wanglab/gogpt-training-data huggingface dataset:
Protein: Coiled-coil domain-containing protein 74A (Q96AQ1)
Organism: Homo sapiens (Human)
Interaction partners:
- Coiled-coil domain-containing protein 74B
Sequence:
MSGAGVAAGTRPPSSPTPGSRRRRQRPSVGVQSLRPQSPQLRQSDPQKRNLDLEKSLQFLQQQHSEMLAKLHEEIEHLKRENKDLHYKLIMNQTSQKKDGPSGNHLSRASAPLGARWVCINGVWVEPGGPSPARLKEGSSRTHRPGGKRGRLAGGSADTVRSPADSLSMSSFQSVKSISNSGKARPQPGSFNKQDSKADVSQKADLEEEPLLHNSKLDKVPGVQGQARKEKAEASNAGAACMGNSQHQGRQMGAGAHPPMILPLPLRKPTTLRQCEVLIRELWNTNLLQTQELRHLKSLLEGSQRPQAAPEEASFPRDQEATHFPKVSTKSLSKKCLSPPVAERAILPALKQTPKNNFAERQKRLQAMQKRRLHRSVL
Protein: Porphobilinogen deaminase (PBG-D) (EC 2.5.1.61) (Hydroxymethylbilane synthase) (HMBS) (Pre-uroporphyrinogen synthase) (P19356)
Organism: Rattus norvegicus (Rat)
Function: As part of the heme biosynthetic pathway, catalyzes the sequential polymerization of four molecules of porphobilinogen to form hydroxymethylbilane, also known as preuroporphyrinogen. Catalysis begins with the assembly of the dipyrromethane cofactor by the apoenzyme from two molecules of porphobilinogen or from preuroporphyrinogen. The covalently linked cofactor acts as a primer, around which the tetrapyrrole product is assembled. In the last step of catalysis, the product, preuroporphyrinogen, is released, leaving the cofactor bound to the holodeaminase intact.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P22907}.
Interaction partners:
- Delta-aminolevulinic acid dehydratase
- Uroporphyrinogen-III synthase
- Uroporphyrinogen decarboxylase
- Ferrochelatase
- Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
- Amine oxidase
- Endonuclease V
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- 5-aminolevulinate synthase, non-specific, mitochondrial
- Hypoxanthine-guanine phosphoribosyltransferase
Sequence:
MSGNGGAATTAEENGSMMRVIRVGTRKSQLARIQTDTVVAMLKTLYPGIQFEIIAMSTTGDKILDTALSKIGEKSLFTKELENALEKNEVDLVVHSLKDVPTILPPGFTIGAICKRENPCDAVVFHPKFIGKTLETLPEKSAVGTSSLRRVAQLQRKFPHLEFKSIRGNLNTRLRKLDEQLEFSAIILAVAGLQRMGWQNRVGQILHPEECMYAVGQGALAVEVRAKDQDILDLVGVLHDPETLLRCIAERAFLRHLEGGCSVPVAVHTVMKDGQLYLTGGVWSLDGSDSMQETMQATIQVPVQQEDGPEDDPQLVGITARNIPRGAQLAAENLGISLASLLLNKGAKNILDVARQLNDVR
Protein: Tryptophan 2,3-dioxygenase (TDO) (EC 1.13.11.11) (Tryptamin 2,3-dioxygenase) (Tryptophan oxygenase) (TO) (TRPO) (Tryptophan pyrrolase) (Tryptophanase) (P21643)
Organism: Rattus norvegicus (Rat)
Function: Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.
Interaction partners:
- Kynureninase
- Indoleamine 2,3-dioxygenase 2
- Indoleamine 2,3-dioxygenase 1
- Kynurenine formamidase
- Tryptophan 5-hydroxylase 1
- Acetylserotonin O-methyltransferase-like
- Kynurenine 3-monooxygenase
- Tryptophan 5-hydroxylase 2
- Aromatic-L-amino-acid decarboxylase
- Amine oxidase
Sequence:
MSGCPFSGNSVGYTLKNLSMEDNEEDGAQTGVNRASKGGLIYGDYLQLEKILNAQELQSEIKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNGHVRDERNMLKVMTRMHRVVVIFKLLVQQFSVLETMTALDFNDFREYLSPASGFQSLQFRLLENKIGVLQSLRVPYNRKHYRDNFEGDYNELLLKSEQEQTLLQLVEAWLERTPGLEPHGFNFWGKFEKNILKGLEEEFLKIQAKKDSEEKEEQMAEFRKQKEVLLCLFDEKRHDYLLSKGERRLSYRALQGALMIYFYREEPRFQVPFQLLTSLMDIDTLMTKWRYNHVCMVHRMLGSKAGTGGSSGYYYLRSTVSDRYKVFVDLFNLSSYLVPRHWIPKMNPIIHKFLYTAEYSDSSYFSSDESD
Protein: Protein ROH1A (Protein ROH1) (Q9CAK4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for seed coat mucilage deposition.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9CA69}.
Interaction partners:
- Exocyst complex component EXO70A1
- Dentin sialophosphoprotein
- Exocyst complex component EXO70C2
- Exocyst complex component EXO70C1
- Probable protein kinase At2g41970
- GPI-anchored protein
- Probable LRR receptor-like serine/threonine-protein kinase At4g31250
- Exocyst complex component SEC8
- Plant intracellular Ras-group-related LRR protein 2
- Serine/threonine-protein kinase RHS3
Sequence:
MRPAQDNQGSFLGRISIRRNQFVDVNNEQEQEDLELFQKHIADRFTELLSPPQPPPSDEINTVASVAATEQIMSVTWLRKLMDVFLCCEAEFKAILLMGRDPTQISKPPFDRLVPEMLDRSIKALDICTAVVNGIDSVRHYQRLAEIAVTALEQRPLGDGNVRRAKRALANLVVALSLEDKENVSGGGGGGGGGNKTTERSWSFGRRSGGSSAASKGGATIGQLKSSSWAVGRNWSAAKQIHAMTANLTPPRGNEAAGLPQPMFIMSTVMVFVMWVLTAAVPCQERSGLANHLPVPPKHLNWAQSLIGIHEKIGDEWKKKEKKGSAGLMEEMTRMEKLGHSLMEFADGFHYPAEKDAAESAAVQVAEMAEICRRMEEELVPLQQQIREVFHRIVRSRAEILEVLEQAGKVSAPVV
Protein: Gamma-crystallin D (Gamma-D-crystallin) (Gamma-crystallin 1) (P04342)
Organism: Mus musculus (Mouse)
Function: Crystallins are the dominant structural components of the vertebrate eye lens.
Interaction partners:
- Alpha-crystallin A chain
- Gamma-crystallin C
- Gamma-crystallin E
- Gap junction alpha-8 protein
- Lens fiber major intrinsic protein
- Phakinin
- Alpha-crystallin B chain
- Gap junction alpha-3 protein
- Filensin
- Heat shock factor protein 4
Sequence:
MGKITFYEDRGFQGRHYECSTDHSNLQPYFSRCNSVRVDSGCWMLYEQPNFTGCQYFLRRGDYPDYQQWMGFSDSVRSCRLIPHAGSHRIRLYEREEYRGQMIEFTEDCPSLQDRFHFNEIYSLNVLEGCWVLYDMTNYRGRQYLLRPGEYRRYHDWGAMNARVGSLRRVMDFY
Protein: TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L (TAF6L) (PCAF-associated factor 65-alpha) (PAF65-alpha) (Q9Y6J9)
Organism: Homo sapiens (Human)
Function: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex (Probable). With TAF5L, acts as an epigenetic regulator essential for somatic reprogramming. Regulates target genes through H3K9ac deposition and MYC recruitment which trigger MYC regulatory network to orchestrate gene expression programs to control embryonic stem cell state. Functions with MYC to activate target gene expression through RNA polymerase II pause release (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:11564863, ECO:0000269|PubMed:9674425}.
Interaction partners:
- Transcription initiation factor TFIID subunit 9
- Transformation/transcription domain-associated protein
- Transcriptional adapter 3
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 12
- STAGA complex 65 subunit gamma
- TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L
- Transcription initiation protein SPT3 homolog
- Transcriptional adapter 1
- Transcription factor SPT20 homolog
Sequence:
MSEREERRFVEIPRESVRLMAESTGLELSDEVAALLAEDVCYRLREATQNSSQFMKHTKRRKLTVEDFNRALRWSSVEAVCGYGSQEALPMRPAREGELYFPEDREVNLVELALATNIPKGCAETAVRVHVSYLDGKGNLAPQGSVPSAVSSLTDDLLKYYHQVTRAVLGDDPQLMKVALQDLQTNSKIGALLPYFVYVVSGVKSVSHDLEQLHRLLQVARSLFRNPHLCLGPYVRCLVGSVLYCVLEPLAASINPLNDHWTLRDGAALLLSHIFWTHGDLVSGLYQHILLSLQKILADPVRPLCCHYGAVVGLHALGWKAVERVLYPHLSTYWTNLQAVLDDYSVSNAQVKADGHKVYGAILVAVERLLKMKAQAAEPNRGGPGGRGCRRLDDLPWDSLLFQESSSGGGAEPSFGSGLPLPPGGAGPEDPSLSVTLADIYRELYAFFGDSLATRFGTGQPAPTAPRPPGDKKEPAAAPDSVRKMPQLTASAIVSPHGDESPRGSGGGGPASASGPAASESRPLPRVHRARGAPRQQGPGTGTRDVFQKSRFAPRGAPHFRFIIAGRQAGRRCRGRLFQTAFPAPYGPSPASRYVQKLPMIGRTSRPARRWALSDYSLYLPL
Protein: Gamma-secretase-activating protein (GSAP) (Protein pigeon homolog) [Cleaved into: Gamma-secretase-activating protein 16 kDa C-terminal form (GSAP-16K)] (A4D1B5)
Organism: Homo sapiens (Human)
Function: Regulator of gamma-secretase activity, which specifically activates the production of amyloid-beta protein (amyloid-beta protein 40 and amyloid-beta protein 42), without affecting the cleavage of other gamma-secretase targets such has Notch. The gamma-secretase complex is an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Specifically promotes the gamma-cleavage of APP CTF-alpha (also named APP-CTF) by the gamma-secretase complex to generate amyloid-beta, while it reduces the epsilon-cleavage of APP CTF-alpha, leading to a low production of AICD.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:20811458}.
Interaction partners:
- Amyloid-beta precursor protein
- Presenilin-1
- Gamma-secretase subunit PEN-2
- Nicastrin
- Gamma-secretase subunit APH-1A
Sequence:
MALRLVADFDLGKDVLPWLRAQRAVSEASGAGSGGADVLENDYESLHVLNVERNGNIIYTYKDDKGNVVFGLYDCQTRQNELLYTFEKDLQVFSCSVNSERTLLAASLVQSTKEGKRNELQPGSKCLTLLVEIHPVNNVKVLKAVDSYIWVQFLYPHIESHPLPENHLLLISEEKYIEQFRIHVAQEDGNRVVIKNSGHLPRDRIAEDFVWAQWDMSEQRLYYIDLKKSRSILKCIQFYADESYNLMFEVPLDISLSNSGFKLVNFGCDYHQYRDKFSKHLTLCVFTNHTGSLCVCYSPKCASWGQITYSVFYIHKGHSKTFTTSLENVGSHMTKGITFLNLDYYVAVYLPGHFFHLLNVQHPDLICHNLFLTGNNEMIDMLPHCPLQSLSGSLVLDCCSGKLYRALLSQSSLLQLLQNTCLDCEKMAALHCALYCGQGAQFLEAQIIQWISENVSACHSFDLIQEFIIASSYWSVYSETSNMDKLLPHSSVLTWNTEIPGITLVTEDIALPLMKVLSFKGYWEKLNSNLEYVKYAKPHFHYNNSVVRREWHNLISEEKTGKRRSAAYVRNILDNAVKVISNLEARNLGPRLTPLLQEEDSHQRLLMGLMVSELKDHFLRHLQGVEKKKIEQMVLDYISKLLDLICHIVETNWRKHNLHSWVLHFNSRGSAAEFAVFHIMTRILEATNSLFLPLPPGFHTLHTILGVQCLPLHNLLHCIDSGVLLLTETAVIRLMKDLDNTEKNEKLKFSIIVRLPPLIGQKICRLWDHPMSSNIISRNHVTRLLQNYKKQPRNSMINKSSFSVEFLPLNYFIEILTDIESSNQALYPFEGHDNVDAEFVEEAALKHTAMLLGL
Protein: Major capsid protein (Gene product 8) (gp8) (Major head protein) (Protein p8) (P13849)
Organism: Bacillus phage phi29 (Bacteriophage phi-29)
Function: Assembles to form a prolate capsid shell of about 54 nm in length and 45 nm in width, with a T=3, Q=5 symmetry.
Subcellular location: Virion {ECO:0000269|PubMed:11562162, ECO:0000269|PubMed:9814712}. Note=Present in about 235 copies in the virion. {ECO:0000269|PubMed:11562162, ECO:0000269|PubMed:9814712}.
Interaction partners:
Sequence:
MRITFNDVKTSLGITESYDIVNAIRNSQGDNFKSYVPLATANNVAEVGAGILINQTVQNDFITSLVDRIGLVVIRQVSLNNPLKKFKKGQIPLGRTIEEIYTDITKEKQYDAEEAEQKVFEREMPNVKTLFHERNRQGFYHQTIQDDSLKTAFVSWGNFESFVSSIINAIYNSAEVDEYEYMKLLVDNYYSKGLFTTVKIDEPTSSTGALTEFVKKMRATARKLTLPQGSRDWNSMAVRTRSYMEDLHLIIDADLEAELDVDVLAKAFNMNRTDFLGNVTVIDGFASTGLEAVLVDKDWFMVYDNLHKMETVRNPRGLYWNYYYHVWQTLSVSRFANAVAFVSGDVPAVTQVIVSPNIAAVKQGGQQQFTAYVRATNAKDHKVVWSVEGGSTGTAITGDGLLSVSGNEDNQLTVKATVDIGTEDKPKLVVGEAVVSIRPNNASGGAQA
Protein: Putative helicase; 55525-51977 (RAD3-like DNA-binding helicase protein) (Q9CA92)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Chromosome transmission fidelity protein 18 homolog
- Pentatricopeptide repeat-containing protein At4g30825
- General transcription and DNA repair factor IIH subunit TFB4
- General transcription factor IIH subunit 2
- General transcription and DNA repair factor IIH subunit TFB2
- Cyclin-H1-1
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Large ribosomal subunit protein uL15x
- Transcription initiation factor IIF subunit alpha
- Protein CHROMOSOME TRANSMISSION FIDELITY 7
Sequence:
MTEIREFPAFPYKPYSIQIDFMNALYQFLDKGGVSMLESPTGTGKSLSIICSALQWLTDRKEKRNSGLTEESHKVDGNDDEDEPDWMRNFTLNEADGANGDKSIKNTKSPFSLRKHAKEVFTEGEKADELNDQEFLLDEYESQDESSPGGGNSKRKPARGFDSSSSEDEEDENDCSDDEQGGFKVFFCSRTHSQLSQFVKELRKTVFAKKLKVVCLGSRKNLCINEDVLKLGNVTRINERCLDLQKKKISQVSKKKNLGANVRIVRTKASCRCPMLRKHKLQREFKAESFQQEAMDIEDLVQLGREMRTCPYYGSRRMAPAADLVILPYQSLLSKSSRESLGLSLKNSVVIIDEAHNLADTLLSMHDAKLTVSQLEDIHCSIESYLGRFQNLLGAGNRRYIQIMLILTRAFLKPLASDRNLSSVNVGLDTENPSKSKPCGACSMAIYDFLFSLNIDNINLVKLLAYIKESNIIHKVSGYGERVAAMLQKDPVAHEEMSKLTSFRAFSDMLVALTNNNGDGRIIISRTSSSTSGQHGGYIKYVMLTGAKLFSEVVDEAHAVILAGGTLQPIEETRERLFPWLPSNQLQFFSCSHIVPPESIMPIAVSHGPSGQSFDFSHSSRSSIGMIQELGLLMSNLVAVVPEGIIVFFSSFEYETQVHTAWSNSGILRRIVKKKRVFREPRKNTEVEAVLRDYKEAIESERGAIMLAVVGGKVSEGINFSDSMCRCVVMVGLPYPSPSDIELLERIKHIEGRADSDSIKPSVTLVDDSYYSGDVQAGFGVLKSCKRRGKEYYENLCMKAVNQSIGRAIRHEKDYASILLVDARYSNDPSKRTSHSHPSNKLPKWIKDRLIYSTKGYGDVHRLLHQFFKHKNVENSSETNQH
Protein: Ubiquitin carboxyl-terminal hydrolase isozyme L3 (UCH-L3) (EC 3.4.19.12) (Ubiquitin thioesterase L3) (Q9JKB1)
Organism: Mus musculus (Mouse)
Function: Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3'', and exhibits a preference towards 'Lys-48'-linked ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. Required for stress-response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11341770, ECO:0000269|PubMed:17967898}.
Interaction partners:
- Ubiquitin-like protein NEDD8
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-B
- Polyubiquitin-C
- 26S proteasome non-ATPase regulatory subunit 14
- Sentrin-specific protease 8
- NEDD8-activating enzyme E1 catalytic subunit
- Ubiquitin carboxyl-terminal hydrolase 14
- Ubiquitin carboxyl-terminal hydrolase 5
- NEDD8-activating enzyme E1 regulatory subunit
Sequence:
MEGQRWLPLEANPEVTNQFLKQLGLHPNWQFVDVYGMEPELLSMVPRPVCAVLLLFPITEKYEVFRTEEEEKIKSQGQDVTSSVYFMKQTISNACGTIGLIHAIANNKDKMHFESGSTLKKFLEESVSMSPEERAKFLENYDAIRVTHETSAHEGQTEAPSIDEKVDLHFIALVHVDGHLYELDGRKPFPINHGKTSDETLLEDAIEVCKKFMERDPDELRFNAIALSAA
Protein: Serpentine receptor class alpha-6 (Protein sra-6) (Q09208)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Serpentine receptor class r-10
Sequence:
MSNLSCAAPDVLERLDSFNMKLSQFVDLLAIILAFFASYFAIKIVINQSFFELSTKILLLQNLFYTNLYQISYGIEAIGMLYRGFFMLSEPCSILQSETSCAPYFKVLMIGTSGMIFGQTGLLIERAFATFATTYKTKKSVYIGVCISLIVLVCSTSSGFIILWDDPLEGWTIGCFAVSKSVVPRFNLFSILSTVLTLFNLIVSIFIQRYNKRFEFETRFKVGARFQKQELIESTGAICFLALSQFLWMFMYSFGILILRIIREDILPSTFYFWIAWCYTMPFIALMFPVLLIYRIRKTRARRTEKMKGITTEKQTQDDHIKQINAMWT
Protein: Malate dehydrogenase, cytoplasmic (EC 1.1.1.96) (Aromatic alpha-keto acid reductase) (Cytosolic malate dehydrogenase) (C9JLV6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQSEPIRVLVTGAAGQIAYSLLYSIGNGSVFGKDQPIILVLLDITPMMGVLDGVLMELQDCALPLLKDVIATDKEDVAFKDLDVAILVGSMPRREGMERKDLLKANVKIFKSQG
Protein: Interleukin-36 gamma (Interleukin-1 family member 9) (IL-1F9) (Q8R460)
Organism: Mus musculus (Mouse)
Function: Functions as an agonist of NF-kappa B activation through the orphan IL-1-receptor-related protein 2/IL1RL2. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP (By similarity). Seems to be involved in skin inflammatory response by acting on keratinocytes, dendritic cells and indirectly on T-cells to drive tissue infiltration, cell maturation and cell proliferation. May play a role in pro-inflammatory responses during particular neutrophilic airway inflammation. May be involved in the innate immune response to fungal pathogens. Induces the production of pro-inflammatory cytokines in bone marrow-derived dendritic cells (BMDCs), including IL-12, Il-1 beta, IL-6, TNF-alpha and IL-23. Involved in dendritic cell maturation by stimulating the surface expression of CD80, CD86 and MHC class II. Induces the production of IFN-gamma, IL-4 and IL-17 by cultured CD4(+) T-cells and splenocytes.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9NZH8}. Secreted {ECO:0000250|UniProtKB:Q9NZH8}. Note=The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. {ECO:0000250|UniProtKB:Q9NZH8}.
Interaction partners:
- Interleukin-1 receptor-like 2
- Interleukin-36 receptor antagonist protein
- Interleukin-1 receptor antagonist protein
- Interleukin-1 receptor accessory protein
Sequence:
MFSKHPFSTHISGRETPDFGEVFDLDQQVWIFRNQALVTVPRSHRVTPVSVTILPCKYPESLEQDKGIAIYLGIQNPDKCLFCKEVNGHPTLLLKEEKILDLYHHPEPMKPFLFYHTRTGGTSTFESVAFPGHYIASSKTGNPIFLTSKKGEYYNINFNLDIKS
Protein: Katanin p80 WD40 repeat-containing subunit B1 (Katanin p80 subunit B1) (p80 katanin) (A0A0G2JX20)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03022}. Note=Predominantly cytoplasmic. Localized to the interphase centrosome and mitotic spindle poles. Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis. {ECO:0000256|HAMAP-Rule:MF_03022}.
Interaction partners:
Sequence:
MATPVVTKTAWKLQEIVAHASNVSSLVLGKASGRLLATGGDDCRVNLWSINKPNCIMSLTGHTSPVESVRLNTPEELIVAGSQSGSIRVWDLEAAKILRTLMGHKANICSLDFHPYGEFVASGSQDTNIKLWDIRRKGCVFRYRGHSQAVRCLRFSPDGKWLASAADDHTVKLWDLTAGKMMSEFPGHTGPVNVVEFHPNEYLLASGSSDRTIRFWDLEKFQVVSCIEGEPGPVRSVLFNPDGCCLYSGCQDSLRVYGWEPERCFDVVLVNWGKVADLAICNDQLIGVAFSQSNVSSYVVDLTRVTRTGTVTQDPVQASQPQTQQTPNPGVSLRRIYERPSTTCSKPQRVKHNSESERRSPSSEDDKDERESRAEIQNAEDYNEIFQPKNSISRTPPRRSEPFPAPPEDDIATAKEASKPSPAMDVQLPVPSQEVPARPSVMTSTPAPKGEPVIIPATRNEPIGLKASDFLPAVKVPQQAELVDEDAMSQIRKGHDTMCVVLTSRHKNLDTVRAVWTTGDIKTSVDSAVAINDLSVVVDLLNIVNQKACLSSSLWKLDLCTTVLPQIEKLLQSKYESYVQTGCTSLKLILQRFLPLITDILAAPPSVGVDISREERLHKCRLCFKQLKSISGLVKSRSGLSGRHGSAFRELHLLMASLD
Protein: Smoothelin (P53814)
Organism: Homo sapiens (Human)
Function: Structural protein of the cytoskeleton.
Subcellular location: Cytoplasm, cytoskeleton. Note=Exhibits a filamentous organization.
Interaction partners:
- Myosin-11
- Calponin-1
- Transgelin
- Protein HIRA
- Smoothelin-like protein 1
- Myocardin
Sequence:
MADEALAGLDEGALRKLLEVTADLAERRRIRSAIRELQRQELEREEEALASKRFRAERQDNKENWLHSQQREAEQRAALARLAGQLESMNDVEELTALLRSAGEYEERKLIRAAIRRVRAQEIEAATLAGRLYSGRPNSGSREDSKGLAAHRLEQCEVPEREEQEQQAEVSKPTPTPEGTSQDVTTVTLLLRAPPGSTSSSPASPSSSPTPASPEPPLEPAEAQCLTAEVPGSPEPPPSPPKTTSPEPQESPTLPSTEGQVVNKLLSGPKETPAAQSPTRGPSDTKRADVAGPRPCQRSLSVLSPRQPAQNRESTPLASGPSSFQRAGSVRDRVHKFTSDSPMAARLQDGTPQAALSPLTPARLLGPSLTSTTPASSSSGSSSRGPSDTSSRFSKEQRGVAQPLAQLRSCPQEEGPRGRGLAARPLENRAGGPVARSEEPGAPLPVAVGTAEPGGSMKTTFTIEIKDGRGQASTGRVLLPTGNQRAELTLGLRAPPTLLSTSSGGKSTITRVNSPGTLARLGSVTHVTSFSHAPPSSRGGCSIKMEAEPAEPLAAAVEAANGAEQTRVNKAPEGRSPLSAEELMTIEDEGVLDKMLDQSTDFEERKLIRAALRELRQRKRDQRDKERERRLQEARGRPGEGRGNTATETTTRHSQRAADGSAVSTVTKTERLVHSNDGTRTARTTTVESSFVRRSENGSGSTMMQTKTFSSSSSSKKMGSIFDREDQASPRAGSLAALEKRQAEKKKELMKAQSLPKTSASQARKAMIEKLEKEGAAGSPGGPRAAVQRSTSFGVPNANSIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPEAFDYGQLSPQNRRQNFEVAFSSAEMLVDCVPLVEVDDMMIMGKKPDPKCVFTYVQSLYNHLRRHELRLRGKNV
Protein: WHIM2 domain-containing protein (Q38B59)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSQKEENSVNGDETNTTLPRAVLKTRTASQLYKEGGSVGTMASFNSLPQVEQLLFKVQAAEMTLLAALDVAERSPEDKKIFGHATLTMAENYLSEIISIIPHCSRSTDAPHLSINSSAIQRLIALYGASDDVVKFVAHLSTSQPRVAELSPRDVTTVVYNISEVARLFKQSMKESGEQCGVFTKSTTSLQPSPMKESESAVADEGTVPPAPTAGRKRGRPSRNKSSDTPAEPGAEGSPEHGTFTGEGGAAAKDKRKKSEETSSRKPKSNEGTPSGPRKISYCRLRALTTAEKRVTTSLNQIVQLLGHLYAHQYNDLLPVFGFLEARVKQLQETIDVERAAFAKKDIATRSPEPFIGVSVQSIIAAIRSSLHTYSTEEWCRQEFDEDLLHPVAHACMTEVNRIEGFATEPFVGITAEALAAKIATRKAARIKLEEKWEKERERAREKEEAQVKYNEERRWLRARFGDIDKASLVEDTSIDNPAVSAPVYYSDLPLQDVELYERALFVWTMLVSVPQALRLSQMPFNIFLKSVTTGVGGTDTLIEEIVKSLLEVLVENLRAGNGSRINIKGKYWFDAMVEFVAVTSGNRRKRDNKQKKDIKEEEEEEEEEEEEGEETEDETVEEQEEDEEEAQEKIEGSTDTEKTGNDREPQNSEDLKQDVEEEKSKEENEGENLANMIRGTMENVAELRNMATWFNINLPDRLNLLYYLVLEALHTPVVQGEAEKMRKRYEEQQLLVGKCIKEVCEEACKEFKGLARKLAVSKSEDEEQSVEEKRKEILQECSNRLKSTVEEQIGVQDGKDVGTIIRPIGMDRYKRVYWRLPFDRHITVQSTQATNLDFPALRGVTYLAERTSHSFAGNLLDDDDCETGVQVGSTESASAQGSANDQIPQKVWGTVPLTCLGTFIEGLDRRGVREGELRRNLEILQPYLASMSEITGGRITRFRSQTFGYQNKLRLEL
Protein: Cyclin-dependent kinase 4 inhibitor D (p19-INK4d) (Q60773)
Organism: Mus musculus (Mouse)
Function: Interacts strongly with CDK4 and CDK6 and inhibits them.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Cyclin-dependent kinase 4
- Cyclin-dependent kinase 6
- G1/S-specific cyclin-D3
- G1/S-specific cyclin-D1
- G1/S-specific cyclin-D2
- Cyclin-dependent kinase 2
- Cyclin-dependent kinase inhibitor 1C
- Cyclin-dependent kinase inhibitor 1B
- Cyclin-dependent kinase inhibitor 1
Sequence:
MLLEEVCVGDRLSGAAARGDVQEVRRLLHRELVHPDALNRFGKTALQVMMFGSPAVALELLKQGASPNVQDASGTSPVHDAARTGFLDTLKVLVEHGADVNALDSTGSLPIHLAIREGHSSVVSFLAPESDLHHRDASGLTPLELARQRGAQNLMDILQGHMMIPM
Protein: DNA polymerase delta interacting protein 3 (F6VRR5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MADISLDELIRKRGAAAKGRLNARPGVGGVRSRVGIQQGLLSQSTRTATFQQRFDARQKIGLSDARLKLGVKDAREKLLQKDARFRIKGKVQDAREMLNSRKQQTTVPQKPRQVADAREKISLKRSSPAAFINPPIGTVTPALKLTKTIQRMHVDPVGWILTTECFQVPQQKAMAPLHPHPAGMRINVVNNHQAKQNLYDLDEDDDGIASVPTKQMKFAASGGFLHHMAGLSSSKLSMSKALPLTKVVQNDAYTAPALPSSIRTKALTNMSRTLVNKEEPPKELPAAEPVLSPLEGTKMTVNNLHPRVTEEDIVELFCVCGALKRARLVHPGVAEVVFVKKDDAITAYKKYNNRCLDGQPMKCNLHMNGNVITSDQPILLRLSDSPSMKKESELPRRVNSASSSNPPAEVDPDTILKALFKSSGASVTTQPTEFKIKL
Protein: Probable 26S proteasome regulatory subunit rpn9 (Q9US13)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Interaction partners:
- 26S proteasome regulatory subunit 4 homolog
- 26S proteasome regulatory subunit rpn502
- 26S proteasome regulatory subunit rpn7
- 26S proteasome regulatory subunit rpn12
- Probable 26S proteasome regulatory subunit rpn6
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome regulatory subunit rpn10
- Probable 26S proteasome regulatory subunit rpn3
- 26S proteasome regulatory subunit rpn1
- 26S proteasome regulatory subunit rpn2
Sequence:
MDTEMSVNMSDFLHDQATRAPESLQQSYILMEDLYERKLWKQLTDALIVFFDTPETVPLRLPLYTNFVNSFRPNINQLKAVYMGLKAFESCSNDEALRNLNQIVNELDEEKYKDAYVYSIVAIARIKLISGKLDEARELLVKASKIIDHIDYVESLIHSSYYSVSADYYKAKADYAQYYRHCLLYLSCIDLDKCSHTELVERAVDLSVAAILGDIYNFGELLLHPVFELLVGTQHEWLHDLVIAMNVGDLPLFERLMGQINKMPLLQSSVALLGQKIRLMALIELVFQLPPNQRTLTFDTIARATRIPSNEVELLIMRALSVGLITGVIDEVTQIVTISSVQSRILNHSQIASMESRLREWNQNIKNLSNVVEISGKGVFV
Protein: tRNA:m(4)X modification enzyme TRM13 (EC 2.1.1.225) (tRNA methylase 13) (Q12383)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- tRNA
- tRNA
- tRNA
- tRNA
- tRNA
Sequence:
MLQDNNGPAVKRAKPSERLQCEYFMEKKKRRCGMTRSSQNLYCSEHLNLMKKAANSQVHNKNGSEAEKERERVPCPLDPNHTVWADQLKKHLKKCNKTKLSHLNDDKPYYEPGYNGENGLLSSSVKIDITAEHLVQSIELLYKVFEGESMDELPLRQLNNKLMSLKRFPQLPSNTKHAVQQSSLIENLVDAGAFERPESLNFIEFGCGRAEFSRYVSLYLLTQLTSLPAEHSGSNSNEFVLIDRATNRMKFDKKIKDDFSEIKSNSPSKPISCPSIKRIKIDIRDLKMDPILKSTPGDDIQYVCISKHLCGVATDLTLRCIGNSSILHGDDNNGCNPKLKAICIAMCCRHVCDYGDYVNRSYVTSLVEKYRAHGSILTYETFFRVLTKLCSWGTCGRKPGTAITDIVNVVESFEGAEPYTITIKERENIGLMARRVIDEGRLVYVKEKFTEFNAELIRYVESDVSLENVAMLVYKK
Protein: Protein lyl-1 (Class A basic helix-loop-helix protein 18) (bHLHa18) (Lymphoblastic leukemia-derived sequence 1) (P12980)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Rhombotin-2
- Transcription factor E2-alpha
- LIM domain-binding protein 1
- LIM domain-binding protein 2
- Core-binding factor subunit beta
- Runt-related transcription factor 1
- Endothelial transcription factor GATA-2
- Rhombotin-1
- Histone acetyltransferase p300
- T-cell leukemia homeobox protein 3
Sequence:
MCPPQAQAEVGPTMTEKAEMVCAPSPAPAPPPKPASPGPPQVEEVGHRGGSSPPRLPPGVPVISLGHSRPPGVAMPTTELGTLRPPLLQLSTLGTAPPTLALHYHPHPFLNSVYIGPAGPFSIFPSSRLKRRPSHCELDLAEGHQPQKVARRVFTNSRERWRQQNVNGAFAELRKLLPTHPPDRKLSKNEVLRLAMKYIGFLVRLLRDQAAALAAGPTPPGPRKRPVHRVPDDGARRGSGRRAEAAARSQPAPPADPDGSPGGAARPIKMEQTALSPEVR