wanglab/gogpt-training-data huggingface dataset:
Protein: Proteasome regulatory ATPase subunit 1 (EC 3.6.4.8) (D6XKG7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Proteasome subunit alpha type
- Proteasome regulatory non-ATP-ase subunit
- Proteasome subunit beta
- Proteasome regulatory non-ATP-ase subunit 5
- 26S proteasome regulatory subunit 4 homolog
- 26S proteasome regulatory non-ATPase subunit
- Proteasome subunit alpha type
- Probable 26S proteasome regulatory subunit rpn-6.2
- Proteasome subunit alpha type
- Proteasome subunit beta
Sequence:
MASEKGGCQTKNTVRIKGENEEEKEIIPLDQDDIALLKLYGSGPYHATVKELEEFVKTKAEAVNKLAGTRDNELGLAPPVQWDLNSDQEVMRSENSLHVARCTRIINKGQDDAKYVVAIRDTAKYVVKLGNRVARQDIEESMRVGVLVGYSSIHIEIPLPPRVDPSVSMMQVEEKPDVTYNDVGGAKEQIDRIREVVELPLTNPEKYTQLGIDPPKGVLLYGPPGTGKTLLAKAVANRTDATFIRVIGSELVQRYIGEGARMIREIFQLARTKKAAIIFFDEVDAVGGARGGGDGDDEIQRTMLEMVNQMDGFDSRGNIKVIMATNRPDTLDPALTRPGRMDRKLEVGLPDLEGRTKILRIHAKSLSCEKAIRFELIARLCPNATGADLRSVCTEAGMFAIRARRKTINEKDFLDAVNKVIKGHHKFSATAKYMVYN
Protein: Hexokinase-4 (EC 2.7.1.1) (Q56XE8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Fructose and glucose phosphorylating enzyme (By similarity). May be involved in the phosphorylation of glucose during the export from mitochondrion to cytosol (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:14671022}; Single-pass membrane protein {ECO:0000269|PubMed:14671022}.
Interaction partners:
- Glucose-6-phosphate isomerase, cytosolic
- Glucose-6-phosphate isomerase 1, chloroplastic
- Probable phosphoglucomutase, cytoplasmic 1
- Phosphoglucomutase, chloroplastic
- Probable phosphoglucomutase, cytoplasmic 2
- Phosphomannomutase
- Mannose-6-phosphate isomerase 2
- Fructose-1,6-bisphosphatase, cytosolic
- Mannose-6-phosphate isomerase 1
- Fructose-1,6-bisphosphatase 1, chloroplastic
Sequence:
MGKVLVMLTAAAAVVACSVATVMVRRRMKGRRKWRRVVGLLKDLEEACETPLGRLRQMVDAIAVEMQAGLVSEGGSKLKMLLTFVDDLPNGSETGTYYALHLGGSYFRIIKVHLGGQRSSLEVQDVERHSIPTSLMNSTSEVLFDFLASSLQRFIEKEGNDFSLSQPLKRELAFTFSFPVKQTSISSGVLIKWTKGFAISEMAGEDIAECLQGALNKRGLDIRVAALVNDTVGALSFGHFHDPDTIAAVVFGTGSNACYLERTDAIIKCQNPRTTSGSMVVNMEWGNFWSSRLPRTSYDLELDAESMNSNDMGFEKMIGGMYLGDIVRRVILRMSQESDIFGPISSILSTPFVLRTNSVSAMHEDDTSELQEVARILKDLGVSEVPMKVRKLVVKICDVVTRRAARLAAAGIAGILKKVGRDGSGGGRRSDKQIMRRTVVAVEGGLYLNYRMFREYMDEALRDILGEDVAQHVVVKAMEDGSSIGSALLLASSQSVQTIPSV
Protein: GDP-mannose-dependent alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase (EC 2.4.1.346) (Alpha-D-mannose-alpha-(1-6)-phosphatidylmyo-inositol-mannosyltransferase) (Alpha-mannosyltransferase) (Alpha-ManT) (Guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase) (Phosphatidylinositol alpha-mannosyltransferase) (PI alpha-mannosyltransferase) (P9WMZ3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM). Catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 6 of a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1) to generate phosphatidyl-myo-inositol bearing alpha-1,2- and alpha-1,6-linked mannose residues (Ac1PIM2). PimB also catalyzes the addition of a mannosyl residue from GDP-Man to the position 6 of phosphatidyl-myo-inositol bearing an acylated alpha-1,2-linked mannose residue (Ac1PIM1) to generate monoacylated phosphatidyl-myo-inositol bearing alpha-1,2- and alpha-1,6-linked mannose residues (Ac1PIM2) (By similarity). The addition of the second mannosyl residue by PimB preferentially occurs before the acylation of the mannosyl residue transferred by PimA (By similarity). Also able to transfer a mannosyl residue from GDP-Man to the position 6 of a phosphatidyl-myo-inositol (PI), but this reaction is very slow (By similarity).
Interaction partners:
- Phosphatidylinositol mannoside acyltransferase
- Phosphatidyl-myo-inositol mannosyltransferase
- Polyprenol-phosphate-mannose-dependent alpha-
- 1,4-alpha-glucan branching enzyme GlgB
- Malto-oligosyltrehalose trehalohydrolase
- DUF4157 domain-containing protein
- Alpha-
- Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase
- Putative glycosyltransferases
- Probable endopeptidase Rv2190c
Sequence:
MSRVLLVTNDFPPRRGGIQSYLGEFVGRLVGSRAHAMTVYAPQWKGADAFDDAARAAGYRVVRHPSTVMLPGPTVDVRMRRLIAEHDIETVWFGAAAPLALLAPRARLAGASRVLASTHGHEVGWSMLPVARSVLRRIGDGTDVVTFVSSYTRSRFASAFGPAASLEYLPPGVDTDRFRPDPAARAELRKRYRLGERPTVVCLSRLVPRKGQDTLVTALPSIRRRVDGAALVIVGGGPYLETLRKLAHDCGVADHVTFTGGVATDELPAHHALADVFAMPCRTRGAGMDVEGLGIVFLEASAAGVPVIAGNSGGAPETVQHNKTGLVVDGRSVDRVADAVAELLIDRDRAVAMGAAGREWVTAQWRWDTLAAKLADFLRGDDAAR
Protein: Phospholipid-transporting ATPase 6 (AtALA6) (EC 7.6.2.1) (Aminophospholipid flippase 6) (Q9SLK6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in transport of phospholipids and in regulation of pollen plasma membrane lipid asymmetry.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25954280}; Multi-pass membrane protein {ECO:0000255}. Endomembrane system {ECO:0000269|PubMed:25954280}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ALA-interacting subunit 3
- ALA-interacting subunit 1
- ALA-interacting subunit 5
- Defensin-like protein 90
- At1g52870/F14G24_14 family protein)
- At3g13062
- Protein DETOXIFICATION 29
- Adenine phosphoribosyltransferase 4
- non-specific serine/threonine protein kinase
- Inactive RHOMBOID-like protein 8
Sequence:
MARRRIRSRIRKSHFYTFRCLRPKTLDDQGPHVINGPGYTRIVHCNQPHLHLATKLIRYRSNYVSTTRYNLLTFLPKCLYEQFHRVANFYFLVAAILSVFPLSPFNKWSMIAPLVFVVGLSMGKEALEDWRRFMQDVEVNSRKASVHKGSGDFGRRTWKRIRVGDIVRVEKDEFFPADLLLLSSSYEDGICYVETMNLDGETNLKVKRCLDATLALEKDESFQNFSGTIKCEDPNPNLYTFVGNLECDGQVYPLDPNQILLRDSKLRNTAYVYGVVVFTGHDTKVMQNSTKSPSKRSRIEKRMDYIIYTLFALLLTVSFISSLGFAVMTKLLMAEWWYLRPDKPESLTNPTNPLYAWVVHLITALLLYGYLIPISLYVSIEVVKVLQAHFINQDLQLYDSESGTPAQARTSNLNEELGQVDTILSDKTGTLTCNQMDFLKCSIAGTSYGVRASEVELAAAKQMAMDLEEKGEEVANLSMNKGRTQRYAKLASKTSSDFELETVVTASDEKDQKQNTGVKGFSFEDNRLMNENWLNEPNSDDILMFFRILAVCHTAIPEVDEDTGMCTYEAESPDEVAFLVASREFGFEFTKRTQSSVFIAERFSSSGQPVDREYKILNLLDFTSKRKRMSAIVRDEEGQILLLCKGADSIIFERLSKSGKEYLGATSKHLNVYGEAGLRTLALGYRKLDETEYAAWNSEFHKAKTSVGADRDEMLEKVSDMMEKELILVGATAVEDKLQKGVPQCIDNLAQAGLKIWVLTGDKMETAINIGYACSLLRQGMKQISISLTNVEESSQNSEAAAKESILMQITNASQMIKIEKDPHAAFALIIDGKTLTYALKDDVKYQFLALAVDCASVICCRVSPKQKALVTRLAKEGTGKTTLAIGDGANDVGMIQEADIGVGISGVEGMQAVMASDFSIAQFRFLERLLVVHGHWCYKRIAQMICYFFYKNITFGLTLFYFECFTGFSGQSIYNDSYLLLFNVVLTSLPVISLGVFEQDVPSDVCLQFPALYQQGPKNLFFDWYRILGWMGNGVYASIVIFTLNLGIFHVQSFRSDGQTADMNAMGTAMFTCIIWAVNVQIALTMSHFTWIQHVMIWGSIGAWYVFLALYGMLPVKLSGNIFHMLVEILAPAPIFWLTSLLVIAATTLPYLFHISYQRSVNPLDHHIIQEIKHFRIDVEDERMWKREKSKAREKTKIGFTARVDAKIRQLRGRLQRKHSVLSVMSGTSSNDTPSSNSQ
Protein: EF-hand domain-containing family member C2 (Q9D485)
Organism: Mus musculus (Mouse)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A0A3Q1N1R0}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:37295417, ECO:0000269|PubMed:37865089, ECO:0000269|PubMed:37989994}.
Interaction partners:
- WD repeat-containing protein 90
- Parkin coregulated gene protein homolog
- Tektin-1
- Piercer of microtubule wall 1 protein
- Tektin-2
- Cilia- and flagella-associated protein 161
- Calaxin
- EF-hand domain-containing protein 1
- Tektin-4
- EF-hand domain-containing family member B
Sequence:
MALPFLPGNSFNRNIGKERFHKSQHWGFCNNVRMLVSENKPGVGGDLLYGQKIKPKHSVFPKGDGTDAPSWVAFDKQVLSFDAYLEDEISDKRQEIFRIRYYKIYFYLEDDTIQVNEPEVINSGLPQGTSIRRQRIPYPPPNDDQFYTVYDFNINISVVFYGRTFKIYDCDPFTKNFLKKIGIKLNPPGQCPLDPYMKMRRETLEFVDPFRPYQSFDTLKRFIQYDGKVLRFFCLWDDSTSLFGDRREFVLHYFLCDGTVEIREVLPSNSGRDAMSSFLRRGKLPKYGPPGIYQPGQITDRAVLNVYGGLSEWRADGYLLDKYQLGKVEQDFYTDQDLSIGATINVWGRKVLLCDCDEFTKTYYRTKYGVDNFTPISCKPPHLPKIERKYPPYTGFGSEEDSFRSCVGLKPTPHRKNFKKFMELDSFGNISNILRYFGKLITHKCADVDRIFVIAFYLSDDTISVFEPIENNSGNAGGMFLKRSRVKKPGQEVFKSEFSEYIKAEELYIGATVNINGYLFILLNADEYTLNYMENNTDKFPYSNFELAIQKLKQEKSKSREITQVFAAADYNHTKVVPYNTFRDILMSITMGKLIDQELITIARHYRVPEIMDPDLAYLIARAHEKFKKNIFENFDMFIYNCVYEDREKKGVLPTKDIRRMCKSSRLPLDDDFLDCLLSRFEDKDHQINYEIFFSVLNWRMNPTPDLQAPPYLKEKCEDVWVGMPSPIPVKYVRYLDFLIDVYGLEDNML
Protein: LHFPL tetraspan subfamily member 5 protein (LHFPL tetraspan subfamily member 5a) (F1Q837)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAKMLSAQEAAKIYHTNYVRNARAVGVLWTIFTICFAIIGMVVFIQPYWIGDSVDTPQSGYFGLFHYCIGNPITGELVCKGSALDFGSIPSGAFKTAMFFVGISLLLIVGTIVCFSLFFFCNSGSVYKICAWMQLAAATCMVIGCMIYPDGWDSEEVKRMCGQRTDKYTLGNCTVRWAYILAIISIMDSLTLSFLAFVLGNRQDKLLPEDFQEEKKEEA
Protein: Kit ligand (Mast cell growth factor) (Stem cell factor) (c-Kit ligand) (Q56JH5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Cell projection, filopodium {ECO:0000256|ARBA:ARBA00004486}. Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MFHMREVKIGESICVLVLLFSGLVTCSGVFGSPLTDDVATLDTLSENIPSDYRIPIKFITKDVGGACWLHLNLYPVESSLKKLAVKFGNQSTNKANITIFITMLQDFRFTLNSDDLEDRMQAFKCHYRREKWPTRRFFSYVKSVLTVAGSTYGDIPPCTPPPCQTLAAPPFTPGQSRQQNGMNSAVHGLLALLIIPSVAILVLTIQMALGRRGRCGARMREIEPHDRAEENRNELHSGAAQEDPASTSASEQDRAWLDSLGCADTEV
Protein: Anaphase-promoting complex subunit 5 (Cyclosome subunit 5) (Q8H1U4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex controls several key steps in the cell cycle by mediating ubiquitination and subsequent degradation of target proteins such as cyclins. The APC/C complex is required for the female gametophyte development and is involved in several aspect of development by controlling cell division and cell elongation. Involved in the control of endoreduplication (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 6
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 7
- Cell division cycle protein 27 homolog A
- Cell division cycle protein 27 homolog B
Sequence:
MAGLTRTAGAFAVTPHKISVCILLQIYAPSAQMSLPFPFSSVAQHNRLGLYLLSLTKSCDDIFEPKLEKLINQLREVGEEMDAWLTDHLTNRFSSLASPDDLLNFFNDMRGILGSLDSGVVQDDQIILDPNSNLGMFVRRCILAFNLLSFEGVCHLFSSIEDYCKEAHSSFAQFGAPNNNLESLIQYDQMDMENYAMDKPTEEIEFQKTASGIVPFHLHTPDSLMKATEGLLHNRKETSRTSKKDTEATPVARASTSTLEESLVDESLFLRTNLQIQGFLMEQADAIEIHGSSSSFSSSSIESFLDQLQKLAPELHRVHFLRYLNKLHSDDYFAALDNLLRYFDYSAGTEGFDLVPPSTGCSMYGRYEIGLLCLGMMHFRFGHPNLALEVLTEAVRVSQQLSNDTCLAYTLAAMSNLLSEMGIASTSGVLGSSYSPVTSTASSLSVQQRVYILLKESLRRADSLKLRRLVASNHLAMAKFELMHVQRPLLSFGPKASMRHKTCPVSVCKEIRLGAHLISDFSSESSTMTIDGSLSSAWLKDLQKPWGPPVISPDSGSRKSSTFFQLCDHLVSIPGSVSQLIGASYLLRATSWELYGSAPMARMNTLVYATLFGDSSSSSDAELAYLKLIQHLALYKGYKDAFAALKVAEEKFLTVSKSKVLLLKLQLLHERALHCGNLKLAQRICNELGGLASTAMGVDMELKVEASLREARTLLAAKQYSQAANVAHSLFCTCHKFNLQIEKASVLLLLAEIHKKSGNAVLGLPYALASISFCQSFNLDLLKASATLTLAELWLGLGSNHTKRALDLLHGAFPMILGHGGLELRARAYIFEANCYLSDPSSSVSTDSDTVLDSLRQASDELQALEYHELAAEASYLMAMVYDKLGRLDEREEAASLFKKHIIALENPQDVEQNMA
Protein: Tubulin-specific chaperone E (Tubulin-folding cofactor E) (A1Z6J5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Tubulin-folding protein which is required for the development of the neuronal microtubule network. Essential for the development and function of neuromuscular synapses. Likely to promote microtubule formation by acting in the negative regulation of the microtubule-severing protein spas.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19297412}.
Interaction partners:
- Tubulin-specific chaperone D
- LD34582p
- ADP-ribosylation factor-like protein 2
- Tubulin-binding cofactor B
- Tubulin-specific chaperone A
- Tubulin beta chain
Sequence:
MVGIIDEVQLFYPLGTRIKIGDNYGTVRYVGEVSGHMGSWLGIEWDDGLRGKHNGIVDGKRYFQTQTPTGGSFIRPGKVGPCATLEDAARERYLNYDSSNVDESLIREAQASLQASLFEVVGMDKIARKQSKFEQLEEVSVDQTPVNAAGYLKELTHLTTLNVSHTLIWNWEIVASIAQQLPSLTNLNLSSNRLVLPTSSQITELEPSFRQLKRINLRSCGFSDWKDVMHTALLWPNILSLGLQENSLGQLAEVDRTKIFKQLHELDLHRTNIMDFDQVTKLGNLTTLRLLNIMENGIEEIKLPDCDSQEKLNIFVSLEQLNLLHNPIWNEADAFNELDKLPQLKRLSKTPHLKSNFDEMFSKAVASIASLQFINKAEVTAEQRRGAEYDIWKKYALDWMQATQGGTDSLREFCRRHRTYPLLVKKYGSPADFVPRSQAKQSNLINVSIRHQLTGETWEKKVPRMITVQTLQGLVMKRFRLSGDVPQLCYVDALHPDLVVPLDNNAKTLDFYSVQEHDTVLVQ
Protein: Binding partner of ACD11 1 (Q9LFD5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18845362}. Membrane {ECO:0000269|PubMed:18845362}.
Interaction partners:
- Accelerated cell death 11
- PRA1 family protein F3
- Pentatricopeptide repeat-containing protein At5g16860
- PRA1 family protein F2
- RING-H2 finger protein ATL72
- Senescence/dehydration-associated protein At3g51250
- THO complex subunit 4C
- Senescence/dehydration-associated protein At4g35985
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH7
Sequence:
MASQVRSVKVGNLSSGATEHDIKEFFSFSGEVESIDIQSNEHSAYVTFKETQGAETAVLLSGASIADQSVIIELAPNYSPPAAPHAETQSSGAESVVQKAEDVVSSMLAKGFILGKDAVGKAKAFDEKHGFTSTATAGVASLDQKIGLSQKLTAGTSLVNEKIKAVDQNFQVTERTKSVYAAAEQTVSSAGSAVMKNRYVLTGVSWAAGAFNRVAQAAGEVGQKTKEKVEAEQPSQPAQSQQQLPEGYSPIHSSEYSKN
Protein: E3 ubiquitin-protein ligase TRIM58 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM58) (Tripartite motif-containing protein 58) (Q5NCC9)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin ligase induced during late erythropoiesis. Directly binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. May participate in the erythroblast enucleation process through regulation of nuclear polarization.
Interaction partners:
Sequence:
MATAPGERLQEEARCSVCLDFLQEPISVDCGHSFCLRCISEFCEKSDSAQGVYACPQCRGPFRPASFRPNRQLASLVDSVRQLGLGTGHAGSRQCARHGEDLSHFCEEDQTMLCWVCDTSPEHRSHRTETLQEAASRYQRMLRASLELVKKEMEEALTQEANVGKKTIIWKEKVEMQRQRFRLEFEKHRGFLAQEEQLQLRRLEEEERATLQRLRDSRNRLAQQNKALKELAEELEERSQRPAPGLLEGARGVLTRCEAITRLEPEAVPMDLKTVCRIPGMREMLRKFQVDVKLDPATAHPSLLLTADLRSVQDAEVWRDVPSNPERFDTWPCILGLQGFSSGRHYWEVIVGERAEWGLGVCRDSVLRKGETTPSPENGVWAMWLLRGNEYMVLSSPSVPVLQDERPRRIGIFLDYEAGEISFYNVTNGSYIYTFNHLFSGVLRPYFFVCDTTPLILPPMTEAAPGNWTPRGIFDLAAAARNEEY
Protein: Snake venom metalloproteinase acutolysin-A (SVMP) (EC 3.4.24.-) (Hemorrhagin I) (HI) (Q9PW35)
Organism: Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus)
Function: This protein is a zinc metalloprotease from snake venom that possesses hemorrhagic activity.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MIQVLLVTICLAAFPYQGSSIILESGNVNDYEVVYPRKVTALPKGAVQQKYEDAMQYEFKVNGEPVVLHLEKNKGLFSKDYSEIHYSPDGRRITTHPLVEDHCYYRGHIRNDADSTASISACNGLKGHFKLQGEMYLIEPMKMSYSEAHAVYKYGNVEKEDEAPKMCGVTQNWESYEPIKKASQLIVSTEFQRYMEIVIVVDHSMVKKYNGDSDKIKAWVYEMINTITESYSYLYIDIILSGLEIWSEKDLINVETSAENTLKSFGEWRAKDLIHRISHDNAQLLTATDFDGPTIGLAYVASMCDPKRSVGVVQDHSSVNRLVAITLAHEMAHNLGVRHDEGSCSCGSGYTCIMSPVINSEVIKYFSDCSYIQCREYISKENPPCILNKPLRTDTVSTPVSGNELLEAGKDYD
Protein: CTD small phosphatase-like protein (CTDSP-like) (EC 3.1.3.16) (Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 3) (NIF-like protein) (Nuclear LIM interactor-interacting factor 1) (NLI-interacting factor 1) (Small C-terminal domain phosphatase 3) (SCP3) (Small CTD phosphatase 3) (P58465)
Organism: Mus musculus (Mouse)
Function: Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MDGPAIITQVTNPKEDEARSPVAGEKASQRNISLKKQRGRSILSSFFCCFRDYNVEAPPANSPSVLPPLVEENGGLQKGDQRQVIPVPSPPAKYLLPEVTVLDYGKKCVVIDLDETLVHSSFKPISNADFIVPVEIDGTIHQVYVLKRPHVDEFLQRMGQLFECVLFTASLAKYADPVADLLDRWGVFRARLFRESCVFHRGNYVKDLSRLGRELSKVIIVDNSPASYIFHPENAVPVQSWFDDMTDTELLDLIPFFEGLSREDDVYSMLHRLCSR
Protein: Intraflagellar transport complex B protein 46 C terminal (Q583M4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}.
Interaction partners:
- Intraflagellar transport protein 57/55
- C2H2-type domain-containing protein
- Intraflagellar transport protein A1
- Intraflagellar transport protein component, putative
- Intraflagellar transport protein 56 homolog
- Uncharacterized protein
- Intraflagellar transport protein IFT88, putative
- IFT80/172/WDR35 TPR domain-containing protein
- Intraflagellar transport protein 80
- Intraflagellar transport protein 27 homolog
Sequence:
MPRGSSKSKKEVSEEPKTTGGSGGDATETSPPTPKAKKGKGGDKMLVNEPNDEKHTVEDARTVQTPSDHETSAARKKPPPKDVKDEKKSEPAHGGGRLLKNNPNDEVVPVEGMHNVATPRSGLITTESDGAKGTMLRNAPHDEAIPVSGHAITMDTPKRTIDVHPGTITNTDDDDDPKSTEEEESVPIGRTRGYCNPRPEAINLEAEVPETTAPNLGYKPQEYAMVNANASREVQELFKRILDYQPQTPELPAKLRPFIPDYVPSIGDLDPFCKIPRPDGKPDGLGIYVLDEPSVAQSNPAVVLLELRATNIHSVGGLAEAVDSFEDAANRPEVIDRWINDVKKVHYKKPLPTINYQKPMPEIDLLLQVWPQEFEEFLNSDVQFPPPQIDLDLDQYVRALCCILDIPTYTSLIDSLHVMFTLYQEFRANQHFQHE
Protein: Peroniin-1.4 (P86494)
Organism: Litoria peronii (Emerald spotted tree frog) (Hyla peronii)
Function: Induces contraction of intestinal smooth muscle in isolated guinea pig ileum.
Subcellular location: Secreted {ECO:0000269|PubMed:19642086}.
Interaction partners:
Sequence:
QTWLPFV
Protein: Large ribosomal subunit protein bL31c (50S ribosomal protein L31, chloroplastic) (CL31) (Protein EMBRYO DEFECTIVE 2184) (Q9FWS4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds the 23S rRNA.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Large ribosomal subunit protein bL21c
- Large ribosomal subunit protein bL28c
- 50S ribosomal protein L33
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
- Large ribosomal subunit protein bL27c
- Small ribosomal subunit protein uS9c
- Large ribosomal subunit protein bL21m
- 50S ribosomal protein L20
- Large ribosomal subunit protein bL20c
Sequence:
MAVSLPNSFLQISPCVPSLQLRKPVMAAVKGGKQSVRRSSNTVVQITCRKKELHPEFHEDAKVYCNGELVMTTGGTKKEYVVDVWSGNHPFYLGNRSALMVDADQVEKFRKRFAGLSEIMEIPVLKGEIIMPTKKSKGPKGKKK
Protein: Synaptosomal-associated protein 47 (SNAP-47) (Epididymis luminal protein 170) (Synaptosomal-associated 47 kDa protein) (Q5SQN1)
Organism: Homo sapiens (Human)
Function: Plays a role in intracellular membrane fusion.
Subcellular location: Endomembrane system {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Appears to be exclusively membrane-bound. {ECO:0000250}.
Interaction partners:
- Syntaxin-3
- Syntaxin-12
- Syntaxin-7
- Vesicle-associated membrane protein 2
- Vesicle-associated membrane protein 4
- Syntaxin-18
- Vesicle-trafficking protein SEC22b
- Syntaxin-1A
- Synaptosomal-associated protein 29
- Syntaxin-4
Sequence:
MRAARRGLHCAGAERPRRRGRLWDSSGVPQRQKRPGPWRTQTQEQMSRDVCIHTWPCTYYLEPKRRWVTGQLSLTSLSLRFMTDSTGEILVSFPLSSIVEIKKEASHFIFSSITILEKGHAKHWFSSLRPSRNVVFSIIEHFWRELLLSQPGAVADASVPRTRGEELTGLMAGSQKRLEDTARVLHHQGQQLDSVMRGLDKMESDLEVADRLLTELESPAWWPFSSKLWKTPPETKPREDVSMTSCEPFGKEGILIKIPAVISHRTESHVKPGRLTVLVSGLEIHDSSSLLMHRFEREDVDDIKVHSPYEISIRQRFIGKPDMAYRLISAKMPEVIPILEVQFSKKMELLEDALVLRSARTSSPAEKSCSVWHAASGLMGRTLHREPPAGDQEGTALHLQTSLPALSEADTQELTQILRRMKGLALEAESELERQDEALDGVAAAVDRATLTIDKHNRRMKRLT
Protein: Cytoplasmic polyadenylation element-binding protein 2 (CPE-BP2) (CPE-binding protein 2) (hCPEB-2) (Q7Z5Q1)
Organism: Homo sapiens (Human)
Function: May play a role in translational regulation of stored mRNAs in transcriptionally inactive haploid spermatids. Binds to poly(U) RNA oligomers (By similarity). Required for cell cycle progression, specifically for the transition from metaphase to anaphase.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q812E0}.
Interaction partners:
- Fragile X messenger ribonucleoprotein 1
- Cyclin-dependent kinase 1
- Aurora kinase A
- Serine/threonine-protein kinase PLK1
- G2/mitotic-specific cyclin-B2
- Elongation factor 2
- Cytoplasmic polyadenylation element-binding protein 4
- RNA-binding protein FXR1
- Eukaryotic translation initiation factor 4E
- Probable ATP-dependent RNA helicase DDX6
Sequence:
MPPPSPDSENGFYPGLPSSMNPAFFPSFSPVSPHGCTGLSVPTSGGGGGGFGGPFSATAVPPPPPPAMNIPQQQPPPPAAPQQPQSRRSPVSPQLQQQHQAAAAAFLQQRNSYNHHQPLLKQSPWSNHQSSGWGTGSMSWGAMHGRDHRRTGNMGIPGTMNQISPLKKPFSGNVIAPPKFTRSTPSLTPKSWIEDNVFRTDNNSNTLLPLQVRSSLQLPAWGSDSLQDSWCTAAGTSRIDQDRSRMYDSLNMHSLENSLIDIMRAEHDPLKGRLSYPHPGTDNLLMLNGRSSLFPIDDGLLDDGHSDQVGVLNSPTCYSAHQNGERIERFSRKVFVGGLPPDIDEDEITASFRRFGPLVVDWPHKAESKSYFPPKGYAFLLFQEESSVQALIDACIEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGDIDKRVEVKPYVLDDQMCDECQGARCGGKFAPFFCANVTCLQYYCEFCWANIHSRAGREFHKPLVKEGADRPRQIHFRWN
Protein: Defensin alpha 4 (Neutrophil antibiotic peptide NP-4) (RatNP-4) (Neutrophil defensin 4) (Q62714)
Organism: Rattus norvegicus (Rat)
Function: Host-defense peptide that has antimicrobial activity against Gram-positive and Gram-negative bacteria and fungi (in vitro). Exhibits activity against E.coli, A.calcoaceticus, S,aureus and C.albicans.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q01523}.
Interaction partners:
Sequence:
MRTLTLLITLLLLALHTQAESPQERAKAAPDQDMVMEDQDIFISFGGYKGTVLQDAVVKAGQACYCRIGACVSGERLTGACGLNGRIYRLCCR
Protein: Trafficking protein particle complex subunit 3 homolog (P34605)
Organism: Caenorhabditis elegans
Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi (By similarity). Required for the systemic spread of the RNAi response.
Subcellular location: Golgi apparatus, cis-Golgi network {ECO:0000250|UniProtKB:Q04183}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9CQP2}.
Interaction partners:
- Trafficking protein particle complex subunit 5
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit 2-like protein
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit 6B
- Trafficking protein particle complex subunit 8
- Trafficking protein particle complex subunit 9
- Trafficking protein particle complex subunit 10
- Probable trafficking protein particle complex subunit 2
- Trafficking protein particle complex subunit 11 domain-containing protein
Sequence:
MSKAIKQNLADSKKMSAELFCLTYGAMVTEMLKDYEDPKDVTIQLDKMGFNMGTRLADDFLAKNANVPRCVDTRQIADVLCRNAIPCYLGISATASSWTSGDREFTITLEANPLTELVQVPAHLVSAGLSYSQLIAGAIRGALEAVHFKVYASATDTGANTEIRIRFDQVLKDSLPAGEDD