wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase chk1 (EC 2.7.11.1) (Checkpoint kinase 1) (P34208)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. Binds to and phosphorylates CDC25. This leads to negative regulation of CDC25 and prevents mitotic entry.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Protein kinase rad3
- DNA repair protein crb2
- Cell division control protein 45 homolog
- DNA replication licensing factor mcm4
- Mitosis inhibitor protein kinase wee1
- M-phase inducer phosphatase
- Exodeoxyribonuclease 1
- Serine/threonine-protein kinase cds1
- Checkpoint protein rad17
- ATP-dependent DNA helicase II subunit 1
Sequence:
MAQKLDNFPYHIGREIGTGAFASVRLCYDDNAKIYAVKFVNKKHATSCMNAGVWARRMASEIQLHKLCNGHKNIIHFYNTAENPQWRWVVLEFAQGGDLFDKIEPDVGIDEDVAQFYFAQLMEGISFMHSKGVAHRDLKPENILLDYNGNLKISDFGFASLFSYKGKSRLLNSPVGSPPYAAPEITQQYDGSKVDVWSCGIILFALLLGNTPWDEAISNTGDYLLYKKQCERPSYHPWNLLSPGAYSIITGMLRSDPFKRYSVKHVVQHPWLTSSTPFRTKNGNCADPVALASRLMLKLRIDLDKPRLASSRASQNDSGFSMTQPAFKKNDQKELDRVEVYGALSQPVQLNKNIDVTEILEKDPSLSQFCENEGFIKRLAKKAKNFYEICPPERLTRFYSRASRETIIDHLYDSLRLLAISVTMKYVRNQTILYVNLHDKRKCLLQGVIELTNLGHNLELINFIKRNGDPLEWRKFFKNVVSSIGKPIVLTDVSQN
Protein: Uncharacterized protein, isoform D (A0A0C4DHA5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Guanine nucleotide exchange factor subunit Rich
- Ras-related protein Rab6
- Golgin-245
Sequence:
MIEIKAKLLRADSAIYATGERVQCLIEFTHKVFSDEPAASQAVHNANEARSQENLAWASAQLHCYRKTSYSTSAGDRAAELTEMIGRTALDAVTQAPGEVIVATKPKILFCDLRLQPGETKMYFFNEFIPRDGPPTYRGHNIRYFYKITIATQRVKSKVQTLAVPIRVLPIPIISRPDELPVTVETNEELAPTNPFLEKREISELEISWHHLKNVTARRAPKFYRISNKRGFVGRFCLFKPAYKLGEDIVGSLDFDPGVNPRKVRCVQFSVKLQQQELSIRPQPVQNHQLQSQSSTGDDVSSMNSFDMASIASGVLADNLHKSATSASSKVKEAPEPTGKLSTISTSHQVCYATLQTQVVVPIPLHVTPTFRTDLVDVRWRLHFEFVTTTLIDFGIPNPESGELKAPSEMPVETMVWNLPVTVYAANPLQIYAPNQTFNLLIK
Protein: Polypeptide N-acetylgalactosaminyltransferase 16 (EC 2.4.1.41) (Polypeptide GalNAc transferase 16) (GalNAc-T16) (Polypeptide GalNAc transferase-like protein 1) (GalNAc-T-like protein 1) (pp-GaNTase-like protein 1) (Polypeptide N-acetylgalactosaminyltransferase-like protein 1) (Protein-UDP acetylgalactosaminyltransferase-like protein 1) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 1) (Q8N428)
Organism: Homo sapiens (Human)
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- C1GALT1-specific chaperone 1
Sequence:
MRKIRANAIAILTVAWILGTFYYLWQDNRAHAASSGGRGAQRAGRRSEQLREDRTIPLIVTGTPSKGFDEKAYLSAKQLKAGEDPYRQHAFNQLESDKLSPDRPIRDTRHYSCPSVSYSSDLPATSVIITFHNEARSTLLRTVKSVLNRTPANLIQEIILVDDFSSDPEDCLLLTRIPKVKCLRNDRREGLIRSRVRGADVAAATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVVSPIIDVISLDNFAYLAASADLRGGFDWSLHFKWEQIPLEQKMTRTDPTRPIRTPVIAGGIFVIDKSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFRKRHPYNFPEGNALTYIRNTKRTAEVWMDEYKQYYYEARPSAIGKAFGSVATRIEQRKKMNCKSFRWYLENVYPELTVPVKEALPGIIKQGVNCLESQGQNTAGDFLLGMGICRGSAKNPQPAQAWLFSDHLIQQQGKCLAATSTLMSSPGSPVILQMCNPREGKQKWRRKGSFIQHSVSGLCLETKPAQLVTSKCQADAQAQQWQLLPHT
Protein: Putative oxidoreductase YgfK (Putative oxidoreductase Fe-S subunit) (Q46811)
Organism: Escherichia coli (strain K12)
Function: Could be an iron-sulfur flavoprotein with NADPH:O(2) oxidoreductase activity.
Interaction partners:
- Uncharacterized protein YgfM
- Probable hypoxanthine oxidase XdhD
- Glutamate synthase large chain
- Putative aminohydrolase SsnA
- NAD
- Thioredoxin reductase
- Putative xanthine dehydrogenase FAD-binding subunit XdhB
- Sulfate adenylyltransferase subunit 2
- Putative dimethyl sulfoxide reductase chain YnfE
- D-phenylhydantoinase
Sequence:
MGDIMRPIPFEELLTRIFDEYQQQRSIFGIPEQQFYSPVKGKTVSVFGETCATPVGPAAGPHTQLAQNIVTSWLTGGRFIELKTVQILDRLELEKPCIDAEDECFNTEWSTEFTLLKAWDEYLKAWFALHLLEAMFQPSDSGKSFIFNMSVGYNLEGIKQPPMQQFIDNMMDASDHPKFAQYRDTLNKLLQDDAFLARHGLQEKRESLQALPARIPTSMVHGVTLSTMHGCPPHEIEAICRYMLEEKGLNTFVKLNPTLLGYARVREILDVCGFGYIGLKEESFDHDLKLTQALEMLERLMALAKEKSLGFGVKLTNTLGTINNKGALPGEEMYMSGRALFPLSINVAAVLSRAFDGKLPISYSGGASQLTIRDIFDTGIRPITMATDLLKPGGYLRLSACMRELEGSDAWGLDHVDVERLNRLAADALTMEYTQKHWKPEERIEVAEDLPLTDCYVAPCVTACAIKQDIPEYIRLLGEHRYADALELIYQRNALPAITGHICDHQCQYNCTRLDYDSALNIRELKKVALEKGWDEYKQRWHKPAGSGSRHPVAVIGAGPAGLAAGYFLARAGHPVTLFEREANAGGVVKNIIPQFRIPAELIQHDIDFVAAHGVKFEYGCSPDLTIEQLKNQGFHYVLIATGTDKNSGVKLAGDNQNVWKSLPFLREYNKGTALKLGKHVVVVGAGNTAMDCARAALRVPGVEKATIVYRRSLQEMPAWREEYEEALHDGVEFRFLNNPERFDADGTLTLRVMSLGEPDEKGRRRPVETNETVTLLVDSLITAIGEQQDTEALNAMGVPLDKNGWPDVDHNGETRLTDVFMIGDVQRGPSSIVAAVGTARRATDAILSRENIRSHQNDKYWNNVNPAEIYQRKGDISITLVNSDDRDAFVAQEAARCLECNYVCSKCVDVCPNRANVSIAVPGFQNRFQTLHLDAYCNECGNCAQFCPWNGKPYKDKITVFSLAQDFDNSSNPGFLVEDCRVRVRLNNQSWVLNIDSKGQFNNVPPELNDMCRIISHVHQHHHYLLGRVEV
Protein: Killer cell lectin-like receptor subfamily C, member 3 (L7N477)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
Sequence:
MSHLLGTEQASEPRKATKKTQAQLRFSNAAGDRLLEFSLQHASQKHLKASRHGYCKNFASPPEKLIAGILGTIWFTLLIALVISTRIVSPSQTYALCPKEWILYSHNCYYIGMERKSWNDSLVSCISKNCSLLYIDSEEEQDFLQSLSLVSWTGILRKGRGQPWVWKKDSTFKPKIAEILHDECNCAMMSASGLTADSCTTLHPYLCKCKFPI
Protein: Resistin-like alpha (Cysteine-rich secreted protein A12-gamma) (Cysteine-rich secreted protein FIZZ1) (Hypoxia-induced mitogenic factor) (Parasite-induced macrophage novel gene 1 protein) (RELMalpha) (Q9EP95)
Organism: Mus musculus (Mouse)
Function: Probable hormone. Plays a role in pulmonary vascular remodeling.
Subcellular location: Secreted.
Interaction partners:
- Chitinase-like protein 3
- Arginase-1
- Macrophage mannose receptor 1
- Macrophage galactose N-acetyl-galactosamine specific lectin 2
- Interleukin-4
- Acidic mammalian chitinase
- Interleukin-13
- Tumor necrosis factor
- Chitinase-like 6
- Chitotriosidase-1
Sequence:
MKTTTCSLLICISLLQLMVPVNTDETIEIIVENKVKELLANPANYPSTVTKTLSCTSVKTMNRWASCPAGMTATGCACGFACGSWEIQSGDTCNCLCLLVDWTTARCCQLS
Protein: Arylacetamide deacetylase (EC 3.1.1.3) (P22760)
Organism: Homo sapiens (Human)
Function: Displays cellular triglyceride lipase activity in liver, increases the levels of intracellular fatty acids derived from the hydrolysis of newly formed triglyceride stores and plays a role in very low-density lipoprotein assembly. Displays serine esterase activity in liver. Deacetylates a variety of arylacetamide substrates, including xenobiotic compounds and procarcinogens, converting them to the primary arylamide compounds and increasing their toxicity.
Subcellular location: Endoplasmic reticulum membrane; Single-pass type II membrane protein. Microsome membrane; Single-pass type II membrane protein.
Interaction partners:
- Arylamine N-acetyltransferase 2
- Arylamine N-acetyltransferase 1
Sequence:
MGRKSLYLLIVGILIAYYIYTPLPDNVEEPWRMMWINAHLKTIQNLATFVELLGLHHFMDSFKVVGSFDEVPPTSDENVTVTETKFNNILVRVYVPKRKSEALRRGLFYIHGGGWCVGSAALSGYDLLSRWTADRLDAVVVSTNYRLAPKYHFPIQFEDVYNALRWFLRKKVLAKYGVNPERIGISGDSAGGNLAAAVTQQLLDDPDVKIKLKIQSLIYPALQPLDVDLPSYQENSNFLFLSKSLMVRFWSEYFTTDRSLEKAMLSRQHVPVESSHLFKFVNWSSLLPERFIKGHVYNNPNYGSSELAKKYPGFLDVRAAPLLADDNKLRGLPLTYVITCQYDLLRDDGLMYVTRLRNTGVQVTHNHVEDGFHGAFSFLGLKISHRLINQYIEWLKENL
Protein: Inner membrane complex protein 1h, putative (Q8I5J9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MSYQDVQEKKNEDINYDEIASSMLEKMDKHINGEKQPTIHYENLNVQEQEGAHAYYSNQDINNINSSMSFLKNVKELNSSNILDHRTTTNDVGYPRRVMTALGPLPLPEEFKKNIPEKFVAKPIIEEREIYVSKKERKQREIEIPHVKYEHTFEKVKKQLKVNKLVPNVTQVIKEVPKEILKPVIEEKIIEVPQGVKYVEVPVEVPCLYPPKIMPKVVTQYVERIVETIKPVVQEKIIEVPQTVIKQVPKIKTVEVPYYVPRYVEKIIEVPFKPNGEMPKIATHLPISISDSLPPLKPTHILSAQNEKNITKHNNNMNSNNMNNMNPFQTTNFMMPLMNCFQQNPDPNTLKNSENGIPNMNMSPTILRPINSRDTPNNNMNPQEHIKNNITPYPNNSLNSNFTNYNMPQNLYSQIENLPHAHNLPDGFQWQYPDGVSNNPLCNTRNMPSLVVTCPPQIGRVTCTRKDIQPDILTKTGVYEFDGFKKKGTSQSLFPPLAHHNRVPFLPAPAAPGTPDIENIEKNM
Protein: Homeobox protein PKNOX2 (Homeobox protein PREP-2) (PBX/knotted homeobox 2) (Q96KN3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:11549286}.
Interaction partners:
- Pre-B-cell leukemia transcription factor 1
- ATP-dependent RNA helicase DDX25
- Centriolar and ciliogenesis-associated protein HYLS1
- Homeobox protein Hox-B1
- Pre-B-cell leukemia transcription factor 2
- Homeobox protein Hox-B2
- Pre-B-cell leukemia transcription factor 3
- Pre-B-cell leukemia transcription factor 4
- LIM homeobox transcription factor 1-beta
Sequence:
MMQHASPAPALTMMATQNVPPPPYQDSPQMTATAQPPSKAQAVHISAPSAAASTPVPSAPIDPQAQLEADKRAVYRHPLFPLLTLLFEKCEQATQGSECITSASFDVDIENFVHQQEQEHKPFFSDDPELDNLMVKAIQVLRIHLLELEKVNELCKDFCNRYITCLKTKMHSDNLLRNDLGGPYSPNQPSINLHSQDLLQNSPNSMSGVSNNPQGIVVPASALQQGNIAMTTVNSQVVSGGALYQPVTMVTSQGQVVTQAIPQGAIQIQNTQVNLDLTSLLDNEDKKSKNKRGVLPKHATNIMRSWLFQHLMHPYPTEDEKRQIAAQTNLTLLQVNNWFINARRRILQPMLDASNPDPAPKAKKIKSQHRPTQRFWPNSIAAGVLQQQGGAPGTNPDGSINLDNLQSLSSDSATMAMQQAMMAAHDDSLDGTEEEDEDEMEEEEEEELEEEVDELQTTNVSDLGLEHSDSLE
Protein: N-acylglucosamine 2-epimerase (AGE) (EC 5.1.3.8) (GlcNAc 2-epimerase) (N-acetyl-D-glucosamine 2-epimerase) (Renin-binding protein) (RnBP) (P82343)
Organism: Mus musculus (Mouse)
Function: Catalyzes the interconversion of N-acetylglucosamine to N-acetylmannosamine. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway.
Interaction partners:
- N-acetyl-D-glucosamine kinase
- Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
- N-acetylneuraminate lyase
- N-acetylneuraminate-9-phosphate synthase
- Beta-hexosaminidase subunit alpha
- Beta-hexosaminidase subunit beta
- Chitotriosidase-1
- Chitinase-like 6
- Acidic mammalian chitinase
- UDP-N-acetylhexosamine pyrophosphorylase-like protein 1
Sequence:
MEKERETLQVWKKRVEQELDRVIAFWMEHSHDQEHGGFFTCLGRDGKVYDHLKYVWLQGRQVWMYCRLYRSFERFRRVELLDAARAGGEFLLRYARVAPPGKKCAFVLTRDGRPVKVQRTIFSECFYTMAMNELWKVTGEVRYQSEAIEMMDQIIHWVREDPAGLGRPQLSGALATEPMAVPMMLLSLVEQLGEEDEELTNMYAELGDWCVHRILQHVQRDGQVVLENVSEDGKELPGCLGRHQNPGHTLEAGWFLLQYALRKGDPKLRMHIIDKFLLLPFHSGWDPEHGGLFYFQDADGLCPTQLEWNMKLWWPHSEAMIAFLMGYSDSGDPALLHLFYKVAEYTFRQFRDPEYGEWFGYLNQEGKVALTIKGGPFKGCFHVPRCLAMCEQILGALLQRLEPAPLDSSPAVSTHEGSK
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9SV69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Serine/threonine-protein kinase OXI1
- Serine/threonine-protein kinase PEPKR2
- Kinase superfamily with octicosapeptide/Phox/Bem1p domain-containing protein
- G-type lectin S-receptor-like serine/threonine-protein kinase At1g61440
- L-type lectin-domain containing receptor kinase IV.3
- Protein kinase superfamily protein
- Leucine-rich repeat protein kinase family protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein T14D3.50
Sequence:
MSNHLLPPENKIPTLNFDHLEIFSALGRGSKGVVFLVKADNKWLALKVILRESIESKKAKDEYKRISFEQGVLSRFDHPLFPRLHGVISTDKVIGYAIDYCPGRDLNSLRKKQSEEMFSDEIIRFYAAELVIALEYLHNQGIVYRDLKPDNVMIQENGHLMLVDFDLSTNLPPRTPQSSFSSSPRLSTATKKERSIFAFSGLCNSGISPDDSVSRSSESEFSGEKSNSFVGTEEYVAPEVITGSGHDFAVDWWSLGVVLYEMLYGATPFRGSNRKETFLKILTEPPSLVGETTSLRDLVRKLLEKDPSRRINVEGIKGHDFFKGLDWDLVLKVSRPPYIPAPENYEISKIDVEKFVHEIFTKCEHNGNFIVF
Protein: Trehalose-phosphatase (EC 3.1.3.12) (Trehalose synthase complex catalytic subunit TPS2) (Trehalose-6-phosphate phosphatase) (TPP) (P31688)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Phosphatase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Trehalose synthase complex regulatory subunit TPS3
- Alpha,alpha-trehalose-phosphate synthase 56 kDa subunit
- Trehalose synthase complex regulatory subunit TSL1
- Cytosolic neutral trehalase
- Glycogen [starch] synthase isoform 2
- Glycogen [starch] synthase isoform 1
- Probable trehalase
- UTP--glucose-1-phosphate uridylyltransferase
- Periplasmic acid trehalase ATH1
- Probable UTP--glucose-1-phosphate uridylyltransferase
Sequence:
MTTTAQDNSPKKRQRIINCVTQLPYKIQLGESNDDWKISATTGNSALFSSLEYLQFDSTEYEQHVVGWTGEITRTERNLFTREAKEKPQDLDDDPLYLTKEQINGLTTTLQDHMKSDKEAKTDTTQTAPVTNNVHPVWLLRKNQSRWRNYAEKVIWPTFHYILNPSNEGEQEKNWWYDYVKFNEAYAQKIGEVYRKGDIIWIHDYYLLLLPQLLRMKFNDESIIIGYFHHAPWPSNEYFRCLPRRKQILDGLVGANRICFQNESFSRHFVSSCKRLLDATAKKSKNSSNSDQYQVSVYGGDVLVDSLPIGVNTTQILKDAFTKDIDSKVLSIKQAYQNKKIIIGRDRLDSVRGVVQKLRAFETFLAMYPEWRDQVVLIQVSSPTANRNSPQTIRLEQQVNELVNSINSEYGNLNFSPVQHYYMRIPKDVYLSLLRVADLCLITSVRDGMNTTALEYVTVKSHMSNFLCYGNPLILSEFSGSSNVLKDAIVVNPWDSVAVAKSINMALKLDKEEKSNLESKLWKEVPTIQDWTNKFLSSLKEQASSNDDMERKMTPALNRPVLLENYKQAKRRLFLFDYDGTLTPIVKDPAAAIPSARLYTILQKLCADPHNQIWIISGRDQKFLNKWLGGKLPQLGLSAEHGCFMKDVSCQDWVNLTEKVDMSWQVRVNEVMEEFTTRTPGSFIERKKVALTWHYRRTVPELGEFHAKELKEKLLSFTDDFDLEVMDGKANIEVRPRFVNKGEIVKRLVWHQHGKPQDMLKGISEKLPKDEMPDFVLCLGDDFTDEDMFRQLNTIETCWKEKYPDQKNQWGNYGFYPVTVGSASKKTVAKAHLTDPQQVLETLGLLVGDVSLFQSAGTVDLDSRGHVKNSESSLKSKLASKAYVMKRSASYTGAKV
Protein: Cytochrome c oxidase assembly protein COX16 homolog, mitochondrial (hCOX16) (Q9P0S2)
Organism: Homo sapiens (Human)
Function: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Promotes the insertion of copper into the active site of cytochrome c oxidase subunit II (MT-CO2/COX2). Interacts specifically with newly synthesized MT-CO2/COX and its copper center-forming metallochaperones SCO1, SCO2 and COA6. Probably facilitates MT-CO2/COX2 association with the MITRAC assembly intermediate containing MT-CO1/COX1, thereby participating in merging the MT-CO1/COX1 and MT-CO2/COX2 assembly lines.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:29355485, ECO:0000269|PubMed:29381136}; Single-pass membrane protein {ECO:0000305|PubMed:29381136}.
Interaction partners:
- Cytochrome c oxidase assembly factor 3 homolog, mitochondrial
- Voltage-gated monoatomic cation channel TMEM109
- Glutamyl-tRNA
- Cytochrome c oxidase assembly factor 6 homolog
- Cytochrome c oxidase copper chaperone
- Cytochrome c oxidase assembly protein COX18, mitochondrial
Sequence:
MFAPAVMRAFRKNKTLGYGVPMLLLIVGGSFGLREFSQIRYDAVKSKMDPELEKKLKENKISLESEYEKIKDSKFDDWKNIRGPRPWEDPDLLQGRNPESLKTKTT
Protein: Dynactin subunit 4 (Dyn4) (Dynactin subunit p62) (Q9UJW0)
Organism: Homo sapiens (Human)
Function: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10671518}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10671518}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q9QUR2}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9QUR2}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:Q8CBY8}. Note=Has a punctate cytoplasmic distribution as well as centrosomal distribution typical of dynactin (PubMed:10671518). Overexpression in cultured mammalian cells revealed colocalization with cortical actin, stress fibers, and focal adhesion sites, sites of potential interaction between microtubules and the cell cortex (By similarity). In skeletal muscles, costamere localization requires the presence of ANK2 (By similarity). {ECO:0000250|UniProtKB:Q8CBY8, ECO:0000250|UniProtKB:Q9QUR2, ECO:0000269|PubMed:10671518}.
Interaction partners:
- Dynactin subunit 6
- Dynactin subunit 5
- Actin-related protein 10
- Dynactin subunit 1
- Dynactin subunit 2
- Alpha-centractin
- Beta-centractin
- Dynactin subunit 3
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit alpha-1
Sequence:
MASLLQSDRVLYLVQGEKKVRAPLSQLYFCRYCSELRSLECVSHEVDSHYCPSCLENMPSAEAKLKKNRCANCFDCPGCMHTLSTRATSISTQLPDDPAKTTMKKAYYLACGFCRWTSRDVGMADKSVASGGWQEPENPHTQRMNKLIEYYQQLAQKEKVERDRKKLARRRNYMPLAFSDKYGLGTRLQRPRAGASISTLAGLSLKEGEDQKEIKIEPAQAVDEVEPLPEDYYTRPVNLTEVTTLQQRLLQPDFQPVCASQLYPRHKHLLIKRSLRCRKCEHNLSKPEFNPTSIKFKIQLVAVNYIPEVRIMSIPNLRYMKESQVLLTLTNPVENLTHVTLFECEEGDPDDINSTAKVVVPPKELVLAGKDAAAEYDELAEPQDFQDDPDIIAFRKANKVGIFIKVTPQREEGEVTVCFKMKHDFKNLAAPIRPIEESDQGTEVIWLTQHVELSLGPLLP
Protein: Zinc finger protein 485 (Q8NCK3)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MAPRAQIQGPLTFGDVAVAFTRIEWRHLDAAQRALYRDVMLENYGNLVSVGLLSSKPKLITQLEQGAEPWTEVREAPSGTHAVEDYWFETKMSALKQSTSEASVLGERTKSVMMEKGLDWEGRSSTEKNYKCKECGKVFKYNSSFISHQRNHTSEKPHKCKECGIAFMNSSSLLNHHKVHAGKQPYRCIECGKFLKKHSTFINHQRIHSREKPHKCIECGKTFRKNSILLSHQRIHTGQKPYKCNDCGKAFAQNAALTRHERIHSGEKPFKCNKCGRAFRDNSTVLEHQKIHTGEKPYQCNECGKAFRKSSTLISHQRMHTGEKPYHCSKCGKSFRYSSSFAGHQKTHSGNKPYQCRDCGKAFTKSSTLTGHQRIHTGEKPYHCKKCGKAFRHSSGLVEHQRLHTGEKPYKCNECGKAFPRSSALKQHKKIHNKERAMKCS
Protein: X-ray repair cross-complementing protein 5 (EC 3.6.4.-) (ATP-dependent DNA helicase 2 subunit ku80) (Q54LY5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in non-homologous end joining (NHEJ) DNA double strand break repair.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P13010}.
Interaction partners:
- ATP-dependent DNA helicase ku70
- DNA 3'-5' helicase
- DNA ligase 4
- DNA-dependent protein kinase catalytic subunit
- Double-strand break repair protein
- DNA cross-link repair 1 protein
- BRCT domain-containing protein
- Telomerase reverse transcriptase
- Exonuclease 1
- Poly [ADP-ribose] polymerase
Sequence:
MTTTIPLKEAVVVILDIGLGMTSKDSDGTTTTTSSIEDALRSVTLLYQQKLIYGKKDQLGLVLIGTKGTKNNLQDDGYQHITVVSDIEEPSIETLKYLENLAPGESKGDVIDSLIVAMDMLIRKTENKKYQKRIFLVTNARDPINTEDLSIVRDQFKKIDVKLNIIGVDFLEEIEENNMDTSNNNKNKSLKEKNEIFLREFAESVDGVLVPVKQALEMMSFFRSQSVMTRTSFRGALEITPELKIPVWGYLKMKQQLLPSLKKISSIAQQQIEQQQQQQQQQNKNKNNEDNEDNEEGKPNITLDVNQEVSYYSITDPDNEILKPDLLKGYKYGKSLIPFSKIDEDQLKYSSSKCLKVVGFTDRKSIPIYYNMGNTEVFVSQPGDKQSEEALSSFIHALVETDQVMVVRYVKTMNGSPYLGYMIPHVKSDYVCLYYNHLPLADDIRQYQFPPISPKNPLTRKSNIPNAEQLEATQQLIDSMDLMKSEFDEDGDPIQMLKPRFTYNPLLQHFYQCLHHRSLHPNTQIPKLDPIIAEYINPDQIIMNKSKQSIKNFADKFPLTKTTVFSKTPAISGGNTNGTTSNTNNTMIGGVKYHWKDGMLIGEEINLDSYVTDDGSEAKKRKVNDFSEFSLDKLVSGYVTEVGTINPVQNFKDMLNRRDMDLVDKAITLMKERILQLVNDSLRDQYYQKAFECIKELRVGCIRESEAEQFNGFLKDMRSLFQSKKRDDFWQYITADVTSILGEKSINLITQDECDSSEVTQEELDQFLDKKVKQFNPPPITNVNTDSVDDLFDQIE
Protein: Citrate synthase (Q9DAM4)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
Sequence:
MALLTAAAWFLGTKNPPCLVLAARHASASSTNLKDVLRNLIPKEQARIKTFRKKHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAKGGKEPLPEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTKLHPMSQLSAAITVLNNESNFARAYAQGMNRTKYWELTYEDCMDLLAKLPCVAAKIYRNLYREDRNIEAIDSKLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWLTQLQKEVGEDASDEKLKNYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPKDPMFKLVGQLYKIVPDILLEQGKVKNPWPNVDAHSGVLLQYYGMREMNYYTVLFGVSRALGVLSQLIWSRALGFPLERPKSMSTDALMKFVNSESG
Protein: Beta-1,4-galactosyltransferase 7 (Beta-1,4-GalTase 7) (Beta4Gal-T7) (b4Gal-T7) (EC 2.4.1.-) (Proteoglycan UDP-galactose:beta-xylose beta1,4-galactosyltransferase I) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 7) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 7) (UDP-galactose:beta-xylose beta-1,4-galactosyltransferase) (XGPT) (XGalT-1) (Xylosylprotein 4-beta-galactosyltransferase) (EC 2.4.1.133) (Xylosylprotein beta-1,4-galactosyltransferase) (Q9UBV7)
Organism: Homo sapiens (Human)
Function: Required for the biosynthesis of the tetrasaccharide linkage region of proteoglycans, especially for small proteoglycans in skin fibroblasts.
Subcellular location: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Cis cisternae of Golgi stack.
Interaction partners:
- Beta-1,3-galactosyltransferase 6
- Xylosyltransferase 2
- Xylosyltransferase 1
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
- Adenosine 3'-phospho 5'-phosphosulfate transporter 1
- Carbohydrate sulfotransferase 14
- Zinc transporter ZIP13
Sequence:
MFPSRRKAAQLPWEDGRSGLLSGGLPRKCSVFHLFVACLSLGFFSLLWLQLSCSGDVARAVRGQGQETSGPPRACPPEPPPEHWEEDASWGPHRLAVLVPFRERFEELLVFVPHMRRFLSRKKIRHHIYVLNQVDHFRFNRAALINVGFLESSNSTDYIAMHDVDLLPLNEELDYGFPEAGPFHVASPELHPLYHYKTYVGGILLLSKQHYRLCNGMSNRFWGWGREDDEFYRRIKGAGLQLFRPSGITTGYKTFRHLHDPAWRKRDQKRIAAQKQEQFKVDREGGLNTVKYHVASRTALSVGGAPCTVLNIMLDCDKTATPWCTFS
Protein: PcfC (Q5G3N9)
Organism: Enterococcus faecalis (Streptococcus faecalis)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MQTYKKELKPYLYLGVFLFVIGFGIGNFFWLLPGTDYFSKTNYLFTKDILTYIEQTFYRFFITPSLLGFSVGVLGFLLGLLMYVRDNDRGIYRHGEEYGSARFATPAEMKKYEDPIPENNIIVSKHVKISLFNKRLPIKLQKNKNIAILGDSGAAKTLAFIKTNLMQRHASFITTDPDGGILPEIGLLLKKGKYKIKVLDLNTLSNSDTFNVFEYMHSELDVDRVLEAVTEATKEVEKTTGDDFWIKAEGLLVRSLIAYLWFDGRRNDYTPHLGMIADMLRHLKRKDKNVPSPVEEWFEELNEAIPDNYAYRQWTLFNNLYESETRASVLGIAAARYSVFDHEEVVNMIRTDTMDIDSWNEEKTAVFIAIPETNTSFNFIAALMFATVGEVLRNKSDQVRLGKRVLEEGKELLHVRFLIDEFANIGRIPHFEKMLTTFRKREMSFTIVLQSLNQLQTLYRNGWQNILNGCACLLYLGGDEEETTKYLSARAGKQTLSIRKHSMNKGNQGGGSENRDKYGRDLIDRSEVALIGGDECLVFISKEHVFKDKKFYAFQHDRADELATGPTDDKWYTWRRYMTDEEAILDKISATDIIDHGEITSELKEETHV
Protein: Extracellular glycosidase UTR2 (EC 3.2.-.-) (Cell-surface factor 4) (Q5AJC0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Extracellular glycosidase which plays an important role in fungal pathogenesis. Involved in cell wall assembly and regeneration, filamentation, and adherence to host cells. Plays a role of cell surface antigen in acute candidemia patients.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:16455273, ECO:0000269|PubMed:18227255, ECO:0000269|PubMed:18712765, ECO:0000269|PubMed:20641015, ECO:0000269|PubMed:20864472, ECO:0000269|PubMed:21602216, ECO:0000269|PubMed:23243062}. Membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
Interaction partners:
- Small ribosomal subunit protein eS21
- 1,3-beta-glucanosyltransferase PGA4
- pH-responsive protein 2
- Coatomer subunit alpha
Sequence:
MRFSTLHFAFLATLSSIFTVVAASDTTTCSSSKHCPEDKPCCSQFGICGTGAYCLGGCDIRYSYNLTACMPMPRMSTFQESFDSKDKVKEIELQSDYLGNSTEADWVYTGWVDYYDNSLLIQMPNHTTGTVVSSTKYLWYGKVGATLKTSHDGGVVTAFILFSDVQDEIDYEFVGYNLTNPQSNYYSQGILNYNNSRNSSVNNTFEYYHNYEMDWTEDKIEWYIDGEKVRTLNKNDTWNETSNRYDYPQTPSRIQFSLWPGGDSSNAKGTIEWAGGLINWDSEDIKKYGYYYAHIKEIYATAYDIPNDVKLDGNSTKESDYHAFLYNSTDGDASNIMLTTKKTWLGSDDATGFDPQNDDEDSSSNKAQETTITSVSGSSTITSVKTDSTKKTANVPAQNTAAAAQATAKSSTGTNTYDPSAGVGGFVQDSKSTDSGSSGSSSQGVANSLNESVISGIFASICLGILSFFM
Protein: Rhesus theta defensin-1/2 subunit B (RTD-1 subunit B) (RTD-1b) (Demidefensin-1) (RTD-2) (P82271)
Organism: Macaca mulatta (Rhesus macaque)
Function: RTD-1 and RTD-2 have similar antimicrobial activities against the Gram-positive bacteria S.aureus 502A and L.monocytogenes, the Gram-negative bacterium S.typhimurium, and the fungi C.albicans 16820 and C.neoformans 271A. RTD-2 is 2-3-fold less active than RTD-1 against E.coli ML35.
Interaction partners:
- Defensin, alpha 4, corticostatin
- Neutrophil defensin 1
- Defensin alpha 6
- B-defensin2-like
- Beta/alpha-defensin C-terminal domain-containing protein
- Defensin beta 4A
- Beta-defensin-like domain-containing protein
- Rhesus theta defensin-1/3 subunit A
- Beta/alpha-defensin C-terminal domain-containing protein
- Elastase, neutrophil expressed
Sequence:
MRTFALLTAMLLLVALHAQAEARQARADEAAAQQQPGADDQGMAHSFTRPENAALPLSESARGLRCLCRRGVCQLL