wanglab/gogpt-training-data huggingface dataset:
Protein: FIGNL1-interacting regulator of recombination and mitosis (FIDGETIN-like-1 interacting protein) (FLIP) (POLO1-associating protein) (Q9NSG2)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000269|PubMed:34260926}. Nucleus {ECO:0000269|PubMed:34260926}. Chromosome, centromere {ECO:0000269|PubMed:34260926}. Midbody {ECO:0000269|PubMed:34260926}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:34260926}. Note=Exhibits cell-cycle-dependent distribution during mitosis. Detected in the nucleus in interphase. Colocalizes with PLK1 to the centromeres in a nearby prometaphase cells. Relocates to the central spindle in anaphase and to the midbody in telophase cells. {ECO:0000269|PubMed:34260926}.
Interaction partners:
- PCNA-interacting partner
Sequence:
MFLPHMNHLTLEQTFFSQVLPKTVKLFDDMMYELTSQARGLSSQNLEIQTTLRNILQTMVQLLGALTGCVQHICATQESIILENIQSLPSSVLHIIKSTFVHCKNSESVYSGCLHLVSDLLQALFKEAYSLQKQLMELLDMVCMDPLVDDNDDILNMVIVIHSLLDICSVISSMDHAFHANTWKFIIKQSLKHQSIIKSQLKHKDIITSLCEDILFSFHSCLQLAEQMTQSDAQDNADYRLFQKTLKLCRFFANSLLHYAKEFLPFLSDSCCTLHQLYLQIHSKFPPSLYATRISKAHQEEIAGAFLVTLDPLISQLLTFQPFMQVVLDSKLDLPCELQFPQCLLLVVVMDKLPSQPKEVQTLWCTDSQVSETTTRISLLKAVFYSFEQCSGELSLPVHLQGLKSKGKAEVAVTLYQHVCVHLCTFITSFHPSLFAELDAALLNAVLSANMITSLLAMDAWCFLARYGTAELCAHHVTIVAHLIKSCPGECYQLINLSILLKRLFFFMAPPHQLEFIQKFSPKEAENLPLWQHISFQALPPELREQTVHEVTTVGTAECRKWLSRSRTLGELESLNTVLSALLAVCNSAGEALDTGKQTAIIEVVSQLWAFLNIKQVADQPYVQQTFSLLLPLLGFFIQTLDPKLILQAVTLQTSLLKLELPDYVRLAMLDFVSSLGKLFIPEAIQDRILPNLSCMFALLLADRSWLLEQHTLEAFTQFAEGTNHEEIVPQCLSSEETKNKVVSFLEKTGFVDETEAAKVERVKQEKGIFWEPFANVTVEEAKRSSLQPYAKRARQEFPWEEEYRSALHTIAGALEATESLLQKGPAPAWLSMEMEALQERMDKLKRYIHTLG
Protein: U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2 (CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 2) (Renal carcinoma antigen NY-REN-20) (U2(RNU2) small nuclear RNA auxiliary factor 1-like 2) (U2AF35-related protein) (URP) (Q15696)
Organism: Homo sapiens (Human)
Function: Pre-mRNA-binding protein required for splicing of both U2- and U12-type introns. Selectively interacts with the 3'-splice site of U2- and U12-type pre-mRNAs and promotes different steps in U2 and U12 intron splicing. Recruited to U12 pre-mRNAs in an ATP-dependent manner and is required for assembly of the prespliceosome, a precursor to other spliceosomal complexes. For U2-type introns, it is selectively and specifically required for the second step of splicing.
Subcellular location: Nucleus {ECO:0000269|PubMed:15146077}.
Interaction partners:
- Splicing factor U2AF 65 kDa subunit
- Splicing factor 3B subunit 1
- RNA-binding region-containing protein 3
- PHD finger-like domain-containing protein 5A
- U11/U12 small nuclear ribonucleoprotein 48 kDa protein
- Splicing factor 3B subunit 2
- Small nuclear ribonucleoprotein F
- U11/U12 small nuclear ribonucleoprotein 35 kDa protein
- Splicing factor 3B subunit 6
- Small nuclear ribonucleoprotein E
Sequence:
MAAPEKMTFPEKPSHKKYRAALKKEKRKKRRQELARLRDSGLSQKEEEEDTFIEEQQLEEEKLLERERQRLHEEWLLREQKAQEEFRIKKEKEEAAKKRQEEQERKLKEQWEEQQRKEREEEEQKRQEKKEKEEALQKMLDQAENELENGTTWQNPEPPVDFRVMEKDRANCPFYSKTGACRFGDRCSRKHNFPTSSPTLLIKSMFTTFGMEQCRRDDYDPDASLEYSEEETYQQFLDFYEDVLPEFKNVGKVIQFKVSCNLEPHLRGNVYVQYQSEEECQAALSLFNGRWYAGRQLQCEFCPVTRWKMAICGLFEIQQCPRGKHCNFLHVFRNPNNEFWEANRDIYLSPDRTGSSFGKNSERRERMGHHDDYYSRLRGRRNPSPDHSYKRNGESERKSSRHRGKKSHKRTSKSRERHNSRSRGRNRDRSRDRSRGRGSRSRSRSRSRRSRRSRSQSSSRSRSRGRRRSGNRDRTVQSPKSK
Protein: SET domain binding factor, isoform A (Q9VGH9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- phosphatidylinositol-3,5-bisphosphate 3-phosphatase
- Histone-lysine N-methyltransferase trithorax
- Ras-related protein Rab-21
- histone acetyltransferase
- Cyclin-dependent kinase 9
- LD21953p
- Negative elongation factor B
- RNA polymerase II elongation factor Ell
- Little elongation complex subunit 1
- RNA polymerase II-associated factor 1 homolog
Sequence:
MSRLADYFVIVGYDSDKEKTASNVGGQPTCGKIVQRFPEKDWPDTPFIEGIEWFCQPLGWSLSYEKQEPKFFVSVLTDIDANKHYCACLSFHETVAITQTRSVDDEDETIGSSRLLGATPSSMDGITTTSTPASITHHSVMYAPKCLVLISRLDCAETFKNCLGTIYTVYIENLAYGLETLIGNILGCIQVPPAGGPQVRFSIGAGDKQSLQPPQSSSLPTTGSGVHFLFKQLGIKNVLILLCSVMTENKILFLSKCYWHLTDSCRALVALMYPFRYTHVYIPILPAPLTEVLSTPTPFIMGIHSSLQTEITDLLDVIVVDLDGGLVTIPESLTPPVPILPSPLWEQTQDLLSMILFPNLAQADLAFPTLERPSAIAKTDAQIDKELRAIFMRLFAQLLQGYRSCLTIIRIHPKPVITFHKAGFLGARDLIESEFLFRVLDSMFFTTFVNERGPPWRSSDAWDELYSSMNELLKSEAQNRNLVGRTQRFKGYFNFTFPSYFQILTHIQELGRVLYENEGTLAHISYAQKVLRPPEGAFQRIHQPAFPRISSEKVELIIQEGIRKNGVPQRFHVTRNQHRIIPMGPRLPEALDVRPNVQNSARRLEVLRICVSYIFENRITDARKLLPAVMRTLMHRDARLILCREFFGYVHGNKAVLDHQQFELVVRFMNKALQKSSGIDEYTVAAALLPMSTIFCRKLSTGVVQFAYTEIQDHAIWKNLQFWESTFFQDVQGQIKALYLLHRRQNEHQKEANCVLDEVPLEEPTALEITAEQLRKSPNIEEEKKAELAKSEESTLYSQAIHFANRMVSLLIPLDVNVDAASKPKPAFRLEENQSVSNSIMGSHSLSEHSDEGFEENNALEIGVTVGKTISRFIDCVCTEGGVTSEHIRNLHDMVPGVVHMHIESLEPVYLEAKRHPHVQKPKIQTPCLLPGEDLVTDHLRCFLMPDGREDETQCLIPAEGALFLTNYRVIFKGSPCDPLFCEQVIVRTFPIASLLKEKKISVLYLAHLDQTLTEGLQLRSSSFQLIKVAFDPEVTPEQIESFRKILSKARHPFDEFEYFAFQSYGTMLQGVAPLKTKEKYSTLKGFAKKTLLRGAKKAGFKQKQQTKRKLVSDYDYGSADAQETQSIDDELEDGDEFETQNNAMPRLLTTKDVERMRERSYVQDWKRLGFDAESQRGFRISNANTSYATCRSYPAIIVAPVQCSDAAIMHLGRCFKGQRIPLPTWRHANGALLIRGGQPNSKSVIGMLKNTTGSTTNAHHDVTHYPEQDKYFLALINTMPKLTPLALNQYSGMNLSMSSLMGHSSSDDRQPLTPELSRKHKNNLDISDGNKSSQGGKGGTMKGNPKNSLAHPFRKMRLYALGEKSQAKSNMNVDFCADFIPVDYPDIRQSRPAFKKLIRACMPSHNTNEADGQSFAKMVEQSDWLQQISSLMQLSGAVVDLIDLQESSVMLSLEDGSDVTAQLSSIAQLCLDPYYRSLDGFRVLVEKEWLAFGHRFAHRSNLKPSHANTNIAFAPTFLQFLDVVHQLQRQFPMAFEFNDFYLRFLAYHSVSCRFRTFLFDCELERSDSGIAAMEDKRGSLNAKHMFGAGGMATNGSDDECSVYPLDIRSQRAPAPLNRIGHSIFDYIERQHNKTPIFYNFLYSGDKSVTLRPQNNVAALDLWCYYTNEELAQGAPYDLEVTTVDDEIDLSETKGKRMVITAGYDNMEKCNPSAYVCLLSEVKQAETERGHLPQKWLQVWNSLEVPQLEPVARNTSLGNIFVQTHQHKRSTLEIIMKGRLAGYQDKYFHPHRFEKHPYTTPTNCNHCTKLLWGPVGYRCMDCGNSYHEKCTEHSMKNCTKYKAIDGAVGPPNVNMSQGDTASIASSAATTARTSSHHFYNQFSSNVAENRTHEGHLYKRGALLKGWKQRWFVLDSIKHQLRYYDTSEDTAPKGIIELAEVQSVTAAQPAQIGAKGVDEKGFFDLKTSKRIYNFYAINANLAQEWIEKLQACLQ
Protein: Coatomer subunit zeta (Zeta-coat protein) (Zeta-COP) (P53600)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit beta'
- Coatomer subunit epsilon
- Coatomer subunit alpha
- Coatomer subunit beta
- Coatomer subunit gamma
- Coatomer subunit delta
- ADP-ribosylation factor 1
- ADP-ribosylation factor GTPase-activating protein GLO3
- Ribosome quality control complex subunit 2
- ER lumen protein-retaining receptor
Sequence:
MSSLSLYTVQAVLILDQQGERIYAKYYQPPHRSDEGHQLLFNSVKKQKEFEKQLYRKTHKQDSEILIFEDHLVLYKEYIDITIYLVASLEENEIVLQQGFSAIRGALDLILNSGMDKKNIQENYDMVLLAIDETIDNGVILETDSNTIASRVSKPPTNEPQMALDLDKGFLGAWGFAKSKFQERLQQGL
Protein: LD29807p (Q9VLS8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}.
Interaction partners:
- Dystroglycan 1
Sequence:
MAAMANLHNTRMLRFFLVLIVVILTIFIYASYSTTSTLTANHVHPAASPPQQLIGSHPGRQPMDQVPPVNSTDKEYNSPPGESSSKQQSVSSRHSQQLPPQQAEIHKRHPQHRLPTIDEDALLDGGSAGASPQVGGPDQTPNVMADELLEEQQYGQSVDGITGNINSSTNNNSSADTLAVKQSIPAQSPQQQLPQSQSQVQPGLSDADLLIPTSNLQKFIENADRILKNITSNSSTGNPSDMAQLNAVDGKLEVSGVESEKQEPESKVIQEIKEAKKEAAVPLPKSAKPPVPPVKTTKSKVPSAPVDPSKGVATETLYEPGHVDEEIDAERICPKGGEFIKLLVLISSAMSHDAARMSIRQTWMHYGTRRDVGMAFVLGRGTNETINKALTQENFIYGDLIRGNFIDSYNNLTLKTISTLEWADVHCPKAKYILKTDDDMFINVPKLLTFLDKHKDKRTIYGRLAKKWKPIRNKKSKYYVSVDQFAAGVFPSFTTGPAYVLTGDIVHELYVRSLKTVYLKLEDVFTTGIVAKSLNVKRVQANEFVNRRISFNPCNIRNAISVHMIKSNEQFDLWKKLLDQTTKCK
Protein: Medium-chain acyl-CoA ligase ACSF2, mitochondrial (EC 6.2.1.2) (Q9UAV8)
Organism: Caenorhabditis elegans
Interaction partners:
- Fatty acid synthase
- Nsp1_C domain-containing protein
- Very-long-chain 3-oxooacyl-coA reductase let-767
- Fatty acid synthase
- Hydroxysteroid dehydrogenase-like protein 2
- Acyl-coenzyme A oxidase acox-1.2
- Long chain fatty acid elongase 5
- Serine palmitoyltransferase 1
- Ribosomal protein L13
- Large ribosomal subunit protein uL3m
Sequence:
MSQVAAMDLRVLTQFDIASLEEDRKKMLYEEPISLEEAALNANDVMVAPSRKSYVHGCSTVPLLFETVGDRLRSAVDQVPDKEFLIFKREGIRKTYSQVATDAENLACGLLHLGLKKGDRIGIWGPNTYEWTTTQFASALAGMVLVNINPSYQSEELRYAIEKVGIRALITPPGFKKSNYYQSIKDILPEVTLKEPGKSGITSRNFTCFQHLIMFDEEDKIYPGAWKYTDVMKMGTEEDRHHLSKIERETQPDDSLNIQYTSGTTGQPKGATLTHHNVLNNAFFVGLRAGYSEKKTIICIPNPLYHCFGCVMGVLAALTHLQTCVFPAPSFDALAALQAIHEEKCTALYGTPTMFIDMINHPEYANYNYDSIRSGFIAGAPCPITLCRRLVQDMHMTDMQVCYGTTETSPVSFMSTRDDPPEQRIKSVGHIMDHLEAAIVDKRNCIVPRGVKGEVIVRGYSVMRCYWNSEEQTKKEITQDRWYHTGDIAVMHDNGTISIVGRSKDMIVRGGENIYPTEVEQFLFKHQSVEDVHIVGVPDERFGEVVCAWVRLHESAEGKTTEEDIKAWCKGKIAHFKIPRYILFKKEYEFPLTVTGKVKKFEIREMSKIELGLQQVVSHFSEL
Protein: Putative electron transfer flavoprotein subunit YdiQ (P76201)
Organism: Escherichia coli (strain K12)
Function: May play a role in a redox process.
Interaction partners:
- Putative electron transfer flavoprotein subunit YdiR
- Protein FixB
- Putative electron transfer flavoprotein subunit YgcQ
- Ferredoxin-like protein YdiT
- Probable electron transfer flavoprotein-quinone oxidoreductase YdiS
- Probable acyl-CoA dehydrogenase YdiO
- Crotonobetainyl-CoA reductase
- Ferredoxin-like protein FixX
- Putative oxidoreductase YgfK
- 2,4-dienoyl-CoA reductase [
Sequence:
MKIITCFKLVPEEQDIVVTPEYTLNFDNADAKISQFDLNAIEAASQLATDDDEIAALTVGGSLLQNSKVRKDVLSRGPHSLYLVQDAQLEHALPLDTAKALAAAIEKIGFDLLIFGEGSGDLYAQQVGLLVGEILQLPVINAVSAIQRQGNTLVIERTLEDDVEVIELSVPAVLCVTSDINVPRIPSMKAILGAGKKPVNQWQASDIDWSQSAPLAELVGIRVPPQTERKHIIIDNDSPEAIAELAEHLKKALN
Protein: Malonyl-CoA decarboxylase, mitochondrial (MCD) (EC 4.1.1.9) (Q99J39)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. Plays a role in controlling the extent of ischemic injury by promoting glucose oxidation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O95822}. Mitochondrion matrix {ECO:0000269|PubMed:23746352}. Peroxisome {ECO:0000250|UniProtKB:O95822}. Peroxisome matrix {ECO:0000250|UniProtKB:Q920F5}. Note=Enzymatically active in all three subcellular compartments. {ECO:0000250|UniProtKB:Q920F5}.
Interaction partners:
- Acetyl-CoA carboxylase 1
- Acetyl-CoA carboxylase 2
- Malonate--CoA ligase ACSF3, mitochondrial
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Acetyl-CoA acetyltransferase, mitochondrial
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- 5'-AMP-activated protein kinase subunit gamma-2
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase subunit beta-1
- 5'-AMP-activated protein kinase subunit gamma-3
Sequence:
MRGLGPGLRARRLLPLRSPPRPPGPRGRRLCGGLAASAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAEASQRAELLGRLAQGFGVDHGQVAEQSAGVLQLRQQAREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPHVREMNGVLKSMLSEWFSSGFLNLERVTWHSPCEVLQKISECEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISNNIQGIVKECPPTETEERNRIAAAIFYSISLTQQGLQGVELGTFLIKRVVKELQKEFPQLGAFSSLSPIPGFTKWLLGLLNVQGKEHGRNELFTDSECQEISAVTGNPVHESLKGFLSSGEWVKSEKLTQALQGPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVMWRINWMADSSLKGLTSSCGLMVNYRYYLEETGPNSISYLGSKNIKASEQILSLVAQFQNNSKL
Protein: ANTH domain-containing protein (Q54Y50)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane, clathrin-coated pit {ECO:0000256|ARBA:ARBA00004600}.
Interaction partners:
- Clathrin heavy chain
- AP-2 complex subunit alpha-2
- I/LWEQ domain-containing protein
- AP-2 complex subunit mu
- Clathrin light chain
- Epidermal growth factor receptor substrate 15 homolog
- Epsin
- AP-1 complex subunit gamma
- AP-3 complex subunit delta
- Synaptobrevin-A
Sequence:
MSTPWGKALDQANIVRASFNDLDRSVIKATRHKLRIPKEKHVRKLIIYTHERLGPIGDLYQSLLKRMEQPDWIIVLKTLIVFHRVLAGGNTRFLEDLTHRGNVFPLSRFTDMTSTQAHQQSVFIRRYSSYLEEKVFAFREMRQEFDKDTFSSKGLTIEQLLTRIPKMQRQFDALLATHVEEVCDNIITINAFELLLKDSFKMYCNLNDAVLNILELYFKMTKRDATKALDVYKVFMRETDAIIEFFSSSRRKFHIDLPELSRAPSTVVQGLEEYLRDLEDDGLPPHPVYTNNFGSKTGSNGGRISSQGGSSNSFNNNYNNNNSNNNNNNNSGNDNMVNSTGRNSNSYSNNNNNNKKNDELINFDDDLFSSAPPPQQQQQQQQQQQQQVHQQHSFNKPTTSQPSFELDPFHVTNISQQQQQQSQQQPQQQSMQPFGGFTTSPPPSQQPSLNQVNPSNYHNPFDPAYNEKALQIKAAFQSSQGENGVINNRNSLNLNDFNFTPNTNVNSSNNNNNMKSAPSTLVPTQNRNNNGMMNNNDMMNNNNNGMMMNNNNNSMMMMQQQQHQPMNNGFGMQQQQPMNNGMGFNNSNNNMNNNMMRPNQPMSNGMGMGMQQQPMGFNNGMMNNGMQQPMNNGFGMQQQPMNNGMGFNNSNNNMNNNMMRPNQPMMQPNQYQQQQQQQQQQQQQQQQQKVQNIYF
Protein: Uncharacterized protein (Q389N4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 50S ribosomal protein L17, putative
- Mitochondrial RNA binding complex 1 subunit
- Large ribosomal subunit protein uL3m
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Rhodanese domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Ribosomal protein L11, putative
Sequence:
MGASAGLIRRGGGVFPDAVSLTLTPSRRVYGGSGRGDLLYENPDARRHSGRALGVLNGVRHSSQATMPESGQLYHRKLILHSRPPNGSCAGLQRHCHDTCNWSYLIPSLHRCAESAISAKLWEKMCQLGLEDRSKAWVNLTQYERQRVRDGQNLYRYEVHQRLPLLEESIGWAQLDDLLGWFRSARRAWVRLPTSVTLSRESSEAGVASVVSPSSTMSCRLEGHADSRDTTPGRNQVFDTPERVEQLTEATVHRIREELQRLNRSERSDCEGSAAMRASARRLARDEELNRCVEEELGWHGVALQHRIPVPK
Protein: Sperm-associated antigen 4 protein (Outer dense fiber-associated protein SPAG4) (SUN domain-containing protein 4) (O55034)
Organism: Rattus norvegicus (Rat)
Function: Involved in spermatogenesis. Required for sperm head formation but not required to establish and maintain general polarity of the sperm head. Required for anchoring and organization of the manchette. Required for targeting of SUN3 and probably SYNE1 through a probable SUN1:SYNE3 LINC complex to the nuclear envelope and involved in accurate posterior sperm head localization of the complex. May anchor SUN3 the nuclear envelope. Involved in maintenance of the nuclear envelope integrity (By similarity). May assist the organization and assembly of outer dense fibers (ODFs), a specific structure of the sperm tail.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10373309}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:10373309}. Nucleus envelope {ECO:0000250|UniProtKB:Q9JJF2}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q9JJF2}. Note=In spermatids, it is localized in the transient manchette and in the axoneme of elongating spermatids and epididymal sperm. {ECO:0000269|PubMed:10373309}.
Interaction partners:
- Outer dense fiber protein 1
- Nesprin-3
- KASH domain containing 5
- Nesprin-4
- Sad1 and UNC84 domain containing 5
Sequence:
MRRNPRPGSAASSHNHTPNFYSENSNSSHSATSGDSNGRRSAGPELGEPDGRMARGSSCGEPALSSGVPGGDTWAGSSRPKLAPRSHNGQTACGAATVRGGASEPSGSPAVLEEQLNLLPILDLRQEMPPPPVSKSFLSLFFQVLSVFLSLVADGLVCVYREICSIRFLFTAVSLLSIFLAALWWGLLYLIPPLENEPKEMLTLSQYHHRVHSQGQQLQQLQAELSKLHKEVTSVRAAHSERVAKLVFQRLNEDFVRKPDYALSSVGASIDLEKTSSDYEDRNTAYFWNRLSFWNYARPPSVILEPDVFPGNCWAFEGEQGQVVIRLPGHVQLSDITLQHPPPTVAHTGGASSAPRDFAVFGLQADDDETEVFLGKFIFEVQKSEIQTFHLQNDPPSAFPKVKIQILSNWGHPRFTCLYRVRAHGVRISESAEDNAMGVTGGPH
Protein: Manganese transporter SMF1 (P38925)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: High-affinity manganese transporter involved in manganese uptake from the extracellular environment. Contributes also to cellular accumulation of other divalent metal ions such as cadmium, cobalt, copper, iron and nickel.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11027260}; Multi-pass membrane protein {ECO:0000255}. Note=In presence of excess manganese, targeted to the vacuolar lumen, where it is degraded.
Interaction partners:
- Metal homeostatis protein BSD2
- Protein ECM21
- Low-affinity Fe
- Calcium-transporting ATPase 1
- Iron transport multicopper oxidase FET3
- Protein CCC1
- E3 ubiquitin-protein ligase RSP5
- Plasma membrane iron permease
- Uncharacterized protein TRE1
- Cell division control protein 1
Sequence:
MVNVGPSHAAVAVDASEARKRNISEEVFELRDKKDSTVVIEGEAPVRTFTSSSSNHEREDTYVSKRQVMRDIFAKYLKFIGPGLMVSVAYIDPGNYSTAVDAGASNQFSLLCIILLSNFIAIFLQCLCIKLGSVTGLDLSRACREYLPRWLNWTLYFFAECAVIATDIAEVIGTAIALNILIKVPLPAGVAITVVDVFLIMFTYKPGASSIRFIRIFECFVAVLVVGVCICFAIELAYIPKSTSVKQVFRGFVPSAQMFDHNGIYTAISILGATVMPHSLFLGSALVQPRLLDYDVKHGNYTVSEEQDKVKKSKSTEEIMEEKYFNYRPTNAAIKYCMKYSMVELSITLFTLALFVNCAILVVAGSTLYNSPEADGADLFTIHELLSRNLAPAAGTIFMLALLLSGQSAGVVCTMSGQIVSEGHINWKLQPWQRRLATRCISIIPCLVISICIGREALSKALNASQVVLSIVLPFLVAPLIFFTCKKSIMKTEITVDHTEEDSHNHQNNNDRSAGSVIEQDGSSGMEIENGKDVKIVYMANNWIITVIAIIVWLFLSLLNVYAIVQLGMSHGDIS
Protein: Tensin-4 (C-terminal tensin-like protein) (Q8IZW8)
Organism: Homo sapiens (Human)
Function: Promotes EGF-induced cell migration by displacing tensin TNS3 from the cytoplasmic tail of integrin ITGB1 which results in dissociation of TNS3 from focal adhesions, disassembly of actin stress fibers and initiation of cell migration. Suppresses ligand-induced degradation of EGFR by reducing EGFR ubiquitination in the presence of EGF. Increases MET protein stability by inhibiting MET endocytosis and subsequent lysosomal degradation which leads to increased cell survival, proliferation and migration.
Subcellular location: Cell junction, focal adhesion {ECO:0000269|PubMed:12154022, ECO:0000269|PubMed:17190795, ECO:0000269|PubMed:17643115, ECO:0000269|PubMed:24814316}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12154022}.
Interaction partners:
- Integrin beta-1
- Breast cancer anti-estrogen resistance protein 1
- Proto-oncogene tyrosine-protein kinase Src
- Focal adhesion kinase 1
Sequence:
MSQVMSSPLLAGGHAVSLAPCDEPRRTLHPAPSPSLPPQCSYYTTEGWGAQALMAPVPCMGPPGRLQQAPQVEAKATCFLPSPGEKALGTPEDLDSYIDFSLESLNQMILELDPTFQLLPPGTGGSQAELAQSTMSMRKKEESEALDIKYIEVTSARSRCHDGPQHCSSPSVTPPFGSLRSGGLLLSRDVPRETRSSSESLIFSGNQGRGHQRPLPPSEGLSPRPPNSPSISIPCMGSKASSPHGLGSPLVASPRLEKRLGGLAPQRGSRISVLSASPVSDVSYMFGSSQSLLHSSNSSHQSSSRSLESPANSSSSLHSLGSVSLCTRPSDFQAPRNPTLTMGQPRTPHSPPLAKEHASSCPPSITNSMVDIPIVLINGCPEPGSSPPQRTPGHQNSVQPGAASPSNPCPATRSNSQTLSDAPFTTCPEGPARDMQPTMKFVMDTSKYWFKPNITREQAIELLRKEEPGAFVIRDSSSYRGSFGLALKVQEVPASAQSRPGEDSNDLIRHFLIESSAKGVHLKGADEEPYFGSLSAFVCQHSIMALALPCKLTIPQRELGGADGASDSTDSPASCQKKSAGCHTLYLSSVSVETLTGALAVQKAISTTFERDILPTPTVVHFKVTEQGITLTDVQRKVFFRRHYPLTTLRFCGMDPEQRKWQKYCKPSWIFGFVAKSQTEPQENVCHLFAEYDMVQPASQVIGLVTALLQDAERM
Protein: Kinesin-like protein (A0A0R4IRM1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Kinesin light chain
- Kinesin light chain
- Kinesin light chain 4
- Syntabulin
- Glutamate receptor-interacting protein 2a
Sequence:
MADPAECTIKVMCRFRPLNSAEVMRGDKYIPSFQGEDSVVIGGKPYVFDRVFQSNTTQEQVYNACAQKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGNLHDSDCMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPYVKGCTERFVCSPEEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEATTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSFNEAETKSTLMFGQRAKTIKNTVSVNVELTAEQWKKKYEKEKEKNKTLKNTITWLENELNRWRNGESVPVDEQYDKEKANADVLALDNVVNNDKFTSTPSVPGLKFTDAEREKCEAELAKLFKQLDDKDDEINQQSQLAEKLKQQMLDQEELLASTRRDHDNLQAELTRLQMENEASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEFETLNEELNQKSSVLASIESELQKLKEMTNHQKKRVTEMMSSLLKDLAEIGIAVGSNDIKHEGGGLIDEEFTVARLYISKMKSEVKTLVKRSKQLESAQTESNKKMDENEKELAACQLRISQYEAKIKSLSEYLQNIEQKKRQLEENVDSLNEELVKLSAQEKVHAMEKENEIQSANEVKAAVEQQIQNHREAHQKQLSSLRDELETKEKLITELQDQNQKIILEQERLKVEHEKLKSTDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEMDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAARDRKRYQQEVDRIKEAVRAKNMARRGHSAQIAKPIRPGQPPVASPTHPNVIRSGAGLFQNNQSAGIRGGGGVKQ
Protein: Ras-related protein Rab-1A (EC 3.6.5.2) (YPT1-related protein) (P62820)
Organism: Homo sapiens (Human)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB1A regulates vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment and on to the cell surface, and plays a role in IL-8 and growth hormone secretion. Required to modulate the compacted morphology of the Golgi. Regulates the level of CASR present at the cell membrane. Plays a role in cell adhesion and cell migration, via its role in protein trafficking. Plays a role in autophagosome assembly and cellular defense reactions against pathogenic bacteria. Plays a role in microtubule-dependent protein transport by early endosomes and in anterograde melanosome transport (By similarity).
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:22939626}. Endoplasmic reticulum {ECO:0000269|PubMed:22939626}. Early endosome {ECO:0000269|PubMed:21303926}. Cytoplasm, cytosol {ECO:0000305|PubMed:19942850}. Membrane {ECO:0000269|PubMed:19942850, ECO:0000269|PubMed:23815289}. Melanosome {ECO:0000250|UniProtKB:P62821}. Note=Alternates between membrane-associated and cytosolic forms. {ECO:0000305|PubMed:19942850}.
Interaction partners:
- Rab GDP dissociation inhibitor beta
- Rab GDP dissociation inhibitor alpha
- Ras-related protein Rab-1B
- General vesicular transport factor p115
- Guanine nucleotide exchange factor C9orf72
- Trafficking protein particle complex subunit 4
- Trafficking protein particle complex subunit 1
- Trafficking protein particle complex subunit 8
- Trafficking protein particle complex subunit 5
- Trafficking protein particle complex subunit 3
Sequence:
MSSMNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESFNNVKQWLQEIDRYASENVNKLLVGNKCDLTTKKVVDYTTAKEFADSLGIPFLETSAKNATNVEQSFMTMAAEIKKRMGPGATAGGAEKSNVKIQSTPVKQSGGGCC