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Q9UPN3

- MACF1_HUMAN

UniProt

Q9UPN3 - MACF1_HUMAN

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Protein

Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5

Gene
MACF1, ABP620, ACF7, KIAA0465, KIAA1251
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Isoform 2 is a F-actin-binding protein which may play a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane. Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics. May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4. Plays a key role in wound healing and epidermal cell migration. Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate MT dynamics and polarize hair follicle stem cells By similarity.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi7054 – 7065121 Reviewed predictionAdd
BLAST
Calcium bindingi7090 – 7101122 Reviewed predictionAdd
BLAST

GO - Molecular functioni

  1. actin binding Source: UniProtKB
  2. actin filament binding Source: UniProtKB
  3. ATPase activity Source: UniProtKB
  4. calcium ion binding Source: InterPro
  5. poly(A) RNA binding Source: UniProtKB
  6. protein binding Source: UniProtKB

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. cell cycle arrest Source: InterPro
  3. cellular component movement Source: Ensembl
  4. establishment or maintenance of cell polarity Source: Ensembl
  5. Golgi to plasma membrane protein transport Source: UniProtKB
  6. mesoderm formation Source: Ensembl
  7. positive regulation of Wnt signaling pathway Source: UniProtKB
  8. posttranslational protein targeting to membrane Source: Ensembl
  9. regulation of epithelial cell migration Source: UniProtKB
  10. regulation of focal adhesion assembly Source: UniProtKB
  11. regulation of microtubule-based process Source: UniProtKB
  12. Wnt signaling pathway Source: UniProtKB-KW
  13. wound healing Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

SignaLinkiQ9UPN3.

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5
Alternative name(s):
620 kDa actin-binding protein
Short name:
ABP620
Actin cross-linking family protein 7
Macrophin-1
Trabeculin-alpha
Gene namesi
Name:MACF1
Synonyms:ABP620, ACF7, KIAA0465, KIAA1251
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:13664. MACF1.

Subcellular locationi

Isoform 2 : Cytoplasmcytoskeleton. Cytoplasm. Golgi apparatus. Cell membrane. Cell projectionruffle membrane
Note: The phosphorylated form is found in the cytoplasm while the non-phosphorylated form associates with the microtubules By similarity. Localizes to the tips of microtubules. APC controls its localization to the cell membrane which is critical for its function in microtubule stabilization.3 Publications
Isoform 1 : Cytoplasm. Golgi apparatus
Note: Localizes to the tips of microtubules.3 Publications

GO - Cellular componenti

  1. actin cytoskeleton Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. cytoskeleton Source: UniProtKB
  4. Golgi apparatus Source: UniProtKB
  5. microtubule Source: UniProtKB
  6. plasma membrane Source: UniProtKB
  7. ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30518.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 73887388Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5PRO_0000073449Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei280 – 2801Phosphoserine2 Publications
Modified residuei1376 – 13761Phosphoserine4 Publications
Modified residuei3122 – 31221Phosphoserine By similarity
Modified residuei3927 – 39271Phosphoserine3 Publications
Modified residuei4495 – 44951Phosphoserine1 Publication
Modified residuei4496 – 44961Phosphoserine2 Publications
Modified residuei4521 – 45211Phosphoserine4 Publications
Modified residuei4962 – 49621Phosphoserine1 Publication
Modified residuei6210 – 62101N6-acetyllysine1 Publication
Modified residuei6967 – 69671Phosphoserine1 Publication
Modified residuei7254 – 72541Phosphothreonine1 Publication
Modified residuei7292 – 72921Phosphoserine1 Publication
Modified residuei7330 – 73301Phosphoserine2 Publications
Modified residuei7333 – 73331Phosphoserine By similarity

Post-translational modificationi

Phosphorylated on serine residues in the C-terminal tail by GSK3B. Phosphorylation inhibits microtubule-binding and this plays a critical role in bulge stem cell migration and skin wound repair. Wnt-signaling can repress phosphorylation By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UPN3.
PaxDbiQ9UPN3.
PRIDEiQ9UPN3.

PTM databases

PhosphoSiteiQ9UPN3.

Expressioni

Tissue specificityi

Isoform 2 is ubiquitously expressed. Isoform 1 is expressed in cell lines NCI-H460, A-549 and HaCaT. Isoform 4 is expressed in heart, lung, pituitary and placenta, not found in brain, kidney, liver, pancreas or skeletal muscle.2 Publications

Gene expression databases

ArrayExpressiQ9UPN3.
BgeeiQ9UPN3.
CleanExiHS_MACF1.
GenevestigatoriQ9UPN3.

Organism-specific databases

HPAiHPA013713.

Interactioni

Subunit structurei

Isoform 2 interacts with MAPRE1, CLASP1, CLASP2, AXIN1 and LRP6 By similarity. Isoform 2 is found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B By similarity. Isoform 2 interacts with GOLGA4.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DISC1Q9NRI55EBI-522925,EBI-529989

Protein-protein interaction databases

BioGridi117048. 36 interactions.
DIPiDIP-50616N.
IntActiQ9UPN3. 26 interactions.
MINTiMINT-1195815.
STRINGi9606.ENSP00000289893.

Structurei

3D structure databases

ProteinModelPortaliQ9UPN3.
SMRiQ9UPN3. Positions 69-298.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 295295Actin-bindingAdd
BLAST
Domaini78 – 181104CH 1Add
BLAST
Repeati148 – 17124LRR 1Add
BLAST
Domaini194 – 295102CH 2Add
BLAST
Repeati240 – 26425LRR 2Add
BLAST
Repeati377 – 39923LRR 3Add
BLAST
Repeati441 – 46424LRR 4Add
BLAST
Domaini871 – 92353SH3Add
BLAST
Repeati1050 – 107324LRR 5Add
BLAST
Repeati1128 – 115427LRR 6Add
BLAST
Repeati1187 – 121024LRR 7Add
BLAST
Repeati1257 – 128226LRR 8Add
BLAST
Repeati1577 – 162145Plectin 1Add
BLAST
Repeati1654 – 169643Plectin 2Add
BLAST
Repeati1769 – 180941Plectin 3Add
BLAST
Repeati1811 – 184838Plectin 4Add
BLAST
Repeati1855 – 188632Plectin 5Add
BLAST
Repeati2290 – 233243Plectin 6Add
BLAST
Repeati2367 – 241044Plectin 7Add
BLAST
Repeati2411 – 243727Plectin 8Add
BLAST
Repeati2501 – 254343Plectin 9Add
BLAST
Repeati2581 – 261232Plectin 10Add
BLAST
Repeati2686 – 273045Plectin 11Add
BLAST
Repeati3239 – 326224LRR 9Add
BLAST
Repeati3264 – 328320LRR 10Add
BLAST
Repeati3646 – 366924LRR 11Add
BLAST
Repeati3696 – 372025LRR 12Add
BLAST
Repeati3883 – 395775Spectrin 1Add
BLAST
Repeati3936 – 395823LRR 13Add
BLAST
Repeati4000 – 4108109Spectrin 2Add
BLAST
Repeati4125 – 415026LRR 14Add
BLAST
Repeati4261 – 428727LRR 15Add
BLAST
Repeati4466 – 4574109Spectrin 3Add
BLAST
Repeati4511 – 453424LRR 16Add
BLAST
Repeati4601 – 462424LRR 17Add
BLAST
Repeati4769 – 479224LRR 18Add
BLAST
Repeati4800 – 4904105Spectrin 4Add
BLAST
Repeati4909 – 5012104Spectrin 5Add
BLAST
Repeati5051 – 507626LRR 19Add
BLAST
Repeati5172 – 519423LRR 20Add
BLAST
Repeati5236 – 5341106Spectrin 6Add
BLAST
Repeati5281 – 530424LRR 21Add
BLAST
Repeati5348 – 5450103Spectrin 7Add
BLAST
Repeati5455 – 5557103Spectrin 8Add
BLAST
Repeati5695 – 571925LRR 22Add
BLAST
Repeati5783 – 5885103Spectrin 9Add
BLAST
Repeati5804 – 582825LRR 23Add
BLAST
Repeati6005 – 6110106Spectrin 10Add
BLAST
Repeati6115 – 6219105Spectrin 11Add
BLAST
Repeati6225 – 6328104Spectrin 12Add
BLAST
Repeati6333 – 6439107Spectrin 13Add
BLAST
Repeati6443 – 6547105Spectrin 14Add
BLAST
Repeati6496 – 651924LRR 24Add
BLAST
Repeati6552 – 6658107Spectrin 15Add
BLAST
Repeati6665 – 6766102Spectrin 16Add
BLAST
Repeati6771 – 6874104Spectrin 17Add
BLAST
Domaini7041 – 707636EF-hand 1Add
BLAST
Domaini7077 – 711236EF-hand 2Add
BLAST
Domaini7117 – 718973GARAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7117 – 7388272C-terminal tail By similarityAdd
BLAST
Regioni7313 – 7328164 X 4 AA tandem repeats of [GS]-S-R-[AR]Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi698 – 7036Poly-Glu
Compositional biasi1122 – 11276Poly-Ser
Compositional biasi1414 – 14174Poly-Glu
Compositional biasi1986 – 19894Poly-Leu
Compositional biasi7222 – 7351130Ser-richAdd
BLAST

Domaini

The C-terminal tail is required for phosphorylation by GSK3B and for microtubule-binding By similarity.

Sequence similaritiesi

Contains 2 EF-hand domains.
Contains 1 GAR domain.
Contains 11 plectin repeats.
Contains 1 SH3 domain.
Contains 17 spectrin repeats.

Keywords - Domaini

Leucine-rich repeat, Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000049054.
HOVERGENiHBG031127.
PhylomeDBiQ9UPN3.
TreeFamiTF335163.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.418.10. 2 hits.
3.30.920.20. 1 hit.
3.90.1290.10. 5 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR003108. GAS2_dom.
IPR028408. Macf1.
IPR001101. Plectin_repeat.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PANTHERiPTHR11915:SF37. PTHR11915:SF37. 1 hit.
PfamiPF00307. CH. 2 hits.
PF13499. EF-hand_7. 1 hit.
PF02187. GAS2. 1 hit.
PF00681. Plectin. 11 hits.
PF00435. Spectrin. 17 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00243. GAS2. 1 hit.
SM00250. PLEC. 20 hits.
SM00150. SPEC. 33 hits.
[Graphical view]
SUPFAMiSSF143575. SSF143575. 1 hit.
SSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 6 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS51460. GAR. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UPN3-1) [UniParc]FASTAAdd to Basket

Also known as: Macf1b

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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MSSSDEETLS ERSCRSERSC RSERSYRSER SGSLSPCPPG DTLPWNLPLH     50
EQKKRKSQDS VLDPAERAVV RVADERDRVQ KKTFTKWVNK HLMKVRKHIN 100
DLYEDLRDGH NLISLLEVLS GIKLPREKGR MRFHRLQNVQ IALDFLKQRQ 150
VKLVNIRNDD ITDGNPKLTL GLIWTIILHF QISDIYISGE SGDMSAKEKL 200
LLWTQKVTAG YTGIKCTNFS SCWSDGKMFN ALIHRYRPDL VDMERVQIQS 250
NRENLEQAFE VAERLGVTRL LDAEDVDVPS PDEKSVITYV SSIYDAFPKV 300
PEGGEGISAT EVDSRWQEYQ SRVDSLIPWI KQHTILMSDK TFPQNPVELK 350
ALYNQYIHFK ETEILAKERE KGRIEELYKL LEVWIEFGRI KLPQGYHPND 400
VEEEWGKLII EMLEREKSLR PAVERLELLL QIANKIQNGA LNCEEKLTLA 450
KNTLQADAAH LESGQPVQCE SDVIMYIQEC EGLIRQLQVD LQILRDENYY 500
QLEELAFRVM RLQDELVTLR LECTNLYRKG HFTSLELVPP STLTTTHLKA 550
EPLTKATHSS STSWFRKPMT RAELVAISSS EDEGNLRFVY ELLSWVEEMQ 600
MKLERAEWGN DLPSVELQLE TQQHIHTSVE ELGSSVKEAR LYEGKMSQNF 650
HTSYAETLGK LETQYCKLKE TSSFRMRHLQ SLHKFVSRAT AELIWLNEKE 700
EEELAYDWSD NNSNISAKRN YFSELTMELE EKQDVFRSLQ DTAELLSLEN 750
HPAKQTVEAY SAAVQSQLQW MKQLCLCVEQ HVKENTAYFQ FFSDARELES 800
FLRNLQDSIK RKYSCDHNTS LSRLEDLLQD SMDEKEQLIQ SKSSVASLVG 850
RSKTIVQLKP RSPDHVLKNT ISVKAVCDYR QIEITICKND ECVLEDNSQR 900
TKWKVISPTG NEAMVPSVCF LIPPPNKDAI EMASRVEQSY QKVMALWHQL 950
HVNTKSLISW NYLRKDLDLV QTWNLEKLRS SAPGECHQIM KNLQAHYEDF 1000
LQDSRDSVLF SVADRLRLEE EVEACKARFQ HLMKSMENED KEETVAKMYI 1050
SELKNIRLRL EEYEQRVVKR IQSLASSRTD RDAWQDNALR IAEQEHTQED 1100
LQQLRSDLDA VSMKCDSFLH QSPSSSSVPT LRSELNLLVE KMDHVYGLST 1150
VYLNKLKTVD VIVRSIQDAE LLVKGYEIKL SQEEVVLADL SALEAHWSTL 1200
RHWLSDVKDK NSVFSVLDEE IAKAKVVAEQ MSRLTPERNL DLERYQEKGS 1250
QLQERWHRVI AQLEIRQSEL ESIQEVLGDY RACHGTLIKW IEETTAQQEM 1300
MKPGQAEDSR VLSEQLSQQT ALFAEIERNQ TKLDQCQKFS QQYSTIVKDY 1350
ELQLMTYKAF VESQQKSPGK RRRMLSSSDA ITQEFMDLRT RYTALVTLTT 1400
QHVKYISDAL RRLEEEEKVV EEEKQEHVEK VKELLGWVST LARNTQGKAT 1450
SSETKESTDI EKAILEQQVL SEELTTKKEQ VSEAIKTSQI FLAKHGHKLS 1500
EKEKKQISEQ LNALNKAYHD LCDGSANQLQ QLQSQLAHQT EQKECRAVAG 1550
VIDLGTVEIF PIFKAMQKGL LDQDTGLVLL ESQVIMSGLI APETGENLSL 1600
EEGIARNLIN PQMYQQLREL QDALALISRL TESRGPLSVV EAIEKRIISE 1650
TVGLKILEAH LATGGFSLSP SENCINLEEA FHQGLISAWL HSVLESYLRT 1700
SKNLIDPNTA EKIGLLDLMQ RCIVHQESGF KLLPVKQLAG GMVSLKSGRK 1750
VSIFRAVQEG LIDRQVTVRL LEAQLFAGGI VDPRTGHRLT VEEAVRHNLI 1800
DQDMACAILI RQLQTGGIID TVTGQRLTID EAVSNDLVAA KIALVILESL 1850
WSFMGLLWPE SGEILPITDA LEQGIVSTEL AHKILSNRQH IKALFLPATT 1900
EILSWKKAIE SGILDRDLAN NLKSICIPDV MPHMQLADSA EQNINPGAAV 1950
LPCSKSHPKA TASQSENLLF QLMTHSYINV QNGQRLLLLD KELMETLTSR 2000
DEYQTSPPKV VEIGHQRQKT PEGLQESANV KISGTFSSGW TVRLPEFQFS 2050
SQNKEYPDRE DCTTEKGKKT TVETEDSSVE NPEQDLFVEQ KERNPNIDAL 2100
KVINKVKLEV QRQLIGTQRE DQTAVSVREN ASRGHLLTIP PAEAEGVPLV 2150
VDKDVFSVET PKKEHQPLRN TSFTCQNEQA HTLETEYIHD ETGGSHIKPQ 2200
SKKLQVQVKK TLGIKLELKS ETDGNVHPLD KKEMLKKTFL AKDDHKESQE 2250
AQNIAGGSMM MSEKTDEEDS GREIFLSCSH PLELLEEATL NVLSAQLLDG 2300
GIFHEQTGQK LLLNEAISRG IVPSHTAVKL MEKLNMFQGF FDSQTCESLT 2350
TEEVINEGLM DEKLLHNVLM ADKAISGVLD PRTQTLCSVK DAVTVGLLDK 2400
ETATRILERQ VVTGGIIDLK RGKKVSVTLA STLGLVDVAD QPELINLEKA 2450
SKGRDAEKTV RERLISLQME TTGLIDPDSK APLTVVQSID RGLLEREEAV 2500
RLLTKQVVDG GIIHHISGMR LSVDNAFRHG LIGEDLAEKL KRVENLNIHQ 2550
IFNPETKENI SLPKAIKLDL ITSDLKREIQ EVQAFTGNFV DLISGQRLTL 2600
AEAKKEGLLT NEAVLSPGMM HGIVDPENCR IVPYSELVKK CKIDIESGQR 2650
YLEVIPFSDI KDGVSDKVLT LSQAIQLGKV DFASTLKVLE AQANTGGIID 2700
TATGKRLTLA SALEEKLVDE NMVRIIASHQ VLNGGIVDIF SDQRVTLVEA 2750
IEKRLISPEL ANMIQIDSSE FSDHRAQIEK QEGIEVCALQ NEFLGKDMLI 2800
ACNQTAEMSC NKVEESERLF QVENQSAQEK VKVRVSDGEQ AKKSREISLK 2850
EFGCKDQRKP RMSSDAKEFI SIINPHNLKG KSLGQVSLTH PYSECDFKLK 2900
EVARNNMGND TNEEQEKAVT KIEIISHMKQ STSCLDSEEI RENQGEVILE 2950
VQETYCETSG KLPSEQVLQQ PMNARVKSKR EKREVIVEES IRTCKPAFLS 3000
EEKLYQETAI RDEHDSHIKS QPREMTSSEK GKEADTEMGF SITFKIEESS 3050
SQVVPQGISV KHLDALTLFS SKQANEGKVN NLSLCLTLKP EENLSREIAC 3100
GAQSEPFPCM TPRPEGLHYQ ESDGKAQVTG PSQISKTDKS FQGTTRQETN 3150
YQDSWVTSKT KETKHQISSS NECKEKSYQE VSFDPARGLK LEEITVSRPD 3200
SKEVRYLEFS DRKDLHHQGS KSDDKLCGTL KSEIATQELT GEKFLEMANP 3250
NVAGLEAGSI EDIVTQRGSR VLGSFLPEKL FKGVSQKENT GQQNAIISPT 3300
VLETSEEKTV SLTVCSAVKT EKTPQEKLRE SPGSEQTPFM TAPEGKGNGG 3350
VNPEPFRATQ NVFTRQLCLE HDEKLVSYLS LLRNIEMRTK QIQPLELNLA 3400
ELQDLLCQAK VLERELKDLT TLVSQELECV NQIIISQPQE VPAQLLKALE 3450
KDAKNLQKSL SSVSDTWNSR LLHFQNAVEI EKTKVLNQHT QLEGRLQDLR 3500
AWVGNKNLIL NSKGSNSEID VDSLNLCLQQ YEDLKQPMAE RKAQLDALAF 3550
DIQFFISEHA QDLSPQQNRQ MLRLLNELQR SFQDILEQTA AQVDALQGHL 3600
QQMEQEALVK TLQKQQNTCH QQLEDLCSWV GQAERALAGH QGRTTQQDLS 3650
ALQKNQSDLK DLQDDIQNRA TSFATVVKDI EGFMEENQTK LSPRELTALR 3700
EKLHQAKEQY EALQEETRVA QKELEEAVTS ALQQETEKSK AAKELAENKK 3750
KIDALLDWVT SVGSSGGQLL TNLPGMEQLS GASLEKGALD TTDGYMGVNQ 3800
APEKLDKQCE MMKARHQELL SQQQNFILAT QSAQAFLDQH GHNLTPEEQQ 3850
MLQQKLGELK EQYSTSLAQS EAELKQVQTL QDELQKFLQD HKEFESWLER 3900
SEKELENMHK GGSSPETLPS LLKRQGSFSE DVISHKGDLR FVTISGQKVL 3950
DMENSFKEGK EPSEIGNLVK DKLKDATERY TALHSKCTRL GSHLNMLLGQ 4000
YHQFQNSADS LQAWMQACEA NVEKLLSDTV ASDPGVLQEQ LATTKQLQEE 4050
LAEHQVPVEK LQKVARDIME IEGEPAPDHR HVQETTDSIL SHFQSLSYSL 4100
AERSSLLQKA IAQSQSVQES LESLLQSIGE VEQNLEGKQV SSLSSGVIQE 4150
ALATNMKLKQ DIARQKSSLE ATREMVTRFM ETADSTTAAV LQGKLAEVSQ 4200
RFEQLCLQQQ EKESSLKKLL PQAEMFEHLS GKLQQFMENK SRMLASGNQP 4250
DQDITHFFQQ IQELNLEMED QQENLDTLEH LVTELSSCGF ALDLCQHQDR 4300
VQNLRKDFTE LQKTVKEREK DASSCQEQLD EFRKLVRTFQ KWLKETEGSI 4350
PPTETSMSAK ELEKQIEHLK SLLDDWASKG TLVEEINCKG TSLENLIMEI 4400
TAPDSQGKTG SILPSVGSSV GSVNGYHTCK DLTEIQCDMS DVNLKYEKLG 4450
GVLHERQESL QAILNRMEEV HKEANSVLQW LESKEEVLKS MDAMSSPTKT 4500
ETVKAQAESN KAFLAELEQN SPKIQKVKEA LAGLLVTYPN SQEAENWKKI 4550
QEELNSRWER ATEVTVARQR QLEESASHLA CFQAAESQLR PWLMEKELMM 4600
GVLGPLSIDP NMLNAQKQQV QFMLKEFEAR RQQHEQLNEA AQGILTGPGD 4650
VSLSTSQVQK ELQSINQKWV ELTDKLNSRS SQIDQAIVKS TQYQELLQDL 4700
SEKVRAVGQR LSVQSAISTQ PEAVKQQLEE TSEIRSDLEQ LDHEVKEAQT 4750
LCDELSVLIG EQYLKDELKK RLETVALPLQ GLEDLAADRI NRLQAALAST 4800
QQFQQMFDEL RTWLDDKQSQ QAKNCPISAK LERLQSQLQE NEEFQKSLNQ 4850
HSGSYEVIVA EGESLLLSVP PGEEKRTLQN QLVELKNHWE ELSKKTADRQ 4900
SRLKDCMQKA QKYQWHVEDL VPWIEDCKAK MSELRVTLDP VQLESSLLRS 4950
KAMLNEVEKR RSLLEILNSA ADILINSSEA DEDGIRDEKA GINQNMDAVT 5000
EELQAKTGSL EEMTQRLREF QESFKNIEKK VEGAKHQLEI FDALGSQACS 5050
NKNLEKLRAQ QEVLQALEPQ VDYLRNFTQG LVEDAPDGSD ASQLLHQAEV 5100
AQQEFLEVKQ RVNSGCVMME NKLEGIGQFH CRVREMFSQL ADLDDELDGM 5150
GAIGRDTDSL QSQIEDVRLF LNKIHVLKLD IEASEAECRH MLEEEGTLDL 5200
LGLKRELEAL NKQCGKLTER GKARQEQLEL TLGRVEDFYR KLKGLNDATT 5250
AAEEAEALQW VVGTEVEIIN QQLADFKMFQ KEQVDPLQMK LQQVNGLGQG 5300
LIQSAGKDCD VQGLEHDMEE INARWNTLNK KVAQRIAQLQ EALLHCGKFQ 5350
DALEPLLSWL ADTEELIANQ KPPSAEYKVV KAQIQEQKLL QRLLDDRKAT 5400
VDMLQAEGGR IAQSAELADR EKITGQLESL ESRWTELLSK AAARQKQLED 5450
ILVLAKQFHE TAEPISDFLS VTEKKLANSE PVGTQTAKIQ QQIIRHKALN 5500
EEIVNRKKNV DQAIKNGQAL LKQTTGEEVL LIQEKLDGIK TRYADITVTS 5550
SKALRTLEQA RQLATKFQST YEELTGWLRE VEEELATSGG QSPTGEQIPQ 5600
FQQRQKELKK EVMEHRLVLD TVNEVSRALL ELVPWRAREG LDKLVSDANE 5650
QYKLVSDTIG QRVDEIDAAI QRSQQYEQAA DAELAWVAET KRKLMALGPI 5700
RLEQDQTTAQ LQVQKAFSID IIRHKDSMDE LFSHRSEIFG TCGEEQKTVL 5750
QEKTESLIQQ YEAISLLNSE RYARLERAQV LVNQFWETYE ELSPWIEETR 5800
ALIAQLPSPA IDHEQLRQQQ EEMRQLRESI AEHKPHIDKL LKIGPQLKEL 5850
NPEEGEMVEE KYQKAENMYA QIKEEVRQRA LALDEAVSQS TQITEFHDKI 5900
EPMLETLENL SSRLRMPPLI PAEVDKIREC ISDNKSATVE LEKLQPSFEA 5950
LKRRGEELIG RSQGADKDLA AKEIQDKLDQ MVFFWEDIKA RAEEREIKFL 6000
DVLELAEKFW YDMAALLTTI KDTQDIVHDL ESPGIDPSII KQQVEAAETI 6050
KEETDGLHEE LEFIRILGAD LIFACGETEK PEVRKSIDEM NNAWENLNKT 6100
WKERLEKLED AMQAAVQYQD TLQAMFDWLD NTVIKLCTMP PVGTDLNTVK 6150
DQLNEMKEFK VEVYQQQIEM EKLNHQGELM LKKATDETDR DIIREPLTEL 6200
KHLWENLGEK IAHRQHKLEG ALLALGQFQH ALEELMSWLT HTEELLDAQR 6250
PISGDPKVIE VELAKHHVLK NDVLAHQATV ETVNKAGNEL LESSAGDDAS 6300
SLRSRLEAMN QCWESVLQKT EEREQQLQST LQQAQGFHSE IEDFLLELTR 6350
MESQLSASKP TGGLPETARE QLDTHMELYS QLKAKEETYN QLLDKGRLML 6400
LSRDDSGSGS KTEQSVALLE QKWHVVSSKM EERKSKLEEA LNLATEFQNS 6450
LQEFINWLTL AEQSLNIASP PSLILNTVLS QIEEHKVFAN EVNAHRDQII 6500
ELDQTGNQLK FLSQKQDVVL IKNLLVSVQS RWEKVVQRSI ERGRSLDDAR 6550
KRAKQFHEAW KKLIDWLEDA ESHLDSELEI SNDPDKIKLQ LSKHKEFQKT 6600
LGGKQPVYDT TIRTGRALKE KTLLPEDSQK LDNFLGEVRD KWDTVCGKSV 6650
ERQHKLEEAL LFSGQFMDAL QALVDWLYKV EPQLAEDQPV HGDLDLVMNL 6700
MDAHKVFQKE LGKRTGTVQV LKRSGRELIE NSRDDTTWVK GQLQELSTRW 6750
DTVCKLSVSK QSRLEQALKQ AEVFRDTVHM LLEWLSEAEQ TLRFRGALPD 6800
DTEALQSLID THKEFMKKVE EKRVDVNSAV AMGEVILAVC HPDCITTIKH 6850
WITIIRARFE EVLTWAKQHQ QRLETALSEL VANAELLEEL LAWIQWAETT 6900
LIQRDQEPIP QNIDRVKALI AEHQTFMEEM TRKQPDVDRV TKTYKRKNIE 6950
PTHAPFIEKS RSGGRKSLSQ PTPPPMPILS QSEAKNPRIN QLSARWQQVW 7000
LLALERQRKL NDALDRLEEL KEFANFDFDV WRKKYMRWMN HKKSRVMDFF 7050
RRIDKDQDGK ITRQEFIDGI LASKFPTTKL EMTAVADIFD RDGDGYIDYY 7100
EFVAALHPNK DAYRPTTDAD KIEDEVTRQV AQCKCAKRFQ VEQIGENKYR 7150
FGDSQQLRLV RILRSTVMVR VGGGWMALDE FLVKNDPCRA RGRTNIELRE 7200
KFILPEGASQ GMTPFRSRGR RSKPSSRAAS PTRSSSSASQ SNHSCTSMPS 7250
SPATPASGTK VIPSSGSKLK RPTPTFHSSR TSLAGDTSNS SSPASTGAKT 7300
NRADPKKSAS RPGSRAGSRA GSRASSRRGS DASDFDLLET QSACSDTSES 7350
SAAGGQGNSR RGLNKPSKIP TMSKKTTTAS PRTPGPKR 7388
Length:7,388
Mass (Da):838,308
Last modified:June 28, 2011 - v4
Checksum:iB044DC183C048416
GO
Isoform 2 (identifier: Q9UPN3-2) [UniParc]FASTAAdd to Basket

Also known as: Macf1a

The sequence of this isoform differs from the canonical sequence as follows:
     1543-3609: Missing.
     5497-5497: K → KALEEDIENH...VLHRQHADHL

Show »
Length:5,430
Mass (Da):620,418
Checksum:i4C0CB72BDFBF9777
GO
Isoform 3 (identifier: Q9UPN3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: MSSSDEETLS...DPAERAVVRV → MFPVLWAGIP...CTSASRVAVI
     1543-3609: Missing.
     4410-4430: Missing.
     5497-5497: K → KALEEDIENH...VLHRQHADHL

Show »
Length:5,374
Mass (Da):614,153
Checksum:i503537231A91ABDA
GO
Isoform 5 (identifier: Q9UPN3-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1543-3609: Missing.
     4410-4430: Missing.

Note: No experimental confirmation available.

Show »
Length:5,300
Mass (Da):606,164
Checksum:iE5364BDE41CBB545
GO
Isoform 4 (identifier: Q9UPN3-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1565: Missing.
     5497-5497: K → KALEEDIENH...VLHRQHADHL
     7150-7150: R → RFFLGNQ

Show »
Length:5,938
Mass (Da):670,137
Checksum:i360611C48946A058
GO

Sequence cautioni

The sequence BAA83821.1 differs from that shown. Reason: Frameshift at positions 575 and 594.
The sequence CAH70156.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAH73668.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI16417.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI21814.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti302 – 3021E → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_035451
Natural varianti4357 – 43571M → V.1 Publication
Corresponds to variant rs2296172 [ dbSNP | Ensembl ].
VAR_048625
Natural varianti6201 – 62011K → R.
Corresponds to variant rs682351 [ dbSNP | Ensembl ].
VAR_048626
Natural varianti6308 – 63081A → T.
Corresponds to variant rs587404 [ dbSNP | Ensembl ].
VAR_048627
Natural varianti6462 – 64621E → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_035452
Natural varianti6628 – 66281S → T.2 Publications
Corresponds to variant rs668556 [ dbSNP | Ensembl ].
VAR_048628
Natural varianti6752 – 67521T → I.
Corresponds to variant rs2296174 [ dbSNP | Ensembl ].
VAR_048629
Natural varianti6855 – 68551I → V.
Corresponds to variant rs12068423 [ dbSNP | Ensembl ].
VAR_048630
Natural varianti7093 – 70931G → E in a breast cancer sample; somatic mutation. 1 Publication
VAR_065256

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 15651565Missing in isoform 4. VSP_043626Add
BLAST
Alternative sequencei1 – 7272MSSSD…AVVRV → MFPVLWAGIPGRDVGSLQPL PPGFKQFCTSASRVAVI in isoform 3. VSP_041390Add
BLAST
Alternative sequencei1543 – 36092067Missing in isoform 2, isoform 3 and isoform 5. VSP_041391Add
BLAST
Alternative sequencei4410 – 443021Missing in isoform 3 and isoform 5. VSP_041392Add
BLAST
Alternative sequencei5497 – 54971K → KALEEDIENHATDVHQAVKI GQSLSSLTSPAEQGVLSEKI DSLQARYSEIQDRCCRKAAL LDQALSNARLFGEDEVEVLN WLAEVEDKLSSVFVKDFKQD VLHRQHADHL in isoform 2, isoform 3 and isoform 4. VSP_041393
Alternative sequencei7150 – 71501R → RFFLGNQ in isoform 4. VSP_043627

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1295 – 12962TA → LP in AAL39000. 1 Publication
Sequence conflicti1487 – 14871T → A in BAA83821. 1 Publication
Sequence conflicti1487 – 14871T → A in AAL39000. 1 Publication
Sequence conflicti3277 – 32771P → S in AAL38997. 1 Publication
Sequence conflicti4030 – 40301V → A in BAA83821. 1 Publication
Sequence conflicti4119 – 41191E → D in BAA83821. 1 Publication
Sequence conflicti4150 – 41501E → K in AAF06360. 1 Publication
Sequence conflicti4388 – 43881C → Y in BAA83821. 1 Publication
Sequence conflicti4411 – 44177SILPSVG → EYRLFKI in BAA86565. 1 Publication
Sequence conflicti4590 – 45901R → Q in BAA83821. 1 Publication
Sequence conflicti6791 – 67911Missing in AAF06360. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB029290 mRNA. Translation: BAA83821.1. Frameshift.
AF141968 mRNA. Translation: AAF06360.1.
AF317696 mRNA. Translation: AAL09459.1.
AF325341
, AF325333, AF325334, AF325335, AF325336, AF325339, AF325340 Genomic DNA. Translation: AAL38997.1.
AF325341
, AF325330, AF325331, AF325332, AF325333, AF325334, AF325335, AF325336, AF325339, AF325340 Genomic DNA. Translation: AAL39000.1.
AL442071
, AL137853, AL355477, AL365277 Genomic DNA. Translation: CAH73668.1. Sequence problems.
AL442071, AL137853, AL365277 Genomic DNA. Translation: CAH73671.1.
AL137853
, AL355477, AL365277, AL442071 Genomic DNA. Translation: CAI21814.1. Sequence problems.
AL137853, AL365277, AL442071 Genomic DNA. Translation: CAI21816.1.
AL365277
, AL137853, AL355477, AL442071 Genomic DNA. Translation: CAI16417.1. Sequence problems.
AL365277, AL137853, AL442071 Genomic DNA. Translation: CAI16422.1.
AL355477
, AL137853, AL365277, AL442071 Genomic DNA. Translation: CAH70156.1. Sequence problems.
AL356055 Genomic DNA. No translation available.
AB033077 mRNA. Translation: BAA86565.1.
AB007934 mRNA. Translation: BAA32310.3.
CCDSiCCDS435.1. [Q9UPN3-2]
PIRiT00079.
RefSeqiNP_036222.3. NM_012090.5. [Q9UPN3-2]
UniGeneiHs.472475.
Hs.692278.

Genome annotation databases

EnsembliENST00000289893; ENSP00000289893; ENSG00000127603. [Q9UPN3-5]
ENST00000361689; ENSP00000354573; ENSG00000127603. [Q9UPN3-2]
ENST00000372915; ENSP00000362006; ENSG00000127603. [Q9UPN3-1]
ENST00000545844; ENSP00000439537; ENSG00000127603. [Q9UPN3-2]
GeneIDi23499.
KEGGihsa:23499.
UCSCiuc001cda.1. human. [Q9UPN3-3]
uc021olt.1. human. [Q9UPN3-2]
uc031pmd.1. human. [Q9UPN3-5]

Polymorphism databases

DMDMi338817989.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB029290 mRNA. Translation: BAA83821.1 . Frameshift.
AF141968 mRNA. Translation: AAF06360.1 .
AF317696 mRNA. Translation: AAL09459.1 .
AF325341
, AF325333 , AF325334 , AF325335 , AF325336 , AF325339 , AF325340 Genomic DNA. Translation: AAL38997.1 .
AF325341
, AF325330 , AF325331 , AF325332 , AF325333 , AF325334 , AF325335 , AF325336 , AF325339 , AF325340 Genomic DNA. Translation: AAL39000.1 .
AL442071
, AL137853 , AL355477 , AL365277 Genomic DNA. Translation: CAH73668.1 . Sequence problems.
AL442071 , AL137853 , AL365277 Genomic DNA. Translation: CAH73671.1 .
AL137853
, AL355477 , AL365277 , AL442071 Genomic DNA. Translation: CAI21814.1 . Sequence problems.
AL137853 , AL365277 , AL442071 Genomic DNA. Translation: CAI21816.1 .
AL365277
, AL137853 , AL355477 , AL442071 Genomic DNA. Translation: CAI16417.1 . Sequence problems.
AL365277 , AL137853 , AL442071 Genomic DNA. Translation: CAI16422.1 .
AL355477
, AL137853 , AL365277 , AL442071 Genomic DNA. Translation: CAH70156.1 . Sequence problems.
AL356055 Genomic DNA. No translation available.
AB033077 mRNA. Translation: BAA86565.1 .
AB007934 mRNA. Translation: BAA32310.3 .
CCDSi CCDS435.1. [Q9UPN3-2 ]
PIRi T00079.
RefSeqi NP_036222.3. NM_012090.5. [Q9UPN3-2 ]
UniGenei Hs.472475.
Hs.692278.

3D structure databases

ProteinModelPortali Q9UPN3.
SMRi Q9UPN3. Positions 69-298.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117048. 36 interactions.
DIPi DIP-50616N.
IntActi Q9UPN3. 26 interactions.
MINTi MINT-1195815.
STRINGi 9606.ENSP00000289893.

PTM databases

PhosphoSitei Q9UPN3.

Polymorphism databases

DMDMi 338817989.

Proteomic databases

MaxQBi Q9UPN3.
PaxDbi Q9UPN3.
PRIDEi Q9UPN3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000289893 ; ENSP00000289893 ; ENSG00000127603 . [Q9UPN3-5 ]
ENST00000361689 ; ENSP00000354573 ; ENSG00000127603 . [Q9UPN3-2 ]
ENST00000372915 ; ENSP00000362006 ; ENSG00000127603 . [Q9UPN3-1 ]
ENST00000545844 ; ENSP00000439537 ; ENSG00000127603 . [Q9UPN3-2 ]
GeneIDi 23499.
KEGGi hsa:23499.
UCSCi uc001cda.1. human. [Q9UPN3-3 ]
uc021olt.1. human. [Q9UPN3-2 ]
uc031pmd.1. human. [Q9UPN3-5 ]

Organism-specific databases

CTDi 23499.
GeneCardsi GC01P039546.
HGNCi HGNC:13664. MACF1.
HPAi HPA013713.
MIMi 608271. gene.
neXtProti NX_Q9UPN3.
PharmGKBi PA30518.
HUGEi Search...
Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000049054.
HOVERGENi HBG031127.
PhylomeDBi Q9UPN3.
TreeFami TF335163.

Enzyme and pathway databases

SignaLinki Q9UPN3.

Miscellaneous databases

ChiTaRSi MACF1. human.
GeneWikii MACF1.
GenomeRNAii 23499.
NextBioi 45871.
PROi Q9UPN3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UPN3.
Bgeei Q9UPN3.
CleanExi HS_MACF1.
Genevestigatori Q9UPN3.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
1.10.418.10. 2 hits.
3.30.920.20. 1 hit.
3.90.1290.10. 5 hits.
InterProi IPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR003108. GAS2_dom.
IPR028408. Macf1.
IPR001101. Plectin_repeat.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view ]
PANTHERi PTHR11915:SF37. PTHR11915:SF37. 1 hit.
Pfami PF00307. CH. 2 hits.
PF13499. EF-hand_7. 1 hit.
PF02187. GAS2. 1 hit.
PF00681. Plectin. 11 hits.
PF00435. Spectrin. 17 hits.
[Graphical view ]
SMARTi SM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00243. GAS2. 1 hit.
SM00250. PLEC. 20 hits.
SM00150. SPEC. 33 hits.
[Graphical view ]
SUPFAMi SSF143575. SSF143575. 1 hit.
SSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 6 hits.
PROSITEi PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS51460. GAR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of macrophin, a human homologue of Drosophila kakapo with a close structural similarity to plectin and dystrophin."
    Okuda T., Matsuda S., Nakatsugawa S., Ichigotani Y., Iwahashi N., Takahashi M., Ishigaki T., Hamaguchi M.
    Biochem. Biophys. Res. Commun. 264:568-574(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Molecular cloning and characterization of human trabeculin-alpha, a giant protein defining a new family of actin-binding proteins."
    Sun Y., Zhang J., Kraeft S.-K., Auclair D., Chang M.-S., Liu Y., Sutherland R., Salgia R., Griffin J.D., Ferland L.H., Chen L.B.
    J. Biol. Chem. 274:33522-33530(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANTS VAL-4357 AND THR-6628.
  3. "MACF1 gene structure: a hybrid of plectin and dystrophin."
    Gong T.-W.L., Besirli C.G., Lomax M.I.
    Mamm. Genome 12:852-861(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 182-6770 (ISOFORM 1), ALTERNATIVE SPLICING, TISSUE SPECIFICITY, VARIANT THR-6628.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
    DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 868-4417 (ISOFORM 2).
    Tissue: Brain.
  6. "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
    Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
    DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 868-7388 (ISOFORM 5).
    Tissue: Brain.
  7. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  8. Ohara O.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  9. "Interaction between p230 and MACF1 is associated with transport of a glycosyl phosphatidyl inositol-anchored protein from the Golgi to the cell periphery."
    Kakinuma T., Ichikawa H., Tsukada Y., Nakamura T., Toh B.H.
    Exp. Cell Res. 298:388-398(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GOLGA4.
  10. "Microtubule actin crosslinking factor 1b: a novel plakin that localizes to the Golgi complex."
    Lin C.-M., Chen H.-J., Leung C.L., Parry D.A.D., Liem R.K.H.
    J. Cell Sci. 118:3727-3738(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF ISOFORM 1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1376; SER-3927; SER-4495; SER-4496; SER-6967; THR-7254; SER-7292 AND SER-7330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1376; SER-4521 AND SER-7330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells."
    Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.
    Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-1376; SER-3927 AND SER-4521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-1376; SER-3927; SER-4496; SER-4521 AND SER-4962, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-302; GLN-6462 AND GLU-7093.

Entry informationi

Entry nameiMACF1_HUMAN
AccessioniPrimary (citable) accession number: Q9UPN3
Secondary accession number(s): B1ALC5
, E9PJT0, O75053, Q5VW20, Q8WXY1, Q8WXY2, Q96PK2, Q9H540, Q9UKP0, Q9ULG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 28, 2011
Last modified: July 9, 2014
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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