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P78559

- MAP1A_HUMAN

UniProt

P78559 - MAP1A_HUMAN

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Protein

Microtubule-associated protein 1A

Gene

MAP1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. structural molecule activity Source: ProtInc

GO - Biological processi

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

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
Complete GO annotation...

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

BgeeiP78559.
CleanExiHS_MAP1A.
ExpressionAtlasiP78559. baseline and differential.
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.
GeneTreeiENSGT00550000074593.
HOGENOMiHOG000231839.
HOVERGENiHBG052408.
InParanoidiP78559.
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

        10         20         30         40         50
MDGVAEFSEY VSETVDVPSP FDLLEPPTSG GFLKLSKPCC YIFPGGRGDS
60 70 80 90 100
ALFAVNGFNI LVDGGSDRKS CFWKLVRHLD RIDSVLLTHI GADNLPGING
110 120 130 140 150
LLQRKVAELE EEQSQGSSSY SDWVKNLISP ELGVVFFNVP EKLRLPDASR
160 170 180 190 200
KAKRSIEEAC LTLQHLNRLG IQAEPLYRVV SNTIEPLTLF HKMGVGRLDM
210 220 230 240 250
YVLNPVKDSK EMQFLMQKWA GNSKAKTGIV LPNGKEAEIS VPYLTSITAL
260 270 280 290 300
VVWLPANPTE KIVRVLFPGN APQNKILEGL EKLRHLDFLR YPVATQKDLA
310 320 330 340 350
SGAVPTNLKP SKIKQRADSK ESLKATTKTA VSKLAKREEV VEEGAKEARS
360 370 380 390 400
ELAKELAKTE KKAKESSEKP PEKPAKPERV KTESSEALKA EKRKLIKDKV
410 420 430 440 450
GKKHLKEKIS KLEEKKDKEK KEIKKERKEL KKDEGRKEEK KDAKKEEKRK
460 470 480 490 500
DTKPELKKIS KPDLKPFTPE VRKTLYKAKV PGRVKIDRSR AIRGEKELSS
510 520 530 540 550
EPQTPPAQKG TVPLPTISGH RELVLSSPED LTQDFEEMKR EERALLAEQR
560 570 580 590 600
DTGLGDKPFP LDTAEEGPPS TAIQGTPPSV PGLGQEEHVM KEKELVPEVP
610 620 630 640 650
EEQGSKDRGL DSGAETEEEK DTWEEKKQRE AERLPDRTEA REESEPEVKE
660 670 680 690 700
DVIEKAELEE MEEVHPSDEE EEDATKAEGF YQKHMQEPLK VTPRSREAFG
710 720 730 740 750
GRELGLQGKA PEKETSLFLS SLTTPAGATE HVSYIQDETI PGYSETEQTI
760 770 780 790 800
SDEEIHDEPE ERPAPPRFHT STYDLPGPEG AGPFEASQPA DSAVPATSGK
810 820 830 840 850
VYGTPETELT YPTNIVAAPL AEEEHVSSAT SITECDKLSS FATSVAEDQS
860 870 880 890 900
VASLTAPQTE ETGKSSLLLD TVTSIPSSRT EATQGLDYVP SAGTISPTSS
910 920 930 940 950
LEEDKGFKSP PCEDFSVTGE SEKRGEIIGK GLSGERAVEE EEEETANVEM
960 970 980 990 1000
SEKLCSQYGT PVFSAPGHAL HPGEPALGEA EERCLSPDDS TVKMASPPPS
1010 1020 1030 1040 1050
GPPSATHTPF HQSPVEEKSE PQDFQEADSW GDTKRTPGVG KEDAAEETVK
1060 1070 1080 1090 1100
PGPEEGTLEK EEKVPPPRSP QAQEAPVNID EGLTGCTIQL LPAQDKAIVF
1110 1120 1130 1140 1150
EIMEAGEPTG PILGAEALPG GLRTLPQEPG KPQKDEVLRY PDRSLSPEDA
1160 1170 1180 1190 1200
ESLSVLSVPS PDTANQEPTP KSPCGLTEQY LHKDRWPEVS PEDTQSLSLS
1210 1220 1230 1240 1250
EESPSKETSL DVSSKQLSPE SLGTLQFGEL NLGKEEMGHL MQAEDTSHHT
1260 1270 1280 1290 1300
APMSVPEPHA ATASPPTDGT TRYSAQTDIT DDSLDRKSPA SSFSHSTPSG
1310 1320 1330 1340 1350
NGKYLPGAIT SPDEHILTPD SSFSKSPESL PGPALEDIAI KWEDKVPGLK
1360 1370 1380 1390 1400
DRTSEQKKEP EPKDEVLQQK DKTLEHKEVV EPKDTAIYQK DEALHVKNEA
1410 1420 1430 1440 1450
VKQQDKALEQ KGRDLEQKDT ALEQKDKALE PKDKDLEEKD KALEQKDKIP
1460 1470 1480 1490 1500
EEKDKALEQK DTALEQKDKA LEPKDKDLEQ KDRVLEQKEK IPEEKDKALD
1510 1520 1530 1540 1550
QKVRSVEHKA PEDTVAEMKD RDLEQTDKAP EQKHQAQEQK DKVSEKKDQA
1560 1570 1580 1590 1600
LEQKYWALGQ KDEALEQNIQ ALEENHQTQE QESLVQEDKT RKPKMLEEKS
1610 1620 1630 1640 1650
PEKVKAMEEK LEALLEKTKA LGLEESLVQE GRAREQEEKY WRGQDVVQEW
1660 1670 1680 1690 1700
QETSPTREEP AGEQKELAPA WEDTSPEQDN RYWRGREDVA LEQDTYWREL
1710 1720 1730 1740 1750
SCERKVWFPH ELDGQGARPH YTEERESTFL DEGPDDEQEV PLREHATRSP
1760 1770 1780 1790 1800
WASDFKDFQE SSPQKGLEVE RWLAESPVGL PPEEEDKLTR SPFEIISPPA
1810 1820 1830 1840 1850
SPPEMVGQRV PSAPGQESPI PDPKLMPHMK NEPTTPSWLA DIPPWVPKDR
1860 1870 1880 1890 1900
PLPPAPLSPA PGPPTPAPES HTPAPFSWGT AEYDSVVAAV QEGAAELEGG
1910 1920 1930 1940 1950
PYSPLGKDYR KAEGEREEEG RAEAPDKSSH SSKVPEASKS HATTEPEQTE
1960 1970 1980 1990 2000
PEQREPTPYP DERSFQYADI YEQMMLTGLG PACPTREPPL GAAGDWPPCL
2010 2020 2030 2040 2050
STKEAAAGRN TSAEKELSSP ISPKSLQSDT PTFSYAALAG PTVPPRPEPG
2060 2070 2080 2090 2100
PSMEPSLTPP AVPPRAPILS KGPSPPLNGN ILSCSPDRRS PSPKESGRSH
2110 2120 2130 2140 2150
WDDSTSDSEL EKGAREQPEK EAQSPSPPHP IPMGSPTLWP ETEAHVSPPL
2160 2170 2180 2190 2200
DSHLGPARPS LDFPASAFGF SSLQPAPPQL PSPAEPRSAP CGSLAFSGDR
2210 2220 2230 2240 2250
ALALAPGPPT RTRHDEYLEV TKAPSLDSSL PQLPSPSSPG APLLSNLPRP
2260 2270 2280 2290 2300
ASPALSEGSS SEATTPVISS VAERFSPSLE AAEQESGELD PGMEPAAHSL
2310 2320 2330 2340 2350
WDLTPLSPAP PASLDLALAP APSLPGDMGD GILPCHLECS EAATEKPSPF
2360 2370 2380 2390 2400
QVPSEDCAAN GPTETSPNPP GPAPAKAENE EAAACPAWER GAWPEGAERS
2410 2420 2430 2440 2450
SRPDTLLSPE QPVCPAGGSG GPPSSASPEV EAGPQGCATE PRPHRGELSP
2460 2470 2480 2490 2500
SFLNPPLPPS IDDRDLSTEE VRLVGRGGRR RVGGPGTTGG PCPVTDETPP
2510 2520 2530 2540 2550
TSASDSGSSQ SDSDVPPETE ECPSITAEAA LDSDEDGDFL PVDKAGGVSG
2560 2570 2580 2590 2600
THHPRPGHDP PPLPQPDPRP SPPRPDVCMA DPEGLSSESG RVERLREKEK
2610 2620 2630 2640 2650
VQGRVGRRAP GKAKPASPAR RLDLRGKRSP TPGKGPADRA SRAPPRPRST
2660 2670 2680 2690 2700
TSQVTPAEEK DGHSPMSKGL VNGLKAGPMA LSSKGSSGAP VYVDLAYIPN
2710 2720 2730 2740 2750
HCSGKTADLD FFRRVRASYY VVSGNDPANG EPSRAVLDAL LEGKAQWGEN
2760 2770 2780 2790 2800
LQVTLIPTHD TEVTREWYQQ THEQQQQLNV LVLASSSTVV MQDESFPACK

IEF
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.
GeneTreei ENSGT00550000074593.
HOGENOMi HOG000231839.
HOVERGENi HBG052408.
InParanoidi P78559.
KOi K10429.
PhylomeDBi P78559.
TreeFami TF350229.

Miscellaneous databases

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

Gene expression databases

Bgeei P78559.
CleanExi HS_MAP1A.
ExpressionAtlasi P78559. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 128 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