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P78559

- MAP1A_HUMAN

UniProt

P78559 - MAP1A_HUMAN

Protein

Microtubule-associated protein 1A

Gene

MAP1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 6 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    Structural protein involved in the filamentous cross-bridging between microtubules and other skeletal elements.

    GO - Molecular functioni

    1. hydrolase activity Source: InterPro
    2. protein binding Source: UniProtKB
    3. structural molecule activity Source: ProtInc

    GO - Biological processi

    1. microtubule cytoskeleton organization Source: InterPro
    2. sensory perception of sound Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Microtubule-associated protein 1A
    Short name:
    MAP-1A
    Alternative name(s):
    Proliferation-related protein p80
    Cleaved into the following 2 chains:
    Gene namesi
    Name:MAP1A
    Synonyms:MAP1L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:6835. MAP1A.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. microtubule Source: UniProtKB-KW
    3. microtubule associated complex Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 28032803Microtubule-associated protein 1APRO_0000018600Add
    BLAST
    Chaini1 – 25662566MAP1A heavy chainPRO_0000418376Add
    BLAST
    Chaini2567 – 2803237MAP1 light chain LC2PRO_0000018601Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei177 – 1771PhosphotyrosineBy similarity
    Modified residuei526 – 5261PhosphoserineBy similarity
    Modified residuei527 – 5271PhosphoserineBy similarity
    Modified residuei612 – 6121Phosphoserine3 Publications
    Modified residuei616 – 6161Phosphothreonine3 Publications
    Modified residuei644 – 6441PhosphoserineBy similarity
    Modified residuei667 – 6671Phosphoserine1 Publication
    Modified residuei896 – 8961Phosphoserine1 Publication
    Modified residuei986 – 9861PhosphoserineBy similarity
    Modified residuei1008 – 10081Phosphothreonine1 Publication
    Modified residuei1013 – 10131Phosphoserine1 Publication
    Modified residuei1069 – 10691Phosphoserine1 Publication
    Modified residuei1160 – 11601Phosphoserine1 Publication
    Modified residuei1218 – 12181Phosphoserine1 Publication
    Modified residuei1326 – 13261Phosphoserine1 Publication
    Modified residuei1329 – 13291Phosphoserine1 Publication
    Modified residuei1654 – 16541Phosphoserine1 Publication
    Modified residuei1675 – 16751Phosphoserine1 Publication
    Modified residuei1776 – 17761Phosphoserine1 Publication
    Modified residuei1791 – 17911Phosphoserine1 Publication
    Modified residuei1797 – 17971Phosphoserine1 Publication
    Modified residuei1801 – 18011Phosphoserine1 Publication
    Modified residuei2022 – 20221Phosphoserine3 Publications
    Modified residuei2104 – 21041Phosphoserine1 Publication
    Modified residuei2449 – 24491Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by CSNK1D.By similarity
    LC2 is generated from MAP1A by proteolytic processing.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP78559.
    PaxDbiP78559.
    PRIDEiP78559.

    PTM databases

    PhosphoSiteiP78559.

    Expressioni

    Tissue specificityi

    Brain.

    Gene expression databases

    ArrayExpressiP78559.
    BgeeiP78559.
    CleanExiHS_MAP1A.
    GenevestigatoriP78559.

    Organism-specific databases

    HPAiHPA039063.
    HPA039064.

    Interactioni

    Subunit structurei

    3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins. Interacts with TIAM2. Interacts with guanylate kinase-like domain of DLG1, DLG2, DLG4. Binds to CSNK1D By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DISC1Q9NRI53EBI-929047,EBI-529989

    Protein-protein interaction databases

    BioGridi110303. 19 interactions.
    IntActiP78559. 10 interactions.
    MINTiMINT-1203375.
    STRINGi9606.ENSP00000300231.

    Structurei

    3D structure databases

    ProteinModelPortaliP78559.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati415 – 41731
    Repeati420 – 42232
    Repeati427 – 42933
    Repeati431 – 43334
    Repeati436 – 43835
    Repeati440 – 44236
    Repeati444 – 44637
    Repeati449 – 45138
    Repeati539 – 54139

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni415 – 5411279 X 3 AA repeats of K-K-[DE]Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi309 – 496188Lys-rich (basic)Add
    BLAST

    Domaini

    The basic region containing the repeats may be responsible for the binding of MAP1A to microtubules.

    Sequence similaritiesi

    Belongs to the MAP1 family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000231839.
    HOVERGENiHBG052408.
    KOiK10429.
    PhylomeDBiP78559.
    TreeFamiTF350229.

    Family and domain databases

    Gene3Di3.60.15.10. 2 hits.
    InterProiIPR001279. Beta-lactamas-like.
    IPR026074. MAP1.
    IPR015656. MAP1A.
    [Graphical view]
    PANTHERiPTHR13843. PTHR13843. 1 hit.
    PTHR13843:SF6. PTHR13843:SF6. 1 hit.
    SUPFAMiSSF56281. SSF56281. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P78559-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MDGVAEFSEY VSETVDVPSP FDLLEPPTSG GFLKLSKPCC YIFPGGRGDS     50
    ALFAVNGFNI LVDGGSDRKS CFWKLVRHLD RIDSVLLTHI GADNLPGING 100
    LLQRKVAELE EEQSQGSSSY SDWVKNLISP ELGVVFFNVP EKLRLPDASR 150
    KAKRSIEEAC LTLQHLNRLG IQAEPLYRVV SNTIEPLTLF HKMGVGRLDM 200
    YVLNPVKDSK EMQFLMQKWA GNSKAKTGIV LPNGKEAEIS VPYLTSITAL 250
    VVWLPANPTE KIVRVLFPGN APQNKILEGL EKLRHLDFLR YPVATQKDLA 300
    SGAVPTNLKP SKIKQRADSK ESLKATTKTA VSKLAKREEV VEEGAKEARS 350
    ELAKELAKTE KKAKESSEKP PEKPAKPERV KTESSEALKA EKRKLIKDKV 400
    GKKHLKEKIS KLEEKKDKEK KEIKKERKEL KKDEGRKEEK KDAKKEEKRK 450
    DTKPELKKIS KPDLKPFTPE VRKTLYKAKV PGRVKIDRSR AIRGEKELSS 500
    EPQTPPAQKG TVPLPTISGH RELVLSSPED LTQDFEEMKR EERALLAEQR 550
    DTGLGDKPFP LDTAEEGPPS TAIQGTPPSV PGLGQEEHVM KEKELVPEVP 600
    EEQGSKDRGL DSGAETEEEK DTWEEKKQRE AERLPDRTEA REESEPEVKE 650
    DVIEKAELEE MEEVHPSDEE EEDATKAEGF YQKHMQEPLK VTPRSREAFG 700
    GRELGLQGKA PEKETSLFLS SLTTPAGATE HVSYIQDETI PGYSETEQTI 750
    SDEEIHDEPE ERPAPPRFHT STYDLPGPEG AGPFEASQPA DSAVPATSGK 800
    VYGTPETELT YPTNIVAAPL AEEEHVSSAT SITECDKLSS FATSVAEDQS 850
    VASLTAPQTE ETGKSSLLLD TVTSIPSSRT EATQGLDYVP SAGTISPTSS 900
    LEEDKGFKSP PCEDFSVTGE SEKRGEIIGK GLSGERAVEE EEEETANVEM 950
    SEKLCSQYGT PVFSAPGHAL HPGEPALGEA EERCLSPDDS TVKMASPPPS 1000
    GPPSATHTPF HQSPVEEKSE PQDFQEADSW GDTKRTPGVG KEDAAEETVK 1050
    PGPEEGTLEK EEKVPPPRSP QAQEAPVNID EGLTGCTIQL LPAQDKAIVF 1100
    EIMEAGEPTG PILGAEALPG GLRTLPQEPG KPQKDEVLRY PDRSLSPEDA 1150
    ESLSVLSVPS PDTANQEPTP KSPCGLTEQY LHKDRWPEVS PEDTQSLSLS 1200
    EESPSKETSL DVSSKQLSPE SLGTLQFGEL NLGKEEMGHL MQAEDTSHHT 1250
    APMSVPEPHA ATASPPTDGT TRYSAQTDIT DDSLDRKSPA SSFSHSTPSG 1300
    NGKYLPGAIT SPDEHILTPD SSFSKSPESL PGPALEDIAI KWEDKVPGLK 1350
    DRTSEQKKEP EPKDEVLQQK DKTLEHKEVV EPKDTAIYQK DEALHVKNEA 1400
    VKQQDKALEQ KGRDLEQKDT ALEQKDKALE PKDKDLEEKD KALEQKDKIP 1450
    EEKDKALEQK DTALEQKDKA LEPKDKDLEQ KDRVLEQKEK IPEEKDKALD 1500
    QKVRSVEHKA PEDTVAEMKD RDLEQTDKAP EQKHQAQEQK DKVSEKKDQA 1550
    LEQKYWALGQ KDEALEQNIQ ALEENHQTQE QESLVQEDKT RKPKMLEEKS 1600
    PEKVKAMEEK LEALLEKTKA LGLEESLVQE GRAREQEEKY WRGQDVVQEW 1650
    QETSPTREEP AGEQKELAPA WEDTSPEQDN RYWRGREDVA LEQDTYWREL 1700
    SCERKVWFPH ELDGQGARPH YTEERESTFL DEGPDDEQEV PLREHATRSP 1750
    WASDFKDFQE SSPQKGLEVE RWLAESPVGL PPEEEDKLTR SPFEIISPPA 1800
    SPPEMVGQRV PSAPGQESPI PDPKLMPHMK NEPTTPSWLA DIPPWVPKDR 1850
    PLPPAPLSPA PGPPTPAPES HTPAPFSWGT AEYDSVVAAV QEGAAELEGG 1900
    PYSPLGKDYR KAEGEREEEG RAEAPDKSSH SSKVPEASKS HATTEPEQTE 1950
    PEQREPTPYP DERSFQYADI YEQMMLTGLG PACPTREPPL GAAGDWPPCL 2000
    STKEAAAGRN TSAEKELSSP ISPKSLQSDT PTFSYAALAG PTVPPRPEPG 2050
    PSMEPSLTPP AVPPRAPILS KGPSPPLNGN ILSCSPDRRS PSPKESGRSH 2100
    WDDSTSDSEL EKGAREQPEK EAQSPSPPHP IPMGSPTLWP ETEAHVSPPL 2150
    DSHLGPARPS LDFPASAFGF SSLQPAPPQL PSPAEPRSAP CGSLAFSGDR 2200
    ALALAPGPPT RTRHDEYLEV TKAPSLDSSL PQLPSPSSPG APLLSNLPRP 2250
    ASPALSEGSS SEATTPVISS VAERFSPSLE AAEQESGELD PGMEPAAHSL 2300
    WDLTPLSPAP PASLDLALAP APSLPGDMGD GILPCHLECS EAATEKPSPF 2350
    QVPSEDCAAN GPTETSPNPP GPAPAKAENE EAAACPAWER GAWPEGAERS 2400
    SRPDTLLSPE QPVCPAGGSG GPPSSASPEV EAGPQGCATE PRPHRGELSP 2450
    SFLNPPLPPS IDDRDLSTEE VRLVGRGGRR RVGGPGTTGG PCPVTDETPP 2500
    TSASDSGSSQ SDSDVPPETE ECPSITAEAA LDSDEDGDFL PVDKAGGVSG 2550
    THHPRPGHDP PPLPQPDPRP SPPRPDVCMA DPEGLSSESG RVERLREKEK 2600
    VQGRVGRRAP GKAKPASPAR RLDLRGKRSP TPGKGPADRA SRAPPRPRST 2650
    TSQVTPAEEK DGHSPMSKGL VNGLKAGPMA LSSKGSSGAP VYVDLAYIPN 2700
    HCSGKTADLD FFRRVRASYY VVSGNDPANG EPSRAVLDAL LEGKAQWGEN 2750
    LQVTLIPTHD TEVTREWYQQ THEQQQQLNV LVLASSSTVV MQDESFPACK 2800
    IEF 2803
    Length:2,803
    Mass (Da):305,485
    Last modified:November 30, 2010 - v6
    Checksum:i94733902420F1FFE
    GO
    Isoform 2 (identifier: P78559-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2752-2752: Q → QSV

    Show »
    Length:2,805
    Mass (Da):305,671
    Checksum:i28E9817E8116EF8A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti134 – 1352VV → IP in CAA87104. 1 PublicationCurated
    Sequence conflicti249 – 2491A → G in CAA87104. 1 PublicationCurated
    Sequence conflicti263 – 2631V → A in CAA87104. 1 PublicationCurated
    Sequence conflicti296 – 2961Q → H in AAD00355. 1 PublicationCurated
    Sequence conflicti311 – 3111S → G in CAA87104. 1 PublicationCurated
    Sequence conflicti324 – 3241K → Q in AAD00355. 1 PublicationCurated
    Sequence conflicti414 – 4196EKKDKE → KKKRNS in CAA87104. 1 PublicationCurated
    Sequence conflicti424 – 4241K → P in AAB41132. (PubMed:8812494)Curated
    Sequence conflicti424 – 4241K → P in AAB41133. (PubMed:8812494)Curated
    Sequence conflicti426 – 4261E → D in AAD00355. 1 PublicationCurated
    Sequence conflicti431 – 4311K → Q in AAD00355. 1 PublicationCurated
    Sequence conflicti439 – 4391E → D in AAD00355. 1 PublicationCurated
    Sequence conflicti444 – 4441K → R in AAD00355. 1 PublicationCurated
    Sequence conflicti452 – 4532TK → SS in AAD00355. 1 PublicationCurated
    Sequence conflicti457 – 4571K → R in AAD00355. 1 PublicationCurated
    Sequence conflicti682 – 6821Q → P in AAB41132. (PubMed:8812494)Curated
    Sequence conflicti682 – 6821Q → P in AAB41133. (PubMed:8812494)Curated
    Sequence conflicti1025 – 10251Q → K in AAB41132. (PubMed:8812494)Curated
    Sequence conflicti1025 – 10251Q → K in AAB41133. (PubMed:8812494)Curated
    Sequence conflicti1303 – 131311KYLPGAITSPD → EVLTWGDHQALN in AAD00355. 1 PublicationCuratedAdd
    BLAST
    Sequence conflicti1335 – 13417Missing in AAD00355. 1 PublicationCurated
    Sequence conflicti1368 – 13681Q → T in AAD00355. 1 PublicationCurated
    Sequence conflicti1470 – 14701A → T in AAD00355. 1 PublicationCurated
    Sequence conflicti1714 – 17141G → V in AAB41132. (PubMed:8812494)Curated
    Sequence conflicti1714 – 17141G → V in AAB41133. (PubMed:8812494)Curated
    Sequence conflicti1869 – 18691E → A in AAA81362. (PubMed:7629894)Curated
    Sequence conflicti1879 – 18835GTAEY → AHSRV in AAA81362. (PubMed:7629894)Curated
    Sequence conflicti2118 – 21181P → A in AAB41132. (PubMed:8812494)Curated
    Sequence conflicti2118 – 21181P → A in AAB41133. (PubMed:8812494)Curated
    Sequence conflicti2174 – 21741Q → E in AAB41132. (PubMed:8812494)Curated
    Sequence conflicti2174 – 21741Q → E in AAB41133. (PubMed:8812494)Curated
    Sequence conflicti2613 – 26131A → D in AAB41132. (PubMed:8812494)Curated
    Sequence conflicti2613 – 26131A → D in AAB41133. (PubMed:8812494)Curated
    Sequence conflicti2616 – 26161A → V in AAB41132. (PubMed:8812494)Curated
    Sequence conflicti2616 – 26161A → V in AAB41133. (PubMed:8812494)Curated
    Sequence conflicti2636 – 26361P → S in AAB41132. (PubMed:8812494)Curated
    Sequence conflicti2636 – 26361P → S in AAB41133. (PubMed:8812494)Curated
    Sequence conflicti2640 – 26401A → V in AAB41132. (PubMed:8812494)Curated
    Sequence conflicti2640 – 26401A → V in AAB41133. (PubMed:8812494)Curated
    Sequence conflicti2647 – 26471P → S in AAB41132. (PubMed:8812494)Curated
    Sequence conflicti2647 – 26471P → S in AAB41133. (PubMed:8812494)Curated
    Sequence conflicti2702 – 27021C → W in AAB41132. (PubMed:8812494)Curated
    Sequence conflicti2702 – 27021C → W in AAB41133. (PubMed:8812494)Curated
    Isoform 2 (identifier: P78559-2)
    Sequence conflicti2753 – 27531S → V in AAB41132. (PubMed:8812494)Curated
    Sequence conflicti2753 – 27531S → V in AAB41133. (PubMed:8812494)Curated
    Sequence conflicti2754 – 27541V → K in AAB41132. (PubMed:8812494)Curated
    Sequence conflicti2754 – 27541V → K in AAB41133. (PubMed:8812494)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti72 – 721F → L.1 Publication
    Corresponds to variant rs2584695 [ dbSNP | Ensembl ].
    VAR_039705
    Natural varianti335 – 3351A → S.1 Publication
    Corresponds to variant rs1060935 [ dbSNP | Ensembl ].
    VAR_039706
    Natural varianti336 – 3361K → T.1 Publication
    Corresponds to variant rs1060936 [ dbSNP | Ensembl ].
    VAR_039707
    Natural varianti353 – 3531A → S.1 Publication
    Corresponds to variant rs1060937 [ dbSNP | Ensembl ].
    VAR_039708
    Natural varianti357 – 3571A → S.1 Publication
    Corresponds to variant rs1060938 [ dbSNP | Ensembl ].
    VAR_039709
    Natural varianti364 – 3641K → Q.1 Publication
    Corresponds to variant rs2602129 [ dbSNP | Ensembl ].
    VAR_039710
    Natural varianti485 – 4851K → Q.
    Corresponds to variant rs2584715 [ dbSNP | Ensembl ].
    VAR_039711
    Natural varianti830 – 8301T → A.
    Corresponds to variant rs3803337 [ dbSNP | Ensembl ].
    VAR_039712
    Natural varianti1078 – 10781N → S.
    Corresponds to variant rs8034794 [ dbSNP | Ensembl ].
    VAR_039713
    Natural varianti1102 – 11021I → T.
    Corresponds to variant rs8036179 [ dbSNP | Ensembl ].
    VAR_039714
    Natural varianti1185 – 11851R → H.
    Corresponds to variant rs3803335 [ dbSNP | Ensembl ].
    VAR_039715
    Natural varianti1245 – 12451D → N.
    Corresponds to variant rs12912505 [ dbSNP | Ensembl ].
    VAR_039716
    Natural varianti1461 – 14611D → N.
    Corresponds to variant rs2245715 [ dbSNP | Ensembl ].
    VAR_039717
    Natural varianti1553 – 15531Q → H.
    Corresponds to variant rs2584717 [ dbSNP | Ensembl ].
    VAR_039718
    Natural varianti1605 – 16051K → N.
    Corresponds to variant rs2584697 [ dbSNP | Ensembl ].
    VAR_039719
    Natural varianti1650 – 16501W → C.1 Publication
    Corresponds to variant rs1060943 [ dbSNP | Ensembl ].
    VAR_039720
    Natural varianti1690 – 16901A → S.1 Publication
    Corresponds to variant rs1060946 [ dbSNP | Ensembl ].
    VAR_039721
    Natural varianti1827 – 18271P → A.
    Corresponds to variant rs2229014 [ dbSNP | Ensembl ].
    VAR_039722
    Natural varianti1881 – 18811A → P.1 Publication
    Corresponds to variant rs1060950 [ dbSNP | Ensembl ].
    VAR_039723
    Natural varianti1912 – 19121A → V.1 Publication
    Corresponds to variant rs2584718 [ dbSNP | Ensembl ].
    VAR_039724
    Natural varianti1938 – 19381S → R.1 Publication
    Corresponds to variant rs2584719 [ dbSNP | Ensembl ].
    VAR_039725
    Natural varianti2056 – 20561S → R.
    Corresponds to variant rs1060953 [ dbSNP | Ensembl ].
    VAR_039726
    Natural varianti2214 – 22141H → Y.1 Publication
    Corresponds to variant rs1060955 [ dbSNP | Ensembl ].
    VAR_039727
    Natural varianti2327 – 23271D → V.
    Corresponds to variant rs8026745 [ dbSNP | Ensembl ].
    VAR_039728
    Natural varianti2405 – 24051T → I.
    Corresponds to variant rs8027254 [ dbSNP | Ensembl ].
    VAR_059432
    Natural varianti2461 – 24611I → T.
    Corresponds to variant rs8028849 [ dbSNP | Ensembl ].
    VAR_056122
    Natural varianti2465 – 24651D → N.
    Corresponds to variant rs8027916 [ dbSNP | Ensembl ].
    VAR_059433

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2752 – 27521Q → QSV in isoform 2. CuratedVSP_040240

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38291 Genomic DNA. Translation: AAB41132.1.
    U38292 mRNA. Translation: AAB41133.1.
    AC019011 Genomic DNA. No translation available.
    AF200415 mRNA. Translation: AAF08305.2.
    U80458 mRNA. Translation: AAD00355.1.
    Z47038 Genomic DNA. Translation: CAA87104.1.
    U14577 mRNA. Translation: AAA81362.1.
    CCDSiCCDS42031.1. [P78559-1]
    PIRiI38857.
    RefSeqiNP_002364.5. NM_002373.5. [P78559-1]
    UniGeneiHs.194301.
    Hs.619338.

    Genome annotation databases

    EnsembliENST00000300231; ENSP00000300231; ENSG00000166963. [P78559-1]
    GeneIDi4130.
    KEGGihsa:4130.
    UCSCiuc001zrt.3. human. [P78559-1]

    Polymorphism databases

    DMDMi313104325.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38291 Genomic DNA. Translation: AAB41132.1 .
    U38292 mRNA. Translation: AAB41133.1 .
    AC019011 Genomic DNA. No translation available.
    AF200415 mRNA. Translation: AAF08305.2 .
    U80458 mRNA. Translation: AAD00355.1 .
    Z47038 Genomic DNA. Translation: CAA87104.1 .
    U14577 mRNA. Translation: AAA81362.1 .
    CCDSi CCDS42031.1. [P78559-1 ]
    PIRi I38857.
    RefSeqi NP_002364.5. NM_002373.5. [P78559-1 ]
    UniGenei Hs.194301.
    Hs.619338.

    3D structure databases

    ProteinModelPortali P78559.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110303. 19 interactions.
    IntActi P78559. 10 interactions.
    MINTi MINT-1203375.
    STRINGi 9606.ENSP00000300231.

    Chemistry

    DrugBanki DB01196. Estramustine.

    PTM databases

    PhosphoSitei P78559.

    Polymorphism databases

    DMDMi 313104325.

    Proteomic databases

    MaxQBi P78559.
    PaxDbi P78559.
    PRIDEi P78559.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300231 ; ENSP00000300231 ; ENSG00000166963 . [P78559-1 ]
    GeneIDi 4130.
    KEGGi hsa:4130.
    UCSCi uc001zrt.3. human. [P78559-1 ]

    Organism-specific databases

    CTDi 4130.
    GeneCardsi GC15P043803.
    HGNCi HGNC:6835. MAP1A.
    HPAi HPA039063.
    HPA039064.
    MIMi 600178. gene.
    neXtProti NX_P78559.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000231839.
    HOVERGENi HBG052408.
    KOi K10429.
    PhylomeDBi P78559.
    TreeFami TF350229.

    Miscellaneous databases

    ChiTaRSi MAP1A. human.
    GeneWikii MAP1A.
    GenomeRNAii 4130.
    NextBioi 16214.
    PROi P78559.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P78559.
    Bgeei P78559.
    CleanExi HS_MAP1A.
    Genevestigatori P78559.

    Family and domain databases

    Gene3Di 3.60.15.10. 2 hits.
    InterProi IPR001279. Beta-lactamas-like.
    IPR026074. MAP1.
    IPR015656. MAP1A.
    [Graphical view ]
    PANTHERi PTHR13843. PTHR13843. 1 hit.
    PTHR13843:SF6. PTHR13843:SF6. 1 hit.
    SUPFAMi SSF56281. SSF56281. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Human microtubule-associated protein 1a (MAP1A) gene: genomic organization, cDNA sequence, and developmental- and tissue-specific expression."
      Fink J.K., Jones S.M., Esposito C., Wilkowski J.
      Genomics 35:577-585(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS LEU-72; SER-335; THR-336; SER-353; SER-357; GLN-364; CYS-1650; SER-1690; PRO-1881; VAL-1912; ARG-1938 AND TYR-2214.
    2. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Identification of a novel protein (P80) in ovarian carcinoma cells."
      Chen Z.C., Fadiel A., Naftolin F.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1825.
      Tissue: Ovarian carcinoma.
    4. "Microtubule associated protein 1A (MAP1A) in human brain -- DNA sequence and physiological role."
      Ohtani K., Rutherford T., Sakamoto H., Naftolin F.
      Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 78-1687.
      Tissue: Brain.
    5. Chiannilkulchai N., Pasturaud P., Richard I., Auffray C., Beckmann J.S.
      Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-419.
      Tissue: Fetal muscle.
    6. "Brain-specific expression of human microtubule-associated protein 1A (MAP1A) gene and its assignment to human chromosome 15."
      Fukuyama R., Rapoport S.I.
      J. Neurosci. Res. 40:820-825(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1607-1883.
      Tissue: Brain.
    7. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2022, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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-612; THR-616; SER-1326; SER-1329 AND SER-2022, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    11. "MAP1 structural organization in Drosophila: in vivo analysis of FUTSCH reveals heavy- and light-chain subunits generated by proteolytic processing at a conserved cleavage site."
      Zou B., Yan H., Kawasaki F., Ordway R.W.
      Biochem. J. 414:63-71(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE SITE.
    12. "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].
    13. "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-612; THR-616; SER-667; SER-896; THR-1008; SER-1013; SER-1069; SER-1160; SER-1218; SER-1654; SER-1675; SER-1776; SER-1791; SER-1797; SER-1801; SER-2022; SER-2104 AND SER-2449, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-612 AND THR-616, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMAP1A_HUMAN
    AccessioniPrimary (citable) accession number: P78559
    Secondary accession number(s): O95643
    , Q12973, Q15882, Q9UJT4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 127 of the entry and version 6 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 15
      Human chromosome 15: 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