wanglab/gogpt-training-data huggingface dataset:
Protein: Aurora/IPL1-related protein kinase 2 (EC 2.7.11.1) (Serine/threonine-protein kinase aurora-B) (O01427)
Organism: Caenorhabditis elegans
Function: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of chromosome segregation and cytokinesis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation. Required for histone H3 phosphorylation during segregation of homologous chromosomes in meiosis and mitosis. Required for histone H3 'Ser-10' phosphorylation. Phosphorylates tlk-1 at 'Ser-634', which enhances its activity. Phosphorylates zen-4 at 'Ser-680'. Required for the recruitment of bub-1 to the ring-shaped domain between chromosomes during meiotic anaphase I. Also required for the localization of the condensin I complex subunit smc-4 to mitotic chromosomes. Acts at the spindle midzone and the midbody to prevent cleavage furrow regression upon chromatin obstructions during cytokinesis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9852156}. Chromosome {ECO:0000269|PubMed:18923084, ECO:0000269|PubMed:23684975, ECO:0000269|PubMed:25475837, ECO:0000269|PubMed:9852156}. Midbody {ECO:0000269|PubMed:23684975, ECO:0000269|PubMed:9852156}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:23684975, ECO:0000269|PubMed:9852156}. Note=Meiotic and mitotic chromosomes (PubMed:18923084, PubMed:9852156). During each division, relocates to the midbody microtubules (PubMed:23684975, PubMed:9852156). Localizes on chromosomes during metaphase and on the central spindle during anaphase (PubMed:23684975, PubMed:25475837). Localization to homologous chromosomes during segregation is dependent on lab-1 (PubMed:18923084). {ECO:0000269|PubMed:18923084, ECO:0000269|PubMed:23684975, ECO:0000269|PubMed:25475837, ECO:0000269|PubMed:9852156}.
Interaction partners:
- Incenp-like protein ICP-1
- Chromosomal passenger complex protein bir-1
- Chromosome segregation and cytokinesis defective protein 1
- Kinesin-like protein
- Kinesin-like protein klp-19
- Mitotic checkpoint serine/threonine-protein kinase bub-1
- Kinetochore protein Nuf2 homolog
- Kinesin-like protein
- Kinetochore protein ndc-80
- Protein regulator of cytokinesis 1
Sequence:
MENKPPVINLPEKETVNTPQKGGKFTINDFEIGRPLGKGKFGSVYLARTKTGHFHVAIKVLFKSQLISGGVEHQLEREIEIQSHLNHPNIIKLYTYFWDAKKIYLVLEYAPGGEMYKQLTVSKRFSEPTAAKYMYEIADALSYCHRKNVIHRDIKPENLLIGSQGELKIGDFGWSVHAPSNKRQTMCGTMDYLPPEMVNGADHSDAVDLWAIGVLCYEFLVGKPPFEHEDQSKTYAAIKAARFTYPDSVKKGARDLIGRLLVVDPKARCTLEQVKEHYWIQGMMEAKIRAEKQQKIEKEASLRNH
Protein: Endoglycoceramidase (EGCase) (EC 3.2.1.123) (Glycosphingolipid-specific enzyme) (GSL-specific enzyme) (Q6L6S1)
Organism: Hydra vulgaris (Hydra) (Hydra attenuata)
Function: Hydrolysis of the glycosidic linkage between oligosaccharides and ceramides of glycosphingolipids, optimal substrates appear to be the glycosphingolipids with a gangliotetraose structure.
Subcellular location: Secreted {ECO:0000269|PubMed:15320336}. Note=Released from digestive cells into the gastric cavity, and eventually into the surrounding medium, during the digestive process. {ECO:0000269|PubMed:15320336}.
Interaction partners:
Sequence:
MISVALIILFLAKVISGKSDDFISVNPETNMLIDGYGRERFFHGTNVVVKHFPFHPETTGFNKDTFSEDDMKILQKFGLNSIRLGMMLPGYVPKREEYNETYIKVIQSIVTTAAKYGIYTLLDMHQDVFSPKFCVEGMPDWIVNTQGAKDFPMPLHKPFNLDPKTGYPYPEDCAKFSWADYYFTEAAGQAFQNLYDNVDGLRDEWAQFWKKTADVFKEEPSVIGYELINEPFCGNVFKHPTLLIPGVADYLNLQPTYDALQKAIRQVDEEHNIFFEGVTWDFFEVGFTEVPGGKQYQNRSVLSYHYYEPPDFSKKLNFEARLLDLKRLKCGGFLTEMFTVGTDFNSMFEMFDLCDKFKQSWHGWMYKSYGCIEQNLGCLNMSSPGKESIQIANTSRTYPQAVAGRTQSYAFDIKTKVFTLVYETVGSCKSGRTIVYFNKNLHYPNGYRYEINPNFKVTPSENEYFLYLDEVNKVPNTVVTFKLFPLSFTDSEDIHPVTVMGDKHLSENHNENEKKKK
Protein: N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) (EC 1.2.1.38) (N-acetyl-glutamate semialdehyde dehydrogenase) (NAGSA dehydrogenase) (P9WPZ9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00150}.
Interaction partners:
- Acetylornithine aminotransferase
- Ornithine carbamoyltransferase
- Arginine biosynthesis bifunctional protein ArgJ
- Acetylglutamate kinase
- Arginine repressor
- Argininosuccinate lyase
- Argininosuccinate synthase
- Probable ornithine aminotransferase
- Glucose-1-phosphate adenylyltransferase
- Carbamoyl phosphate synthase large chain
Sequence:
MQNRQVANATKVAVAGASGYAGGEILRLLLGHPAYADGRLRIGALTAATSAGSTLGEHHPHLTPLAHRVVEPTEAAVLGGHDAVFLALPHGHSAVLAQQLSPETLIIDCGADFRLTDAAVWERFYGSSHAGSWPYGLPELPGARDQLRGTRRIAVPGCYPTAALLALFPALAADLIEPAVTVVAVSGTSGAGRAATTDLLGAEVIGSARAYNIAGVHRHTPEIAQGLRAVTDRDVSVSFTPVLIPASRGILATCTARTRSPLSQLRAAYEKAYHAEPFIYLMPEGQLPRTGAVIGSNAAHIAVAVDEDAQTFVAIAAIDNLVKGTAGAAVQSMNLALGWPETDGLSVVGVAP
Protein: Uncharacterized protein At1g63240 (Q949Y1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MLRQLPPTITADATPDWLPVGWIAHSTVLKRGRQTRTYTQLRTGKKLSTKDQVLEYIKMEKIREKREAGIKRNKASLKALQDKETASERPSWLPDERKAELEIGYVGGNPYKMNVNTSNDFNTNPKETVVLDENSMESEDSSGEVYETGCNEITYAIEEDEEDFSEREYVENVENFSNITSTPLRSQPERMQKLESRAKTQCVFEDEDLSSDSDNKLPEAETSKEGNGLGEGHVVSNLVESFEKKTSHGVMVECDDKAREIPGLTGSLTVEINLDCEPASDSLVEKNWNKSESDETGTRNIEIIDLESDVIHISGSSKAVEVTQESGDTSKEPLKAQEEPDNDWRSSVFFPDREAPSHSVLVFESSNARPSVEDLSNTIELGLTPQEKNISSSKKRKKNTERCASKNIKKKGIEAPSRKLQRGKTPSSKSHGKKGSSSVGMDKKPDDWLKPCPNFPFEPLTRSFQVEDDSAIRMYLEQHFAAPGSADSNLPLPDFGLPTFSDIKISLNEEPAFKKKKSPDPPCVQVASSNIPSCSSMGTSMLPTVAGH
Protein: Histone-lysine N-methyltransferase SETD7 (EC 2.1.1.364) (Histone H3-K4 methyltransferase SETD7) (H3-K4-HMTase SETD7) (SET domain-containing protein 7) (SET7/9) (Q8VHL1)
Organism: Mus musculus (Mouse)
Function: Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3 (By similarity). H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation (By similarity). Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription (By similarity). Has also methyltransferase activity toward non-histone proteins such as CGAS, p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II (By similarity). Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation (By similarity). Monomethylates 'Lys-491' of CGAS, promoting interaction between SGF29 and CGAS.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8WTS6}. Chromosome {ECO:0000250|UniProtKB:Q8WTS6}.
Interaction partners:
- Forkhead box protein O3
- Forkhead box protein O1
- Forkhead box protein O4
- Forkhead box protein O6
- Histone H3.2
- Histone H3.1
- T-box transcription factor TBX21
- NAD-dependent protein deacetylase sirtuin-1
- DNA
- Histone-lysine N-methyltransferase EHMT2
Sequence:
MDSDDEVVEEAVEGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDSDGRLIFKGQYKDNNRHGVCWIHYPDGGSLVGEVNEDGEMTGEKIAYVYPDQRTALYGKFIDGEMLEGKLATLMATEEGRPHFEVTSGSSVYHFDKSTSSCISSDALLPDPYESERVYVADSLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCVYDLFVHPRFGPIKCIRTLRAVEAEEELTVAYGYDHSPPGKSGPEAPEWYQVELKAFQATQQK
Protein: Kinesin (Q5MNW6)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MGLELISQVSVISVLEEVIQQHGNRIEDVANLVSRNTDEASLQRNDAAGWLRKTVGVVLGKDLPAEPSEEEFRLGLRSGKILCTVLNKIKPGSVPKVLEGPSDSIIIPDGAPLSPYQLENLRNFIAAIEEMGIPTFETSDLEQGGNSSRIVQSVLALKSYSEWKRSGGIGTWKYLENSKPPCFPKPKPFTRRNSEPFMHTFSRTMSLGDKSADSFNSEQSEISYAGSIPSLHLLVRAALLNKKQDEIPMIVESMIKKVSEEYERRLASHTELIKSSPKDTEESVPDNSLSRTASCGNVEVDIEVEAPAEEPIDDESSIESEKKELPNEECNTDEEATRHLLKQKTLVEQQRQHLLELKHSLHATKVGMELLQVTYREEFNNLGKHLHSIAYAAMGYQRVLEENRKLYNQVQDLKGSIRVYCRVRPSLSGQSNNLSCVEHIDDTTITVLTPTKTGKEGRKSFTFNKIFSPSVTQAEVFSDTQPLIRSVLDGYNVCIFAYGQTGSGKTYTMSGPTELTEEGLGVNYRALGDLFELSNQRKETISYEISVQMLEIYNEQVRDLLASDGLNKRLEIRNSSQNGINVPEAHLVRVSSTSDVINLMNLGQKNRTVFSTAMNDRSSRSHSCLTVHVQGKDLTSGNIIHGCMHLVDLAGSERVDKSEVMGDRLKEAQYINKSLSALGDVIAALASKGSHVPYRTSKLTQLLQDSLGGQAKPLMFVHIAPEYEASGETISTLKFAERVATVELGAAKVNKDSGEVKELKGQISSLKAALTTAKKEGEPEQLQRSQTISISSSPEIIIPSLGTSPSLPKSQSSSDHSSSVTNAENESSTTSRRDSLEIQEMLANPSLWPPLGKPASSAKEDNKDSASGRWNETLMVNKNDKKDPIPAAGNARWNPTKVYPEQNLNKLTANKNTKGNQDHDQQRIRPEIGSTDDSSDLDECSEIDSVWQSSIPKVTNNNSPNGLASKPKKQQYNHVAKPKSTDFKSAIPSLIPSPSTRKPSNGANPNTNKPKRKTGYSK
Protein: Fasciclin-like arabinogalactan protein 4 (Protein SALT OVERLY SENSITIVE 5) (Q9SNC3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be a cell surface adhesion protein that is required for normal cell expansion.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12509519}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12509519}.
Interaction partners:
- LRR receptor-like serine/threonine-protein kinase FEI 2
- LRR receptor-like serine/threonine-protein kinase FEI 1
- Hydroxyproline O-galactosyltransferase GALT5
- Hydroxyproline O-galactosyltransferase GALT2
- Cellulose synthase A catalytic subunit 5
- Fasciclin-like arabinogalactan protein 16
- Fasciclin-like arabinogalactan protein 18
- Hydroxyproline-rich glycoprotein family protein
- Fasciclin-like arabinogalactan protein 15
- Non-classical arabinogalactan protein 30
Sequence:
MANVISISHFTLLALPYLLLLLSSTAAAINVTAVLSSFPNLSSFSNLLVSSGIAAELSGRNSLTLLAVPNSQFSSASLDLTRRLPPSALADLLRFHVLLQFLSDSDLRRIPPSGSAVTTLYEASGRTFFGSGSVNVTRDPASGSVTIGSPATKNVTVLKLLETKPPNITVLTVDSLIVPTGIDITASETLTPPPTSTSLSPPPAGINLTQILINGHNFNVALSLLVASGVITEFENDERGAGITVFVPTDSAFSDLPSNVNLQSLPAEQKAFVLKFHVLHSYYTLGSLESITNPVQPTLATEEMGAGSYTLNISRVNGSIVTINSGVVLAVVTQTAFDQNPVSVFGVSKVLLPKELFPKSGQPVATAPPQEISLSPESSSEQPSRLVSPPREIVSSGAVKRPLGFLVLWCWCIAFCYVLV
Protein: NAC domain containing protein 50 (F4J3S6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGRESLAVVSSPPSATAPSTAVSATSLAPGFRFHPTDEELVSYYLKRKVLGKPVRFDAIGEVDIYKHEPWDLAEKILCSYLALNCFKNFVFACATVMFACATVMFALFSKLKTRDQEWYFFSALDKKYGNGARMNRATNKGYWKATGKDREIRRDIQLLGMKKTLVFHSGRAPDGLRTNWVMHEYRLVEYETETNGSLLQDAYVLCRVFHKNNIGPPSGNRYAPFMEEEWADGGGALIPGIDVRVRVEALPQANGNNQMDQWADLLKLHNSIKFAITFCRTQLNLTALSNERCSTREIFIVFWLICKEMHSASKDLININELPRDATPMDIEPNQQNHHESAFKPQESNNHSGYEEDEDTLKREHAEEDERPPSLCILNKEAPLPLLQYKRRRQNESNNNSSRNTQDHCSSTITTVDNTTTLISSSAAAATNTAISALLEFSLMGISDKKENQQKEETSPPSPIASPEEKVNDLQKEVHQMSVERETFKLEMMSAEAMISILQSRIDALRQENEELKKKNASGQAS
Protein: Phosphatidylserine decarboxylase proenzyme 3 (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase 3 beta chain; Phosphatidylserine decarboxylase 3 alpha chain] (O14111)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (By similarity). Together with psd1 and psd2, responsible for the majority of phosphatidylethanolamine synthesis.
Subcellular location: Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_03209}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03209}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03209}. Endosome membrane {ECO:0000255|HAMAP-Rule:MF_03209}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03209}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03209}. Cytoplasm {ECO:0000269|PubMed:16823372}. Note=Localizes at the barrier septum. {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized CDP-alcohol phosphatidyltransferase class-I family protein C22A12.10
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Phosphatidylserine decarboxylase proenzyme 2, mitochondrial
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Lysophospholipid acyltransferase
- Phospholipase D1
- Phosphatidyl-N-methylethanolamine N-methyltransferase
- Phosphatidylethanolamine N-methyltransferase
- Triacylglycerol lipase ptl3
- Putative phosphatidate cytidylyltransferase
Sequence:
MPFTKSCRSANTLRKGIKNGKLILKIIVNDIDNVESCLSGDESNDSKKSSASFYMKLKYGSYRALADNILSTDENRKEDIAVFDVPLPNGLQIDTFTLCLYRKSKWKKQIVGEAYIGIQALLLSTNPDETCKYPVISPPSGRNKENQSPSHQICNLSLKWIIYDPEDADADSKTLAKAWLQQIKMNQTSIDPMSNISKSLKELEVDNVESDLEDSSFIAEPDSSIPPSESSVSISTDTGKETPPSKSKKSSNQPYVSIGEGNSDLLGFVFLEIISVSNLPPLKNVFRTGFDMDPFVITAFSKNIFRTKWLRHNLNPVYNEKFLFEVGAFESNYDLVFKVVDHDKMSLNDSIAVGSFNVQSIINSSAQVDPETGLYSFNIETSSPSQDTSSKAEDSPTVQKIADDFSSAVGKDLRTDIIEQIIPLTLCCKHDFSTPRDVKLSFKAMFFPIAALRQKFWRVMLAQYGDIEDGHIGKLGMYAVLDTLGSNIPNSMVDDIYTELSSKNHDDTSDSITVDEAVICLERLVDLVCHQDQQATQTPQSPSSNEESGPGTPTQTSDQYEDSEDSRNFPSKLYLVYLSNCPLCLKFKLSKVNQQKATVHLATCASHDWKRVDRLMMTSYVSLNQAQRRWFSKAFAKVVYGSSKVGSTSATTLVQNRQTGQIQEEKMNAYVRIGIRLLYRGIRNRRIEGSKVKKILRSLTLKQGMKYDSPISVKEIKPFIRFFDLNMNEVDMPVGGFKTFNEFFYRKLKPGSRPCAFPDNPDILVSPADSRIVAYECIEKATTYWIKGTEFTVERLLGYSNEAQRFVGGSICISRLAPQDYHRFHSPVNGCIGPITKIEGQYYTVNPMAIRSYLDVFGENVRVLIPIDSNEFGKVMLVAVGAMMVGSTVLTVDEGKIVQRSDELGYFKFGGSTVITLFEPNVTSFDEDLLRNSKTKIETLVKMGERIGQKIDPNKPTDAEDHSKSDS
Protein: Increased recombination centers protein 21 (Q04772)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in resistance to carboplatin and cisplatin. Is probably involved in a pathway contributing to genomic integrity.
Interaction partners:
- Benzil reductase
Sequence:
MSSDGMNRDVSNSKPNVRFAAPQRLSVAHPAISSPLHMPMSKSSRKPLVRTKIRLDPGHSALDWHSLTSNPANYYTKFVSLQLIQDLLDDPVFQKDNFKFSPSQLKNQLLVQKIPLYKIMPPLRINRKIVKKHCKGEDELWCVINGKVYDISSYLKFHPGGTDILIKHRNSDDLITYFNKYHQWVNYEKLLQVCFIGVVCE
Protein: Transcription initiation factor TFIID subunit 5 (Transcription initiation factor TFIID 72 kDa subunit) (TAFII-72) (O13282)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: TAFs are components of the transcription factor IID (TFIID) complex that are essential for mediating regulation of RNA polymerase transcription. Regulates the genes involved in ubiquitin-dependent proteolysis during the progression of M-phase of mitosis.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- SAGA complex/transcription factor TFIID complex subunit Taf10
- SAGA complex/transcription factor TFIID complex subunit Taf12
- SAGA complex/transcription factor TFIID complex subunit Taf6
- SAGA complex/transcription factor TFIID complex subunit Taf9
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 7
- Transcription initiation factor TFIID subunit 8
- SAGA complex subunit Hfi1
- SAGA complex subunit Ngg1
- SAGA complex subunit Spt8
Sequence:
MSATNGPQPQDLNRIVLDYLAKKGYSRTEAMLRLEASGSGVSVEEKLKSIEETPDAYTHTYTILRDWVDSSLELYKAELHRILFPIFVHSYLNLLSQDHYEAAKQFYELFKDDHTDLHDFDVKNLKSLSLPSHVAEDRTAQQYRQNKYQLHFSRITFDLLLHFLFENVSNGGSIIIKLINQHIDIHIVPGRPTVLENAKVINEQEGITGQSFERGDAQLQPVKLQQMPMDKEMEKIVEMDLEEEDMMHQNDPNNQSPKLLKEFRKLHEPNAEDAPSRDYIPLPPHKGVDILSEVEAVKDWSKRLHLGPRASLPSVCMYTFHHTNNNMNCAEFSPDSTMIACGFQESYIRLWSIKADKKSLPKSTSVEDSDGSVRLLSHSGPVYGTTFSPDNKYLLSCSEDASARLWSVDTKTALVAYKGHTGPVWDVAFGPFGHYFATASHDQTAQLWSCDHIYPLRVFAGHLSDVDCVTFHPNSAYVLTGSSDKTCRLWDVHRGHSVRVFNGHTQPVTAVAIAPDGHTMASADSEGLIHLWDIGTGRRIKTMRGHRGNIYSLSFSRESTVLVSGGSDCTVRAWDVFKTNYNNPVSSSLTGSVVTPFSAKTSTFNEVNWSTSPDQMVALYTKQTPIFNVSFTRRNLCLAISVS
Protein: Tubulin gamma-1 chain (Gamma-1-tubulin) (Gamma-tubulin complex component 1) (GCP-1) (P83888)
Organism: Rattus norvegicus (Rat)
Function: Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation, centrosome duplication and spindle formation (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P23258}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P23258}. Note=Localizes to mitotic spindle microtubules. {ECO:0000250|UniProtKB:P23258}.
Interaction partners:
- Gamma-tubulin complex component
- Tubulin gamma complex component 3
- Gamma-tubulin complex component
- Protein NEDD1
- Gamma-tubulin complex component
- Gamma-tubulin complex component 6
- Mitotic spindle organizing protein 1.
- Tubulin gamma chain
- Serine/threonine-protein kinase PLK1
- HAUS augmin-like complex subunit 1
Sequence:
MPREIITLQLGQCGNQIGFEFWKQLCAEHGISPEGIVEEFATEGTDRKDVFFYQADDEHYIPRAVLLDLEPRVIHSILNSSYAKLYNPENIYLSEHGGGAGNNWASGFSQGEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQDEMSDVVVQPYNSLLTLKRLTQNADCVVVLDNTALNLIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFLMTGYTPLTTDQSVASVRKTTVLDVMRRLLQPKNVMVSTGRDRQTNHCYIAILNIIQGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVALSRKSPYLPSAHRVSGLMMANHTSISSLFERTCRQFDKLRKREAFMEQFRKEDIFKDNFDEMDTSREIVQQLIDEYHAATRPDYISWGTQEQ
Protein: Alpha-fibrinogenase A1 (EC 3.4.21.-) (Snake venom serine protease) (SVSP) (Q9PRW4)
Organism: Crotalus atrox (Western diamondback rattlesnake)
Function: Snake venom serine protease that completely cleaves fibrinogen Aalpha chain (FGA), partially cleaves Bbeta chain (FGB) and has no activity on gamma chain. Is more potent that A2 and A3 alpha-fibrinogenases. Very active within 5 minutes.
Subcellular location: Secreted {ECO:0000269|PubMed:8024586}.
Interaction partners:
Sequence:
VIGGDECNINEHRSLVAIFDS
Protein: Virion infectivity factor (Vif) (SOR protein) [Cleaved into: p17; p7] (P12504)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate NY5) (HIV-1)
Function: Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04081}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04081}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04081}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04081}. Virion {ECO:0000255|HAMAP-Rule:MF_04081}. Note=In the cytoplasm, seems to colocalize with intermediate filament vimentin. A fraction is associated with the cytoplasmic side of cellular membranes, presumably via the interaction with Pr55Gag precursor. Incorporated in virions at a ratio of approximately 7 to 20 molecules per virion. {ECO:0000255|HAMAP-Rule:MF_04081}.
Interaction partners:
Sequence:
MENRWQVMIVWQVDRMRINTWKRLVKHHMYISRKAKDWFYRHHYESTNPKISSEVHIPLGDAKLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPDLADQLIHLHYFDCFSESAIRNTILGRIVSPRCEYQAGHNKVGSLQYLALAALIKPKQIKPPLPSVRKLTEDRWNKPQKTKGHRGSHTMNGH
Protein: Uncharacterized protein LOC768186 (Zgc:153115) (A8E7A9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSFAYSDYLAAECLVSISSGPVLHRPTPVSGAAQAPPQGLPAGEPDGSSEDREVRETLRLDGANMMTVAEILTDLHGKFRPMSAYSESSNSSCGESGYTTLSDSTTPTPTMTPSATPVPGQSQQIWGGGGAPRSPTKRHPCTFDGCDRVYGKSSHLKAHIRTHTGERPFPCTWPECEKKFARSDELARHLRTHTGEKRFLCPLCDKRFMRSDHLIKHARRHPNFQPSMINRKGSAQGSISIQPAAASTAE
Protein: Terminase small subunit (G1P) (Terminase, small subunit) (P68928)
Organism: Bacillus phage SF6 (Bacteriophage SF6)
Function: The terminase small subunit specifically recognizes the non-adjacent pacL and pacR packaging subsites and regulates the ATPase activity of the terminase large subunit. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer once the capsid is full (headful packaging). Once the capsid is packaged with the DNA, the terminase complex is substituted by neck proteins.
Interaction partners:
Sequence:
MKEPKLSPKQERFIEEYFINDMNATKAAIAAGYSKNSASAIGAENLQKPAIRARIDARLKEINEKKILQANEVLEHLTRIALGQEKEQVLMGIGKGAETKTHVEVSAKDRIKALELLGKAHAVFTDKQKVETNQVIIVDDSGDAE
Protein: Disintegrin simusmin (C0HJM4)
Organism: Crotalus simus (Central American rattlesnake) (Caudisona simus)
Function: Inhibits ADP- (IC(50)=56 nM) and collagen-induced (IC(50)=49 nM) aggregation of human platelets. In vitro, inhibits adhesion of endothelial cells to vitronectin, type-I collagen and, to a lower degree, fibronectin and laminin.
Subcellular location: Secreted {ECO:0000269|PubMed:25457103}.
Interaction partners:
Sequence:
AGEECDCGSPANPCCDAATCKLRPGAQCADGLCCDQCRFIKKGTVCRPARGDWNDDTCTGQSADCPRNPFH
Protein: Ubiquitin-conjugating enzyme E2 32 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 32) (Ubiquitin carrier protein 32) (Q9LSP7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein OS-9 homolog
- Ubiquitin-conjugating enzyme E2 6
- ERAD-associated E3 ubiquitin-protein ligase component HRD3A
- ERAD-associated E3 ubiquitin-protein ligase HRD1A
- NEDD8-activating enzyme E1 catalytic subunit
- ERAD-associated E3 ubiquitin-protein ligase HRD1B
- Derlin-1
- Ubiquitin-like modifier-activating enzyme atg7
- Ubiquitin-like modifier-activating enzyme 5
- Probable ubiquitin-conjugating enzyme E2 26
Sequence:
MADERYNRKNPAVKRILQEVKEMQANPSDDFMSLPLEENIFEWQFAIRGPGDTEFEGGIYHGRIQLPADYPFKPPSFMLLTPNGRFETNTKICLSISNYHPEHWQPSWSVRTALVALIAFMPTSPNGALGSVDYPKDERRTLAIKSRETPPKYGSPERQKIIDEIHQYILSKATVVPKPLPLECSQAPSIVSEAHSQVEPQEAITVVEERSIATTDTIVDDQIIEETAEAVNTAASVVPAAAPLPAVEVVVKASVSGEQRMARRAAQKPVDDRLFTWAAVGLTIAIMVLLLKKFIKSNGYSTGFMDDQS
Protein: Sulfate adenylyltransferase subunit 2 (EC 2.7.7.4) (ATP-sulfurylase small subunit) (Sulfate adenylate transferase) (SAT) (P21156)
Organism: Escherichia coli (strain K12)
Function: With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
Interaction partners:
- Sulfite reductase hemoprotein beta-component
- Sulfate transport system permease protein CysW
- Adenylyl-sulfate kinase
- Thiosulfate-binding protein
- Sulfite reductase flavoprotein alpha-component
- Sulfate/thiosulfate import ATP-binding protein CysA
- Sulfate adenylyltransferase subunit 1
- Sulfate-binding protein
- Sulfate transport system permease protein CysT
- Phosphoadenosine 5'-phosphosulfate reductase
Sequence:
MDQIRLTHLRQLEAESIHIIREVAAEFSNPVMLYSIGKDSSVMLHLARKAFYPGTLPFPLLHVDTGWKFREMYEFRDRTAKAYGCELLVHKNPEGVAMGINPFVHGSAKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERIYSFRDRFHRWDPKNQRPELWHNYNGQINKGESIRVFPLSNWTEQDIWQYIWLENIDIVPLYLAAERPVLERDGMLMMIDDNRIDLQPGEVIKKRMVRFRTLGCWPLTGAVESNAQTLPEIIEEMLVSTTSERQGRVIDRDQAGSMELKKRQGYF