein
- Alpha,alpha-trehalose-phosphate synthase A
Sequence:
MNILLKDFKYPESWNKSPNQSNQYIDQVFEDTNKIGIYELNNQDHYLYVENLLNVTSYLYPTFDKEQLRLCATYLHWLFLIDDFLEDEYNTMSEKQNDVIKSHAQILLTGQYLNSDVDVKPSEKLTMFLQNTSKDWAIKYNKFDVHNIYMTTLFQWLYSVYPLNKTTESTKPIHMDLYTFIRKVNIGVAGSIIVGLLADKDITDIDISKIWLNPIFTRIMENSTIQIGLVNDCASYDKEYANGGHITNPLYFLQVRDNLTFNETLNFIVNKCNQSIDEIIKDEQLLLKQLKDQGYTENQLNQVNIILNYNHNLIQGNINWSLISKRYNNHDGKPFIFENTKSKYI
Protein: H2-M beta 2 (Histocompatibility 2, class II, locus Mb2) (MHC class II H2-M beta 2 chain) (MHC class II antigen Mb2) (Q31099)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Class II histocompatibility antigen, M alpha chain
- H2-O alpha
- H-2 class II histocompatibility antigen gamma chain
- Histocompatibility 2, O region beta locus
- H-2 class II histocompatibility antigen, E-B beta chain
- H-2 class II histocompatibility antigen, A beta chain
- T-cell surface glycoprotein CD4
- H-2 class II histocompatibility antigen, A-B alpha chain
- T-cell surface glycoprotein CD3 zeta chain
- Class II histocompatibility antigen, M beta 1 chain
Sequence:
MAALWLLLLVLSLHCMGAGGFVAHVESTCVLNDAGTPQDFTYCVSFNKDLLACWDPDVGKIVPCEFGVLSRLAEIISNILNEQESLIHRLQNGLQDCATHTQPFWDVLTHRTRAPSVRVAQTTPFNTREPVMLACYVWGFYPADVTITWMKNGQLVPSHSNKEKTAQPNGDWTYQTVSYLALTPSYGDVYTCVVQHSGTSEPIRGDWTPGLSPIQTVKVSVSAATLGLGFIIFCVGFFRWRKSHSSSYTPLPGSTYPEGRH
Protein: 10 kDa heat shock protein, mitochondrial (HSP10) (10 kDa chaperonin) (O59804)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (By similarity).
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Heat shock protein 60, mitochondrial
- GrpE protein homolog
- Iron-sulfur cluster biogenesis chaperone, mitochondrial
- Serine/threonine-protein kinase oca2
- Heat shock protein 78
- Heat shock protein 90 homolog
- Heat shock protein homolog pss1
- Probable T-complex protein 1 subunit beta
- Lon protease homolog, mitochondrial
- Large ribosomal subunit protein bL12m
Sequence:
MATKLKSAKSIVPLLDRILVQRIKADTKTASGIFLPEKSVEKLSEGRVISVGKGGYNKEGKLAQPSVAVGDRVLLPAYGGSNIKVGEEEYSLYRDHELLAIIKE
Protein: Chitin deacetylase (EC 3.5.1.41) (A0A1L3THR9)
Organism: Pestalotiopsis sp
Function: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine polymers in chitin to form chitosan and acetate. May play a role in evasion of the host immune response; plant chitinases liberate chitin molecules from the fungal cell wall which act as elicitors of the plant immune response, deacetylation of the liberated chitin neutralizes elicitor activity.
Subcellular location: Secreted {ECO:0000269|PubMed:27901067}.
Interaction partners:
Sequence:
MLAPLFAALLAGAATASPIQERQSSVPVGTIITACTVPNTFALTFDDGPFAYTSELLDLLSSNGVKATFFLNGQNWGSIYDYTSVVTRMDAEGHQIGSHTWSHADLATLDAAGITSQMTQLETALTSILGKVPTYMRPPYFSTNALALSTLGGLGYHVINANIDTLDYEHDDDTIGVAFTNFQNGLASGGTVSLMHDVHAQTVHVLVQEAINAIKAKGLTPVTVGTCLGDASANWYKSGGGSGTTPPPATGGPSPDDTCGGSNGYVCQNSQCCSQWGWCGTTSEYCAAGCQAAYGPCT
Protein: Ribosome-associated molecular chaperone SSB1 (EC 3.6.4.10) (Cold-inducible protein YG101) (Heat shock protein SSB1) (Hsp70 chaperone Ssb) (P11484)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10347213, ECO:0000269|PubMed:23332755, ECO:0000305|PubMed:1394434}. Note=About 50% of the protein is associated with translating ribosomes, but sufficient Ssb exists in the cell for each ribosome to be associated with at least one Ssb molecule. {ECO:0000269|PubMed:1394434, ECO:0000269|PubMed:23332755, ECO:0000269|PubMed:9670014}.
Interaction partners:
- Ribosome-associated molecular chaperone SSB2
- Zuotin
- Heat shock protein homolog SSE1
- Mitochondrial protein import protein MAS5
- ATP-dependent molecular chaperone HSP82
- Heat shock protein STI1
- ATP-dependent molecular chaperone HSC82
- Hsp70 nucleotide exchange factor FES1
- Protein SIS1
- Endoplasmic reticulum chaperone BiP
Sequence:
MAEGVFQGAIGIDLGTTYSCVATYESSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKDMKTWPFKVIDVDGNPVIEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAISGLNVLRIINEPTAAAIAYGLGAGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAILTGQSTSDETKDLLLLDVAPLSLGVGMQGDMFGIVVPRNTTVPTIKRRTFTTCADNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVLEAIFEVDANGILKVTAVEKSTGKSSNITISNAVGRLSSEEIEKMVNQAEEFKAADEAFAKKHEARQRLESYVASIEQTVTDPVLSSKLKRGSKSKIEAALSDALAALQIEDPSADELRKAEVGLKRVVTKAMSSR
Protein: Aspartic protease 6 (EC 3.4.23.-) (O01530)
Organism: Caenorhabditis elegans
Function: Aspartic protease.
Subcellular location: Secreted {ECO:0000269|PubMed:17081123}. Note=Secreted into the pseudocoelom. {ECO:0000269|PubMed:17081123}.
Interaction partners:
- Peptidase A1 domain-containing protein
- Aspartic protease 3
- C-type lectin domain-containing protein
- Aspartic protease 1
- Peptidase A1 domain-containing protein
- Putative serine protease K12H4.7
- C-type LECtin
Sequence:
MKTFILLAVLGLASASVHQHKIVWRESKKMGMIRTGQYPAYLEYQRNLRAVSPNVLANLPQNVNDFGDFEYLGNITIGTPDQGFIVVLDTGSSNLWIPGPTCKTNCKTKSKFDSTASSTFVKNGKSWTIQYGSGDAAGILGQDTVRFGAKGDSQLSVPTTTFGIASKISADFKNDATDGILGLAFTSLAVDGVVPPLINAINQGILDQPLFSVWLEHRGAANNVGGGVFTYGAIDTTNCGALVAYQPLSSATYYQFKAAGFKLGSYSNTKTVDVISDTGTSFLGGPQSVVDGLAKAAGATYDDFNEVYFIDCAAQPGTLDITIGTNTYSIQPVNYIVDAGNGQCLFAAFPFDFGGFGPSWILGDPFIRQYCNIYDIGNKRMGFAPSLQK
Protein: Alpha carbonic anhydrase 3 (AtaCA3) (AtalphaCA3) (EC 4.2.1.1) (Alpha carbonate dehydratase 3) (Q9FYE3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Reversible hydration of carbon dioxide.
Subcellular location: Plastid, chloroplast stroma {ECO:0000250}. Note=Targeted to the chloroplast via a protein-targeting pathway that uses the secretory system. {ECO:0000250}.
Interaction partners:
- Cyanate hydratase
- Thioredoxin-like 3-2, chloroplastic
- F-box/kelch-repeat protein At5g49000
- Probable protein S-acyltransferase 15
- Nucleic acid-binding, OB-fold-like protein
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 9
- Metal-independent phosphoserine phosphatase
- Synaptotagmin-3
- UDP-URONIC ACID TRANSPORTER 1
- Dentin sialophosphoprotein
Sequence:
MKTIILFVTFLALSSSSLADETETEFHYKPGEIADPSKWSSIKAEWKICGTGKRQSPINLTPKIARIVHNSTEILQTYYKPVEAILKNRGFDMKVKWEDDAGKIVINDTDYKLVQSHWHAPSEHFLDGQRLAMELHMVHKSVEGHLAVIGVLFREGEPNAFISRIMDKIHKIADVQDGEVSIGKIDPREFGWDLTKFYEYRGSLTTPPCTEDVMWTIINKVGTVSREQIDVLTDARRGGYEKNARPAQPLNGRLVYLNEQSSPSPTPRLRIPRVGPV
Protein: Glucosyl-3-phosphoglycerate/mannosyl-3-phosphoglycerate phosphatase (GpgP) (MpgP) (EC 3.1.3.70) (EC 3.1.3.85) (Q12XX5)
Organism: Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)
Function: Involved in the biosynthesis of glucosylglycerate. Catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) and mannosyl-3-phosphoglycerate (MPG) to glucosylglycerate (GG) and mannosylglycerate (MG), respectively.
Interaction partners:
- Glucosyl-3-phosphoglycerate synthase
- Protein with six-hairpin-glycosidase domain
- Uncharacterized protein
Sequence:
MKHIIFTDLDGTLIDHDTYSYDAARPALDLLKEKEIPLIFCTSKTRAELEVYVDELECHHPFISENGGAIFIPKDHFSIELKDVHEIGNYKVIEFGTSYTRIRGVLEDIRKKTGFKITGFGDLDAEGVSKDTGLDIRSAKLAKLREYDEAFRLEEDENATAKVIELIHAAGLNYTKGGRYWHIMGDNDKGKAVRALTEIYRQQFTEVVTIALGDSLNDLPMLKAVDIPFLVQKPDGKYDPSIILTEIKHAEGIGPVGWNNAIMDLIGKNNNI
Protein: GH19680p (Q95SK1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MASSVSNLASTVATATTATLEDLHFSLTDYIVFSLMLSASAGIGVYFGFFSKAKNTTEEYLQGGKRMPTLPVAISLVSSQLSGVAMMSVPAETYSFGFNMIFVVWAMVLSVPVLIYIIVPVFYDNNVSNCYEYLELRFSKRTRQLVTITFILNQFLMLPVYMFVPSLAFSQVTGYNIHLINTVVSSICVFYTMLGGIKAVVWTDVVQGSVMLISVVLVAILGTSNTGGITNVLENAAEGGRFDFSFGIDPRLRLTFISGMASGLLMWTGKLGLDQSCVQRIVSLPSYGHAKRCLLMAGVGFLLIMSFTCFTGIIMFAYYYGCDPIQAGLVSKPDKLMPFFIQDIMGHMMGMPGVFISCVFSASLSSLSASLNSFAGVVYFDYIKPRINHSEAKANATMKLVIVVMGAYCIVGGFIVQNFNSIIQTMWTITGINMGAVVGVFCLGMFVPRCNAKVAVSGIAFSCLVMLWIIINGQMNLKAGLIKYDPLPNGLDQCEAKGFEVILNAIRNKNVTNVGTTAIPSLEAPKELTTAFDSNRDFSIYDTSFYWYKVLGALLVFAWAIPMSYVWPLDKEEKQNPKLYSPFVRSMLNKPSPVLELEELPLKTPLSEEQIKEKENGSATEA
Protein: Keratin, type I cytoskeletal 14 (Cytokeratin-14) (CK-14) (Keratin-14) (K14) (Q61781)
Organism: Mus musculus (Mouse)
Function: The nonhelical tail domain is involved in promoting KRT5-KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P02533}. Nucleus {ECO:0000250|UniProtKB:P02533}. Note=Expressed in both as a filamentous pattern. {ECO:0000250|UniProtKB:P02533}.
Interaction partners:
- Keratin, type II cytoskeletal 5
- Keratin, type I cuticular Ha6
- Loricrin
- Tumor protein 63
- Collagen alpha-1
- Keratin, type I cytoskeletal 16
- Plakophilin-1
- Keratin, type I cytoskeletal 17
- Filaggrin
- Desmoglein-3
Sequence:
MATCSRQFTSSSSMKGSCGIGGGSSRMSSILAGGSCRAPSTYGGMSVTSSRFSSGGACGIGGGYGGSFSSSSFGGGLGSGFGGRFDGFGGGFGGGLGGGFGGGLGGGLGGGIGDGLLVGSEKVTMQNLNDRLATYLDKVRALEEANTELEVKIRDWYQRQRPTEIKDYSPYFKTIEDLKSKILAATVDNANVLLQIDNARLAADDFRTKFETEQSLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLKKNHEEEMASMRGQVGGDVNVEMDAAPGVDLSRILNEMRDQYEKMAEKNRKDAEEWFFSKTEELNREVATNSELVQSGKSEISELRRTMQNLEIELQSQLSMKASLENNLEETKGRYCMQLAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAHLSSSQFSSSSQFSSGSQSSRDVTSTNRQIRTKVMDVHDGKVVSTHEQVLRTKN
Protein: Conserved domain protein (A0A0H2UNU9)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSYFKKYKFDKSQFKLGMRTFKTGIAVFLVLLIFGFFGWKGLQIGALTAVFSLRESFDESVHFGTSRILGNSIGGLYALVFFLLNTFFHEAFWVTLVVVPICTMLTIMTNVAMNNKAGVIGGVAAMLIITLSIPSGETILYVFVRVLETFMGVFVAIIVNYDIDRIRLFLEKKEK
Protein: Vacuolar protein sorting-associated protein 28 homolog (H-Vps28) (ESCRT-I complex subunit VPS28) (Q9UK41)
Organism: Homo sapiens (Human)
Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11916981}. Late endosome membrane {ECO:0000269|PubMed:11916981}; Peripheral membrane protein {ECO:0000269|PubMed:11916981}.
Interaction partners:
- Vacuolar protein-sorting-associated protein 36
- Vacuolar protein sorting-associated protein 37A
- Tumor susceptibility gene 101 protein
- Vacuolar protein sorting-associated protein 37C
- Multivesicular body subunit 12B
- Vacuolar protein sorting-associated protein 37B
- Ubiquitin-associated protein 1
- Multivesicular body subunit 12A
- Vacuolar protein-sorting-associated protein 25
- Charged multivesicular body protein 6
Sequence:
MFHGIPATPGIGAPGNKPELYEEVKLYKNAREREKYDNMAELFAVVKTMQALEKAYIKDCVSPSEYTAACSRLLVQYKAAFRQVQGSEISSIDEFCRKFRLDCPLAMERIKEDRPITIKDDKGNLNRCIADVVSLFITVMDKLRLEIRAMDEIQPDLRELMETMHRMSHLPPDFEGRQTVSQWLQTLSGMSASDELDDSQVRQMLFDLESAYNAFNRFLHA
Protein: Telomere elongation protein EST1 (Ever shorter telomeres protein 1) (P17214)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Directly involved in telomere replication. Associates with telomerase and during its interaction with CDC13, telomerase activity is promoted.
Subcellular location: Nucleus. Chromosome, telomere {ECO:0000305}.
Interaction partners:
- Telomere replication protein EST3
- Cell division control protein 13
- Telomerase reverse transcriptase
- ATP-dependent DNA helicase II subunit 2
- ATP-dependent DNA helicase II subunit 1
- Protein STN1
- Ribonucleases P/MRP protein subunit POP1
- Ribonucleases P/MRP protein subunit POP6
- Ribonucleases P/MRP protein subunit POP7
- Telomere length regulation protein TEN1
Sequence:
MDNEEVNEECMRLFFKNARAHLDKHLTSRLTCDENAYITFRCFLDGIHRKSTRFLEELLLKQENMYHNNNYERINDSVIPLVLKLLWLQIHEPTLQWFEHWFHDIMRLSNRRKFRVFRIFQKKMIQFFKITHRYYYDIIEHLCAKYDMNSVISNALFAKLNLMQYTDGLSTHEKIILNTSNPLTFSIVISLQRCVINLGSTHFYKTLLNKPSNKPKSVEGFEKSIRYLNIASLYLPAVGDTYFQRAKIYLITGKFSLYFFELVRGALVRIPSKCALNNLKDFILTPDFPERRRLMKKLAILVSKDLKGEKSFFEGQIVLQFLSIVEHTLVPQSWNASRASNCWLLKEHLQMAALKYHSGNINVILENLAATMGSFDLMFTTRKSKEQKNKLKYADLSERQVFFLDLSFDFIANIIDVVIKPSWQKNMEDFRYLAIIRLLMCWIKSYRSILQYTHRHRKFCTSFALLLNDLINSPLNCSGNIYSHRPKRSYLFREDIIFREFSCINFALTDFNDDYVYDSPDMINNIIGCPTLTKVLSPKEECVLRIRSIIFSGMKFLEKNDTGVIWNASKYKFDLISPNIKIKRQIALSEISSKINVKTQQERVVSSRKVEAKRDEQQRKRAGKIAVTELEKQFANVRRTKKLSPLPEKDGVSSELVKHAASRGRKTITGPLSSDFLSYPDEAIDADEDITVQVPDTPT
Protein: Ubiquitin-conjugating enzyme E2-24 kDa (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 8) (Glucose-induced degradation protein 3) (Ubiquitin carrier protein) (Ubiquitin-protein ligase) (P28263)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). 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).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10811607}.
Interaction partners:
- GID complex subunit 1
- GID complex subunit 5
- GID complex subunit 7
- Ubiquitin-activating enzyme E1 1
- E3 ubiquitin-protein ligase RMD5
- GID complex substrate-recognition subunit 4
Sequence:
MSSSKRRIETDVMKLLMSDHQVDLINDSMQEFHVKFLGPKDTPYENGVWRLHVELPDNYPYKSPSIGFVNKIFHPNIDIASGSICLDVINSTWSPLYDLINIVEWMIPGLLKEPNGSDPLNNEAATLQLRDKKLYEEKIKEYIDKYATKEKYQQMFGGDNDSDDSDSGGDLQEEDSDSDEDMDGTGVSSGDDSVDELSEDLSDIDVSDDDDYDEVANQ
Protein: Uncharacterized protein (Q9A4F6)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Interaction partners:
- Antitoxin RelB3
- Toxin RelE3
Sequence:
MAPTRKSRADLALNEGALAFPQGKALPPGVVEADADPLFVGLVGRHLVAQPAFPHQDRAGRRLHIDERLQTLGRVGFAGRGGHHHRQARILELDGRGARRDGHIDRAGNDAVGVDVAGVLAARLQDVDPEAVHHQLARAQVEAKGLGEGGRVLVELLLEVREQAVAHRQVVQRGVGRVAKIALVIGPGLTGLVLLGDGDAGVVQVVDEGVEALLAGEGGFIERGDEEAAWGHERGHSA
Protein: Kinesin-like protein, KLP38B (O16866)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSNKSTPVRQRIQQFQTRGVHKSTPASEMRKKVLMTRAEDREHRDRPEQLLNTAFSGSTPQPKPKPTALNACYTPSSLYRNANSTPGRAKTPGTGKSSCSRTKERDSLMESCLSVSEESNMIVAVRVRPLNALECTRGQVTNVVQVHGNSNELTVQAGSSADASAGVTHFFSYDQVYYSCDPERKNFACQAKVFEGTARPLIDTAFEGYNACLFAYGQTGSGKSYSMMGIEALDDAALDGGPPHDEAGIIPRFCHELFRRIEAVKSQQQLQVEVEVSYFEIYNEKIHDLLSVQHAAAATGESTPIQQQQQQQRPALKVREHPIFGPYVVDLSAHSVDSYSALRNWLAVGNSQRATASTAMNDKSSRSHSIFNIVLNLTDLSSDDGLSSDTDSSTASSLRQTRRSKISLVDLAGSERISVSGSNGERIREGVSINKSLLTLGKVIAALADSRKASANGPLGSGTPSTFVPYRESVLTWLLRENLGGNSKTVMLATISPASIHADETLATLRYACKARSIVNRVKVNESPHDKIIRDLRAEVDRLKSLRNEYERQRRLSGNSNNPVPRKIIIETSVDETEVEALRQQLAERERELSRAQKSWMEKLKEAEDQRKSELRVLKRRGLALELTAEQKQACLVNLTADPILSGTLFYLLPQGLVRIGRGRLPGGSSSSQPDIVLDGPLVALQHCSIEHERGGKLYVIPGSEDFETYVNGELLKDRRQLFHGDRLVIGGSHYFRISNPFCSQRGKADHPVDFQLAHQEILQKQEQQLRSELEAEKRAALTKIEQERAQHARDFEERLQCLELEQFKYKCNSEMLETERQALALAQQQEHTPLRHEDAVSTPAQKSTILEDIQRIMLNPSEESLHKTQLMVKEATQRCRQLDLPLEFRQTQTPDEFGLLRTVILILDKQRGLKAEWPTARLGVWLDLVRDNAEQQEKLNATTIFQSVEVDWEPLDADLNETLSDTHNSSRIALNLSAMKDVLLNKPLKRLLNASSSKSNTPRQTSTPSPGSQLVHFTKRLLTYDPEEIPESQSSFTTLVQQELQIMQRSAQRLRRHCEAALLERENHQDNGVLAVSLQEALARMDTVLNGMHTSLARAEATACVTSPTKTQKAVRFLID
Protein: Vacuolar protein sorting-associated protein 4A (EC 3.6.4.6) (Q8VEJ9)
Organism: Mus musculus (Mouse)
Function: Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. It is required for proper accomplishment of various processes including the regulation of endosome size, primary cilium organization, mitotic spindle organization and chromosome segregation, and nuclear envelope sealing and spindle disassembly during anaphase (By similarity). In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Involved in cytokinesis: retained at the midbody by ZFYVE19/ANCHR and CHMP4C until abscission checkpoint signaling is terminated at late cytokinesis. It is then released following dephosphorylation of CHMP4C, leading to abscission. VPS4A/B are required for the exosomal release of SDCBP, CD63 and syndecan (By similarity). Critical for normal erythroblast cytokinesis and correct erythropoiesis (By similarity).
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:12594041}; Peripheral membrane protein {ECO:0000305|PubMed:12594041}. Midbody {ECO:0000250|UniProtKB:Q9UN37}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UN37}. Note=Membrane-associated in the prevacuolar endosomal compartment. Localizes to the midbody of dividing cells, interaction with ZFYVE19/ANCHR mediates retention at midbody. Localized in two distinct rings on either side of the Flemming body (By similarity). {ECO:0000250|UniProtKB:Q9UN37}.
Interaction partners:
- Vacuolar protein sorting-associated protein VTA1 homolog
- Charged multivesicular body protein 1B1
- Charged multivesicular body protein 1a
- Charged multivesicular body protein 5
- Charged multivesicular body protein 6
- Vacuolar protein sorting-associated protein 4B
- Charged multivesicular body protein 2a
- Charged multivesicular body protein 1B2
- Charged multivesicular body protein 2b
- IST1 homolog
Sequence:
MTTSTLQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKYEAHSDKAKESIRAKCMQYLDRAEKLKDYLRNKEKHGKKPVKENQSEGKGSDSDSEGDNPEKKKLQEQLMGAVVMEKPNIRWNDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNSTFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNNNDGTLVLGATNIPWVLDSAIRRRFEKRIYIPLPEEAARAQMFRLHLGSTPHNLTDANIHELARKTEGYSGADISIIVRDSLMQPVRKVQSATHFKKVCGPSRTNPSVMIDDLLTPCSPGDPGAIEMTWMDVPGDKLLEPVVCMSDMLRSLATTRPTVNADDLLKVKKFSEDFGQES