wanglab/gogpt-training-data huggingface dataset:
Protein: Protein POLYCHOME (Protein UV-B-INSENSITIVE 4) (O48533)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Negative regulator of the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase required for proper mitotic progression and cell fate determination; inhibits premature cell differentiation. Prevents DNA endoreplication by promoting the maintenance of the mitotic state by preferentially inhibiting APC/C(FZR) and triggering cyclins accumulation (e.g. CYCB1-1, CYCB1-2 and CYCA2-3) in a temporal manner. Required for megagametophyte and endosperm development. Counteracts the activity of CCS52A1 thus inhibiting the turnover of CYCA2-3. Confers immunity to bacterial pathogens (e.g. Pseudomonas syringae pv. tomato DC3000), which is associated with increased expression of disease resistance (R) genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:22167059}. Note=Follows a patchy nuclear accumulation pattern.
Interaction partners:
- Cell division cycle 20.1, cofactor of APC complex
- Anaphase-promoting complex subunit 10
- Protein FIZZY-RELATED 3
- Protein FIZZY-RELATED 2
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 7
- E2F transcription factor-like E2FE
- Cyclin-A2-3
- Protein FIZZY-RELATED 1
- Anaphase-promoting complex subunit 4
Sequence:
MPEARDRIERQVDYPAAFLNRRSHGILLDEPATQHNLFGSPVQRVPSEATGGLGSIGQGSMTGRGGLVRGNFGIRRTGGGRRGQIQFRSPQGRENMSLGVTRRGRARASNSVLPSWYPRTPLRDISAVVRAIERRRARMGEGVGRDIETPTPQQLGVLDSLVPLSGAHLEHDYSMVTPGPSIGFKRPWPPSTAKVHQILLDITRENTGEEDALTPEKKLLNSIDKVEKVVMEEIQKMKSTPSAKRAEREKRVRTLMSMR
Protein: Adipogenin (Small adipocyte factor 1) (SMAF-1) (Q8R400)
Organism: Mus musculus (Mouse)
Function: Plays a role in stimulating adipocyte differentiation and development.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:15567149, ECO:0000269|PubMed:16132694}.
Interaction partners:
- Lipid transferase CIDEC
Sequence:
MKYPLVPLVSDLTLSFLVFWLCLPVALLLFLTIVWLHFLLSQESKEDDSDLCFNWEPWSKRPSECGCEETFPGEEDGLHW
Protein: Protein Hook homolog 1 (h-hook1) (hHK1) (Q9UJC3)
Organism: Homo sapiens (Human)
Function: Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell. Required for spermatid differentiation. Probably involved in the positioning of the microtubules of the manchette and the flagellum in relation to the membrane skeleton (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15471887}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11238449}. Note=Localizes to punctate cytoplasmic foci which do not appear to overlap with early or late endosomes, the endoplasmic reticulum, multivesicular bodies (MVBs), lysosomes, or mitochondria (By similarity). Often found in close association with microtubules (By similarity). Does not associate with the Golgi complex. During spermiogenesis, it localizes to the manchette in spermatids from steps 8-10. It is also present between the microtubule manchette and the nucleus. During manchette elongation, it is preferentially localized to the nuclear ring of the manchette, whereas the strong localization to the manchette decreases. In more mature spermatids, while the manchette migrates posteriorly, it localizes to punctuates spots. At later stages of spermatid differentiation, the punctuate expression pattern is found at both the attachment site and the proximal end of the elongated manchette. In contrast, it is not present in mature spermatozoa (By similarity). {ECO:0000250|UniProtKB:Q8BIL5}.
Interaction partners:
- AKT-interacting protein
- FHF complex subunit HOOK-interacting protein 1B
- Protein Hook homolog 3
- Protein Hook homolog 2
- Battenin
- RIMS-binding protein 3A
- Cytoplasmic dynein 1 light intermediate chain 1
- Ras-related protein Rab-11A
- FHF complex subunit HOOK interacting protein 2A
- Coiled-coil domain-containing protein 88B
Sequence:
MEETQPPPQPKLPLCDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLGQQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKEILSSPPNDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILESECKVAKFRDYEEKLIVSAWYNKSLAFQKLGMESRLVSGGGACSDTGACTPARSFLAQQRHITNTRRNLSVKVPATTSD
Protein: Death domain-containing membrane protein NRADD (Neurotrophin receptor homolog-2) (NRH2) (Neurotrophin receptor-alike death domain protein) (Q8CJ26)
Organism: Mus musculus (Mouse)
Function: Modulates NTRK1 signaling. Can activate several intracellular signaling pathways, leading to activation of JUN. Promotes apoptosis. Promotes translocation of SORT1 to the cell membrane, and thereby hinders lysosomal degradation of SOTR1 and promotes its interaction with NGFR.
Subcellular location: Cell membrane; Single-pass type III membrane protein. Nucleus. Note=Proteolytic processing gives rise to an intracellular domain that translocates to the nucleus.
Interaction partners:
- Nephrocan
Sequence:
MLYNVSKGVVYSDTALQGQDGDREGMWVGAGGALAPNTSSLFPPEPPGASSNIIPVYCALLATVILGLLAYVAFKCWRSHKQRQQLAKARTVELGDPDRDQRRGDSNVFVDSPPSLEPCIPSQGPHPDLGCQLYLHIPQQQQEEVQRLLMMGEPAKGWQELAGHLGYQAEAVETMACDQMPAYTLLRNWAAQEGNRATLRVLEDALAAIGREDVVQVLSSPAESSSVV
Protein: LOB domain-containing protein 13 (ASYMMETRIC LEAVES 2-like protein 10) (AS2-like protein 10) (Q9AT61)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Actin-related protein 2/3 complex subunit 4
- At4g14145
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- LOB domain-containing protein 40
- AT5G19950 protein
- DNA repair endonuclease UVH1
Sequence:
MSREREGFGEYYETVKKIKKDPAFETTTDHAVMGIRRHVAVPPGTTLNTVTPCAACKLLRRRCAEECPFSPYFSPHEPHKFAAVHKVFGASNVSKMLLEVGESQRGDAANSLVYEANLRLRDPIYGCMGAISALQHHIQSLQSELTTVRTEILRHKYQEATTITSLQNNFNSTTTTSSVSCDQHALASAILLPPPPPPPPTPRPPRLLSSQPAPPPTPPVSLPSPSMVVSSSSSSNSSATNSMYNPPPSSTAGYSNSLSSDNNVHYFD
Protein: Origin of replication complex subunit 2 (AtORC2) (Q38899)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein. Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Minichromosome maintenance 10
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM4
- Origin of replication complex subunit 1A
- Origin of replication complex subunit 4
- Origin of replication complex subunit 3
- Origin of replication complex subunit 5
- Origin of replication complex subunit 6
- DNA replication licensing factor MCM3
Sequence:
MEDIENIEEDEYGFSRNYFLAKELGGASKRSAHKLSDIHIVDEQELRETASTIEMKHSKEISELMSDYKTMYSKWVFELRCGFGLLMYGFGSKKALVEDFASASLTDYSVVVINGYLPSVNLKQVLLALAELLSELLKCKRKSSGSLSKGQETFPSRSMDDILSFLHGPQSGDKDCFICVVVHNIDGPALRDPESQQTLARLSSCSHIRLVASIDHVNAPLLWDKKMVHKQFNWLWHHVPTFAPYNVEGVFFPLVLAQGSTAQTAKTAAIVLQSLTPNGQNVFKILAEYQLSHPDEDGMPTDDLYSASRERFFVSSQVTLNSHLTEFKDHELVKTKRNSDGQECLNIPLTSDAIRQLLLDLNQ
Protein: Protein moonraker (MNR) (OFD1- and FOPNL-interacting protein) (Q2KHM9)
Organism: Homo sapiens (Human)
Function: Involved in centriole duplication. Positively regulates CEP63 centrosomal localization. Required for WDR62 centrosomal localization and promotes the centrosomal localization of CDK2. May play a role in cilium assembly.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:26643951}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:24613305, ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:26643951}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:26643951}. Note=Localization to centrioles and pericentriolar satellites may be mediated by interaction with PCM1. {ECO:0000269|PubMed:26643951}.
Interaction partners:
- Coiled-coil domain-containing protein 14
- Centriole and centriolar satellite protein OFD1
- Centrosomal protein 20
- Centrosomal protein of 63 kDa
- Pericentriolar material 1 protein
- Centrosomal protein of 135 kDa
Sequence:
MGPGQPASTCVHLAPRTQLDGRSDPKVLQTQNQLQFNRNVPTHSSNLAIRYSCPHAIRIEKLKHSYNESYHCKDADCRVGPDLGSSVSFSVISQERLSYAVHLARRDVKRRQFEKHIKEHHLRSQPQSSQKCGHTKYKIPDHRVERKESKSQAACQCSHQPSKVEISSSGAKVYLYSSHPGQSDLTVPNSPPTHDPGLQPHPRIGDHKNISEQKSLLEVQRLQKELSSCIHKIEEVTKKDRLEEALDPDEERRIRIRRQEQAARSARMLYVLQQQVKEIQEELDKLSPHKIKHTKKSWAMSKLAAAHRGAIRALQMFVTQFTDRGEHPLPARCKELGSLIRQLSLCSVKLDADPSVPDVVIDILQQIEALESLLEKKLSPKKVKKCFSEIRSRFPIGSQKALERWPSTSPKGERRPLTAKDTFPQETSRPSVAKQLLADKYQPDTELPETQRLQSELDVLDADIVLEEGPFILDQSASFKDEVLAVAKTKAGKKKPVTENVPFRKKDTLAPARQQGLRKAERGRQSQPHSKSRVQQTTVSSRLKMNRQPVKDRKAPWIPPNPTSPPASPKCAAWLKVKTSPRDATKEPLQQEDPQEESHLTGAVEHEAARLAWLDAETSKRLKELEELKAKEIDSMQKQRLDWLDAETSRRTKELNELKAEEMYRLQQLSVSATHLADKVEEAVLDRLKPLLVKAQRVNSTTEANIHLKDGSSVNTAKAQPAQEVAAVDFESNNIRQLDDFLEDCASELWAVTHAKILGSETLATVEDSKDSPDLEIMMRRMEEMEKYQESVRQRYNKIAYADPRLWMQEENNDQKISAISEKPLSPHPIRITKTVDRKDPAVNIMLERPCNGNSLDESVGTEEGSEKREAPLLSLAEDSQQKEGRAPLFVPPGMQHSIGDYCSRFEQYLRIISHEAVGSFNPWLIAESFSEELVDEALGAVAAELQDMCEDYAEAVFTSEFLEAAT
Protein: Inositol-3-phosphate synthase 1 (IPS 1) (EC 5.5.1.4) (Myo-inositol 1-phosphate synthase) (MI-1-P synthase) (MIP synthase) (hIPS) (Myo-inositol 1-phosphate synthase A1) (hINO1) (Q9NPH2)
Organism: Homo sapiens (Human)
Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner. Rate-limiting enzyme in the synthesis of all inositol-containing compounds.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11986}.
Interaction partners:
- Inositol monophosphatase 1
- Inositol monophosphatase 2
- Inositol polyphosphate-4-phosphatase type I A
- Inositol polyphosphate 4-phosphatase type II
- Inositol polyphosphate 1-phosphatase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- 3'
- Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase
- Transcription initiation factor IIB
- Inositol oxygenase
Sequence:
MEAAAQFFVESPDVVYGPEAIEAQYEYRTTRVSREGGVLKVHPTSTRFTFRTARQVPRLGVMLVGWGGNNGSTLTAAVLANRLRLSWPTRSGRKEANYYGSLTQAGTVSLGLDAEGQEVFVPFSAVLPMVAPNDLVFDGWDISSLNLAEAMRRAKVLDWGLQEQLWPHMEALRPRPSVYIPEFIAANQSARADNLIPGSRAQQLEQIRRDIRDFRSSAGLDKVIVLWTANTERFCEVIPGLNDTAENLLRTIELGLEVSPSTLFAVASILEGCAFLNGSPQNTLVPGALELAWQHRVFVGGDDFKSGQTKVKSVLVDFLIGSGLKTMSIVSYNHLGNNDGENLSAPLQFRSKEVSKSNVVDDMVQSNPVLYTPGEEPDHCVVIKYVPYVGDSKRALDEYTSELMLGGTNTLVLHNTCEDSLLAAPIMLDLALLTELCQRVSFCTDMDPEPQTFHPVLSLLSFLFKAPLVPPGSPVVNALFRQRSCIENILRACVGLPPQNHMLLEHKMERPGPSLKRVGPVAATYPMLNKKGPVPAATNGCTGDANGHLQEEPPMPTT
Protein: Diphosphomevalonate decarboxylase (EC 4.1.1.33) (Mevalonate pyrophosphate decarboxylase) (MPD) (Mevalonate-5-diphosphate decarboxylase) (MDD) (MDDase) (A0A1D8PC43)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Diphosphomevalonate decarboxylase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway. MVD1 converts diphosphomevalonate into isopentenyl diphosphate. The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
Interaction partners:
- Mevalonate kinase
- Isopentenyl-diphosphate delta-isomerase
- Farnesyl pyrophosphate synthase
- Phosphomevalonate kinase
- Farnesyltranstransferase
- Hydroxymethylglutaryl-CoA synthase
- Lanosterol synthase
- Squalene epoxidase ERG1
- Acetyl-CoA acetyltransferase
- Squalene synthase ERG9
Sequence:
MYSASVTAPVNIATLKYWGKRDKSLNLPTNSSISVTLSQDDLRTLTTASASESFEKDQLWLNGKLESLDTPRTQACLADLRKLRASIEQSPDTPKLSQMKLHIVSENNFPTAAGLASSAAGFAALVSAIAKLYELPQDMSELSKIARKGSGSACRSLFGGFVAWEMGTLPDGQDSKAVEIAPLEHWPSLRAVILVVSDDKKDTPSTTGMQSTVATSDLFAHRIAEVVPQRFEAMKKAILDKDFPKFAELTMKDSNSFHAVCLDSYPPIFYLNDTSKKIIKMVETINQQEVVAAYTFDAGPNAVIYYDEANQDKVLSLLYKHFGHVPGWKTHYTAETPVAGVSRIIQTSIGPGPQETSESLTK
Protein: Tropinone reductase homolog At2g29310 (EC 1.1.1.-) (Q9ZW14)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AGAMOUS-like 99
- MADS-box family protein
- MADS-box family protein
- AGAMOUS-like 89
- At3g12510
- MADS-box family protein
- strictosidine synthase
- Senescence-associated protein 13
- Protein STRICTOSIDINE SYNTHASE-LIKE 2
- Protein STRICTOSIDINE SYNTHASE-LIKE 11
Sequence:
MDKRWSLQGMTALVTGAASGIGYAIVEELASFGAIIHICDISETLLSQSLSEWEKKGFQVSGSICDVASRPDREKLMQTVSSLFDGKLNILVNNVGVIRGKPTTEYVAEDFSYHISTNLEPAFHFSQLSHLLLKASGFGSIVFMSSATGVVSVQCGSIYSLTKGALNQLTRNLACEWAKDGIRANAVAPNVVKTPLSQSYLEDVGFKEALFSRTPLGRAGEPNEVASLVVFLCLPAASYITGQTICIDGGFTVNAFSYKPQA
Protein: Histone-lysine N-methyltransferase set-9 (EC 2.1.1.-) (O44498)
Organism: Caenorhabditis elegans
Function: Histone methyltransferase (By similarity). Might play a role in transcriptional regulation. Together with set-26, negatively regulates lifespan in a germline-independent, partially daf-16-dependent fashion. Together with set-26, plays a role in germline development and maintenance and might play a role in the restriction of the trimethylation mark on histone H3 'Lys-4'(H3K4me3) to target genes specifically in the germline.
Subcellular location: Nucleus {ECO:0000269|PubMed:22212395, ECO:0000269|PubMed:29714684}.
Interaction partners:
- JmjC domain-containing protein
- SET domain-containing protein
- Histone-lysine N-methyltransferase set-2
- SET domain-containing protein
- Lysine-specific demethylase 4
- Histone-lysine N-methyltransferase set-25
- Set1/Ash2 histone methyltransferase complex subunit ash-2
Sequence:
MADGEHTLPADEELFEQPPPQQQQPEIAEPIVMAQEPIQGVSEDPQASEATHEAPDNYPVDHQMENQEFYHEPQIPEPQQIPQIPVFQPAAYNPPNYVAPQQRANNFGEPAAADARPLTEQEQLAAERPTEDTVWIDSDDDTDVEEAILRANFWLPYSDHNYDPPDPADRIILPTEGPFPCIAGLDEDCNIVKQWMPEDAVGPGSPGTQYRRNQQAGGGLPSTSVASQQQQLPVRHNIQNRPMVAAQPFSIGGNQVEYGGMDSRMQQRGVVRDGPQYRVMNDFGNGLPMRGLLPPRNSPAANAINRAREQQQQMYHQAGARGSLQQRAAPAPADPTPGSYQHIVNAVPGGGANPMRRVPPQARPGMIGGAANNNRARPTHVTRPMDTQEFEHPVAPAAAPPHRVVDVAPHRMTPEQRQELQQMNRQRAAPQFPAAAAQRSAEVIVIQQRPGASSRAPRPSMAQEDLLRSPTRRLSERVPQEHQTPVLEPRRFQVKVTDTYSTPIPKASDQLPAQLTEEDPPEESAAAAAPEDVPDAAPEDPPKVILKPTPPHRMTQEEKNAHFARLTTDKEKPTSSTSILPQDAAPPHVPPPPPPLVLRPHHQDETLAMVQSVFESKPRQPDTPKDKETISKIADLLRFSADEFTGQSGSSAAARQRTVSGSAARAQTYQMHHQQQQHHHQMPMDQRKRPSSGRYDALMGAMPLQQQPPPPPSQFQHTDSIAHRPRGRPKGTRHPSVAVQPQRSGGARTLPPRAQTVAMSARNGANAKNSDSESEGIDEAAEESWTMRCHCGMDHGDGDTIECEGCKTWQHMACMGLTLKSNTSKYKCEMCLPRRLPVSKAEAAREQERILNRLRAAARKQKRKSEPVEQKQKSSQPSTSRKSAPMALQQPAEPRVAQLNDYSKQASALLFGMEQTAGADTLLAESRLHKKARRMFVEEAVEALVTTDLVQIRQVILEVNGHVSMSSEVKRQPGGGNCIFMYDGLMKGTAGEDMGDGQELVCIDTKRKGNDTKFTRRSCVPNCVLKHVLGSNATLGIMIVATKDITRNTEVTLPFDADWRESEVELECAEHMKELQACPFESERRRFAAERHRAMDHKKQEAEEARRADEERRRLEEEVRRERAAKTKQMDEAEKARLEAEKAAEKEKKAKERKKMEASAAAAPESTNSITAREERRIQQAEEMFRRQEEEGKRKEARRRSKSVTPGVLEAAGTAAREDAPEASIPVPAPSPPASRRSVSRTTQPSTSSFATPTEPPAKNKRMRSVVPPKSEPASSAKRVRATTVATPKATTANDSRKRTASATGKTPVAKRSKNVAPTSFALALIEKELREQARNSTVLEMILPDYIMNEERSGLLAGQSPDFSEVRAQIEEENRMKERSRKREAKKKAVEKEKKEHRKEPKKTNEPGPAPKSEKAVEKAVEKVEKKPKSPQKPPAKPTAQNPPLKKTEEVDGIEREASESSSKESSVAPEEKKNPKKITFAEYNSRRSQKREAGECSTPPAVTRRGFIPSTEGEDLVNVELSAIPLDDHPSSSNTAPTTTIAPSVGGAPKPTSVVVKSPSTRSRTRGAASESADDAPAEHSMSLQDRVFSMFGSTVDAPAPPPPPASAETNSRRSRSTRWN
Protein: Flagellar protofilament ribbon protein, putative (Q57UY7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000256|ARBA:ARBA00004611}.
Interaction partners:
Sequence:
MEPAAETINVASNSSSLPQLETATTREKKRLFMMQRAERLKDPKMRHMGIDKEALDRQVREREALRQLEKERNDFYDRQALLMDRHAQALQKEVNEIRANREKQLLDYRETYQKKETQREWDLNDPHWKAKDLPGRVGDNDPRTGVSSLQKFEGEDLDYKNRRAAQQRQQREWARQQTEEKLAKKWMEEEANRVFDERNEETNRRIYDIEQGIAEQRRMIHKNQAEFNKALAEQKRREAIRDKEEDTRKALEEIRFHMEGDFLNETETVVSELGKKVKAERYKGMTEEQKRKFLEDRARQRDLLRRRRFMEVEEERRWAQQDNLQLRMANALERQKERERHAERLSIAAEQMKQREASQIRKKQLDELYTNQVDEDYFKYWDLCM
Protein: Uncharacterized protein YhaC (ORF B') (ORFX) (P11864)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YhaB
Sequence:
MFPVSSIGNDISSDLVRRKMNDLPESPTGNNLEALAPGIEKLKQTSIEMVTLLNTLQPGGKCIITGDFQKELAYLQNVILYNVSSLRLDFLGYNAQIIQRSDNTCELTINEPLKNQEISTGNININCPLKDIYNEIRRLNVIFSCGTGDIVDLSSLDLRNVDLDYYDFTDKHMANTILNPFKLNSTNFTNANMFQVNFVSSTQNATISWDYLLKITPVLISISDMYSEEKIKFVESCLNEPGDITEEQLKIMRFAIIKSIPRATLTDKLENELTKEIYKSSSKIINCLNRIKLTEMKEFSSEKIYDYIDIIIEDYENTKENAYLVVPQINYTMDLNIEDSSSEELLSDNTLEKDENSPDNGFEVGEYNTYEAYNSEKQYFTREDYTYDYDLLNAI
Protein: Apolipoprotein A-IV (Apo-AIV) (ApoA-IV) (Apolipoprotein A4) (P06727)
Organism: Homo sapiens (Human)
Function: May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons.
Subcellular location: Secreted.
Interaction partners:
- Apolipoprotein C-III
- Apolipoprotein E
- Apolipoprotein A-II
- Apolipoprotein B-100
- Apolipoprotein A-I
- Apolipoprotein C-II
- Clusterin
- Apolipoprotein C-I
- Apolipoprotein M
- Beta-2-glycoprotein 1
Sequence:
MFLKAVVLTLALVAVAGARAEVSADQVATVMWDYFSQLSNNAKEAVEHLQKSELTQQLNALFQDKLGEVNTYAGDLQKKLVPFATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVSQKIGDNLRELQQRLEPYADQLRTQVSTQAEQLRRQLTPYAQRMERVLRENADSLQASLRPHADELKAKIDQNVEELKGRLTPYADEFKVKIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRLAPLAEDVRGNLRGNTEGLQKSLAELGGHLDQQVEEFRRRVEPYGENFNKALVQQMEQLRQKLGPHAGDVEGHLSFLEKDLRDKVNSFFSTFKEKESQDKTLSLPELEQQQEQQQEQQQEQVQMLAPLES
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4 (EC 3.1.4.11) (Phosphoinositide phospholipase C-delta-4) (Phospholipase C-delta-4) (PLC-delta-4) (Q8K3R3)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Required for acrosome reaction in sperm during fertilization, probably by acting as an important enzyme for intracellular Ca(2+) mobilization in the zona pellucida-induced acrosome reaction. May play a role in cell growth. Modulates the liver regeneration in cooperation with nuclear PKC. Overexpression up-regulates the Erk signaling pathway and proliferation.
Subcellular location: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Localizes primarily to intracellular membranes mostly to the endoplasmic reticulum. {ECO:0000250}.
Interaction partners:
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Protein kinase C beta type
- Inositol polyphosphate multikinase
- Inositol polyphosphate-5-phosphatase A.
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1
- Protein kinase C gamma type
- Protein kinase C alpha type
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2
Sequence:
MTSQIQDLLATDQDLLLMQEGTMMRKVRTKSWKKLRYFRLQNDGMTVWHGSQPESMPKPTFSISDVERIRKGQDSELLRYLVEEFPLEQGFTVVFHGRRPNLDLVANSVEEAQIWMRGLQLLVDLVASMDHQEQMDQMLNEWFQQADRNQDGRMSFREAQRLLLLMNVEMDEEYAFSLFQEADVTQSDDLGSEEFVQFYKALTKRTEIEEIFEDFSSDKQKLTLLEFVDFLRKEQKEKDHAPDLALELIDRYEPSENGRLLHVLSKDGFLKYLCSKDGNIFNSDCLPIYQDMTQPLSHYYINSSHNTYLVGDQLCGQSSVEGYIRALKRGCRCVEVDTWDGPDGEPVVYHGHTLTSRILFKDVLATLAQYAFQSSDYPLILSLENHCTWEQQRTMAHHLTEILGEQLLRNTLEGLLVDSMPSPEQLRGKILVKGKKLRTIEVDKEEEEEEEEEELEKDEGPDLDPASPELDTQPQPETQGQAAGNKKERKKKVMKCPMSCLLICGHVMAQAPSSIPESILLSKQFLLLSSTTIMCPDLSALVVYLRTVPFCSFTHSKENYHIYDISSFSESKAKNLIKEAGNEFVQHNARQLCRVYPSGLRTDSSNFNPQEHWNVGCQMVAMNMQTAGSAMDICDGLFRQNGGSGYVLKPEFLRDTQSSFNPERPISLYKAQILVVQVISGQQLPKVDKTKETTVVDPLVKVELYGVPEDTKEQETSHVENNGINPYWGETFYFRLQVPELAMLRFVVKDYSRKSRNNFIGQYTLPWTCMKQGYRHVSLLSRDGTSLNPASIFVYTCMQEDLDMDEP
Protein: Anti-tumor lectin (EC 3.1.21.-) (AAL) (Q6WY08)
Organism: Cyclocybe aegerita (Black poplar mushroom) (Agrocybe aegerita)
Function: Anti-tumor lectin with DNase activity. Inhibits the growth of several tumor cell lines in vitro. Induces lymphocyte infiltration and necrosis of tumor cells in a mouse tumor model. Induces apoptosis in HeLa cells. Binds N-acetylneuraminyl lactose (N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucose).
Interaction partners:
Sequence:
QGVNIYNISAGTSVDLAAPVTTGDIVTFFSSALNLNAGAGNPNNTTLNLFAENGAYLLHIAFRLQENVIIFNSRQPDGPWLVEQRVSDVANQFAGIDGKAMVTVFDHGDKYQVVINEKTVIQYTKQISGLTLSLSYNATEETSIFSTVVEAVTYTGLA
Protein: Regulatory factor X associated ankyrin containing protein (F5GY33)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MELTQPAEDLIQTQQTPASELGDPEDPGEEAADGSDTVVLSLFPCTPEPVNPEPDASVSSPQAGSSLKHSTTLTNRQRGNEVSALPATLDCDNLVNKPDERGFTPLIWASAFGEIETVRFLLEWGADPHILAKERESALSLASTGGYTDIVGLLLERDVDINIYDWNGGTPLLYAVRGNHVKCVEALL
Protein: Thymidine kinase, cytosolic (EC 2.7.1.21) (P04184)
Organism: Mus musculus (Mouse)
Function: Cell-cycle-regulated enzyme of importance in nucleotide metabolism. Catalyzes the first enzymatic step in the salvage pathway converting thymidine into thymidine monophosphate. Transcriptional regulation limits expression to the S phase of the cell cycle and transient expression coincides with the oscillation in the intracellular dTTP concentration.
Subcellular location: Cytoplasm.
Interaction partners:
- Thymidylate synthase
- Thymidine kinase 2, mitochondrial
- Thymidylate kinase
- Deoxyuridine triphosphatase.
- Thymidine phosphorylase
- Deoxycytidylate deaminase
- Cytidine deaminase
- Uridine phosphorylase 1
- 5'
- UMP-CMP kinase
Sequence:
MSYINLPTVLPSSPSKTRGQIQVILGPMFSGKSTELMRRVRRFQIAQYKCLVIKYAKDTRYSNSFSTHDRNTMDALPACMLRDVTQESLGVAVIGIDEGQFFPDIVDFCEMMANEGKTVIVAALDGTFQRKAFGSILNLVPLAESVVKLTAVCMECFREAAYTKRLGLEKEVEVIGGADKYHSVCRLCYFKKSSAQTAGSDNKNCLVLGQPGEALVVRKLFASQQVLQYNSAN
Protein: Protein FAM32A (Ovarian tumor-associated gene 12) (OTAG-12) (Q9Y421)
Organism: Homo sapiens (Human)
Function: Isoform 1, but not isoform 2 or isoform 3, may induce G2 arrest and apoptosis. May also increase cell sensitivity to apoptotic stimuli.
Subcellular location: [Isoform 1]: Nucleus.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus.
Interaction partners:
- Pre-mRNA-splicing factor CWC22 homolog
- Pre-mRNA-splicing factor SLU7
- Pre-mRNA-splicing factor SYF2
- Pre-mRNA-processing factor 17
- Peptidyl-prolyl cis-trans isomerase-like 1
- PRKR-interacting protein 1
- Splicing factor Cactin
- Splicing regulator SDE2
- Pre-mRNA-processing-splicing factor 8
- NF-kappa-B-activating protein
Sequence:
MEAYEQVQKGPLKLKGVAELGVTKRKKKKKDKDKAKLLEAMGTSKKNEEEKRRGLDKRTPAQAAFEKMQEKRQMERILKKASKTHKQRVEDFNRHLDTLTEHYDIPKVSWTK