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P78559 (MAP1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microtubule-associated protein 1A

Short name=MAP-1A
Alternative name(s):
Proliferation-related protein p80

Cleaved into the following 2 chains:

  1. MAP1A heavy chain
  2. MAP1 light chain LC2
Gene names
Name:MAP1A
Synonyms:MAP1L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2803 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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.

Subcellular location

Cytoplasmcytoskeleton Probable.

Tissue specificity

Brain.

Domain

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

Post-translational modification

Phosphorylated by CSNK1D By similarity.

LC2 is generated from MAP1A by proteolytic processing.

Sequence similarities

Belongs to the MAP1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DISC1Q9NRI53EBI-929047,EBI-529989

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P78559-1)

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.
Isoform 2 (identifier: P78559-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 28032803Microtubule-associated protein 1A
PRO_0000018600
Chain1 – 25662566MAP1A heavy chain
PRO_0000418376
Chain2567 – 2803237MAP1 light chain LC2
PRO_0000018601

Regions

Repeat415 – 41731
Repeat420 – 42232
Repeat427 – 42933
Repeat431 – 43334
Repeat436 – 43835
Repeat440 – 44236
Repeat444 – 44637
Repeat449 – 45138
Repeat539 – 54139
Region415 – 5411279 X 3 AA repeats of K-K-[DE]
Compositional bias309 – 496188Lys-rich (basic)

Amino acid modifications

Modified residue1771Phosphotyrosine By similarity
Modified residue5261Phosphoserine By similarity
Modified residue5271Phosphoserine By similarity
Modified residue6121Phosphoserine Ref.9 Ref.13 Ref.16
Modified residue6161Phosphothreonine Ref.9 Ref.13 Ref.16
Modified residue6441Phosphoserine By similarity
Modified residue6671Phosphoserine Ref.13
Modified residue8961Phosphoserine Ref.13
Modified residue9861Phosphoserine By similarity
Modified residue10081Phosphothreonine Ref.13
Modified residue10131Phosphoserine Ref.13
Modified residue10691Phosphoserine Ref.13
Modified residue11601Phosphoserine Ref.13
Modified residue12181Phosphoserine Ref.13
Modified residue13261Phosphoserine Ref.9
Modified residue13291Phosphoserine Ref.9
Modified residue16541Phosphoserine Ref.13
Modified residue16751Phosphoserine Ref.13
Modified residue17761Phosphoserine Ref.13
Modified residue17911Phosphoserine Ref.13
Modified residue17971Phosphoserine Ref.13
Modified residue18011Phosphoserine Ref.13
Modified residue20221Phosphoserine Ref.7 Ref.9 Ref.13
Modified residue21041Phosphoserine Ref.13
Modified residue24491Phosphoserine Ref.13

Natural variations

Alternative sequence27521Q → QSV in isoform 2.
VSP_040240
Natural variant721F → L. Ref.1
Corresponds to variant rs2584695 [ dbSNP | Ensembl ].
VAR_039705
Natural variant3351A → S. Ref.1
Corresponds to variant rs1060935 [ dbSNP | Ensembl ].
VAR_039706
Natural variant3361K → T. Ref.1
Corresponds to variant rs1060936 [ dbSNP | Ensembl ].
VAR_039707
Natural variant3531A → S. Ref.1
Corresponds to variant rs1060937 [ dbSNP | Ensembl ].
VAR_039708
Natural variant3571A → S. Ref.1
Corresponds to variant rs1060938 [ dbSNP | Ensembl ].
VAR_039709
Natural variant3641K → Q. Ref.1
Corresponds to variant rs2602129 [ dbSNP | Ensembl ].
VAR_039710
Natural variant4851K → Q.
Corresponds to variant rs2584715 [ dbSNP | Ensembl ].
VAR_039711
Natural variant8301T → A.
Corresponds to variant rs3803337 [ dbSNP | Ensembl ].
VAR_039712
Natural variant10781N → S.
Corresponds to variant rs8034794 [ dbSNP | Ensembl ].
VAR_039713
Natural variant11021I → T.
Corresponds to variant rs8036179 [ dbSNP | Ensembl ].
VAR_039714
Natural variant11851R → H.
Corresponds to variant rs3803335 [ dbSNP | Ensembl ].
VAR_039715
Natural variant12451D → N.
Corresponds to variant rs12912505 [ dbSNP | Ensembl ].
VAR_039716
Natural variant14611D → N.
Corresponds to variant rs2245715 [ dbSNP | Ensembl ].
VAR_039717
Natural variant15531Q → H.
Corresponds to variant rs2584717 [ dbSNP | Ensembl ].
VAR_039718
Natural variant16051K → N.
Corresponds to variant rs2584697 [ dbSNP | Ensembl ].
VAR_039719
Natural variant16501W → C. Ref.1
Corresponds to variant rs1060943 [ dbSNP | Ensembl ].
VAR_039720
Natural variant16901A → S. Ref.1
Corresponds to variant rs1060946 [ dbSNP | Ensembl ].
VAR_039721
Natural variant18271P → A.
Corresponds to variant rs2229014 [ dbSNP | Ensembl ].
VAR_039722
Natural variant18811A → P. Ref.1
Corresponds to variant rs1060950 [ dbSNP | Ensembl ].
VAR_039723
Natural variant19121A → V. Ref.1
Corresponds to variant rs2584718 [ dbSNP | Ensembl ].
VAR_039724
Natural variant19381S → R. Ref.1
Corresponds to variant rs2584719 [ dbSNP | Ensembl ].
VAR_039725
Natural variant20561S → R.
Corresponds to variant rs1060953 [ dbSNP | Ensembl ].
VAR_039726
Natural variant22141H → Y. Ref.1
Corresponds to variant rs1060955 [ dbSNP | Ensembl ].
VAR_039727
Natural variant23271D → V.
Corresponds to variant rs8026745 [ dbSNP | Ensembl ].
VAR_039728
Natural variant24051T → I.
Corresponds to variant rs8027254 [ dbSNP | Ensembl ].
VAR_059432
Natural variant24611I → T.
Corresponds to variant rs8028849 [ dbSNP | Ensembl ].
VAR_056122
Natural variant24651D → N.
Corresponds to variant rs8027916 [ dbSNP | Ensembl ].
VAR_059433

Experimental info

Sequence conflict134 – 1352VV → IP in CAA87104. Ref.5
Sequence conflict2491A → G in CAA87104. Ref.5
Sequence conflict2631V → A in CAA87104. Ref.5
Sequence conflict2961Q → H in AAD00355. Ref.4
Sequence conflict3111S → G in CAA87104. Ref.5
Sequence conflict3241K → Q in AAD00355. Ref.4
Sequence conflict414 – 4196EKKDKE → KKKRNS in CAA87104. Ref.5
Sequence conflict4241K → P in AAB41132. Ref.1
Sequence conflict4241K → P in AAB41133. Ref.1
Sequence conflict4261E → D in AAD00355. Ref.4
Sequence conflict4311K → Q in AAD00355. Ref.4
Sequence conflict4391E → D in AAD00355. Ref.4
Sequence conflict4441K → R in AAD00355. Ref.4
Sequence conflict452 – 4532TK → SS in AAD00355. Ref.4
Sequence conflict4571K → R in AAD00355. Ref.4
Sequence conflict6821Q → P in AAB41132. Ref.1
Sequence conflict6821Q → P in AAB41133. Ref.1
Sequence conflict10251Q → K in AAB41132. Ref.1
Sequence conflict10251Q → K in AAB41133. Ref.1
Sequence conflict1303 – 131311KYLPGAITSPD → EVLTWGDHQALN in AAD00355. Ref.4
Sequence conflict1335 – 13417Missing in AAD00355. Ref.4
Sequence conflict13681Q → T in AAD00355. Ref.4
Sequence conflict14701A → T in AAD00355. Ref.4
Sequence conflict17141G → V in AAB41132. Ref.1
Sequence conflict17141G → V in AAB41133. Ref.1
Sequence conflict18691E → A in AAA81362. Ref.6
Sequence conflict1879 – 18835GTAEY → AHSRV in AAA81362. Ref.6
Sequence conflict21181P → A in AAB41132. Ref.1
Sequence conflict21181P → A in AAB41133. Ref.1
Sequence conflict21741Q → E in AAB41132. Ref.1
Sequence conflict21741Q → E in AAB41133. Ref.1
Sequence conflict26131A → D in AAB41132. Ref.1
Sequence conflict26131A → D in AAB41133. Ref.1
Sequence conflict26161A → V in AAB41132. Ref.1
Sequence conflict26161A → V in AAB41133. Ref.1
Sequence conflict26361P → S in AAB41132. Ref.1
Sequence conflict26361P → S in AAB41133. Ref.1
Sequence conflict26401A → V in AAB41132. Ref.1
Sequence conflict26401A → V in AAB41133. Ref.1
Sequence conflict26471P → S in AAB41132. Ref.1
Sequence conflict26471P → S in AAB41133. Ref.1
Sequence conflict27021C → W in AAB41132. Ref.1
Sequence conflict27021C → W in AAB41133. Ref.1
Isoform 2:
Sequence conflict27531S → V in AAB41132. Ref.1
Sequence conflict27531S → V in AAB41133. Ref.1
Sequence conflict27541V → K in AAB41132. Ref.1
Sequence conflict27541V → K in AAB41133. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 30, 2010. Version 6.
Checksum: 94733902420F1FFE

FASTA2,803305,485
        10         20         30         40         50         60 
MDGVAEFSEY VSETVDVPSP FDLLEPPTSG GFLKLSKPCC YIFPGGRGDS ALFAVNGFNI 

        70         80         90        100        110        120 
LVDGGSDRKS CFWKLVRHLD RIDSVLLTHI GADNLPGING LLQRKVAELE EEQSQGSSSY 

       130        140        150        160        170        180 
SDWVKNLISP ELGVVFFNVP EKLRLPDASR KAKRSIEEAC LTLQHLNRLG IQAEPLYRVV 

       190        200        210        220        230        240 
SNTIEPLTLF HKMGVGRLDM YVLNPVKDSK EMQFLMQKWA GNSKAKTGIV LPNGKEAEIS 

       250        260        270        280        290        300 
VPYLTSITAL VVWLPANPTE KIVRVLFPGN APQNKILEGL EKLRHLDFLR YPVATQKDLA 

       310        320        330        340        350        360 
SGAVPTNLKP SKIKQRADSK ESLKATTKTA VSKLAKREEV VEEGAKEARS ELAKELAKTE 

       370        380        390        400        410        420 
KKAKESSEKP PEKPAKPERV KTESSEALKA EKRKLIKDKV GKKHLKEKIS KLEEKKDKEK 

       430        440        450        460        470        480 
KEIKKERKEL KKDEGRKEEK KDAKKEEKRK DTKPELKKIS KPDLKPFTPE VRKTLYKAKV 

       490        500        510        520        530        540 
PGRVKIDRSR AIRGEKELSS EPQTPPAQKG TVPLPTISGH RELVLSSPED LTQDFEEMKR 

       550        560        570        580        590        600 
EERALLAEQR DTGLGDKPFP LDTAEEGPPS TAIQGTPPSV PGLGQEEHVM KEKELVPEVP 

       610        620        630        640        650        660 
EEQGSKDRGL DSGAETEEEK DTWEEKKQRE AERLPDRTEA REESEPEVKE DVIEKAELEE 

       670        680        690        700        710        720 
MEEVHPSDEE EEDATKAEGF YQKHMQEPLK VTPRSREAFG GRELGLQGKA PEKETSLFLS 

       730        740        750        760        770        780 
SLTTPAGATE HVSYIQDETI PGYSETEQTI SDEEIHDEPE ERPAPPRFHT STYDLPGPEG 

       790        800        810        820        830        840 
AGPFEASQPA DSAVPATSGK VYGTPETELT YPTNIVAAPL AEEEHVSSAT SITECDKLSS 

       850        860        870        880        890        900 
FATSVAEDQS VASLTAPQTE ETGKSSLLLD TVTSIPSSRT EATQGLDYVP SAGTISPTSS 

       910        920        930        940        950        960 
LEEDKGFKSP PCEDFSVTGE SEKRGEIIGK GLSGERAVEE EEEETANVEM SEKLCSQYGT 

       970        980        990       1000       1010       1020 
PVFSAPGHAL HPGEPALGEA EERCLSPDDS TVKMASPPPS GPPSATHTPF HQSPVEEKSE 

      1030       1040       1050       1060       1070       1080 
PQDFQEADSW GDTKRTPGVG KEDAAEETVK PGPEEGTLEK EEKVPPPRSP QAQEAPVNID 

      1090       1100       1110       1120       1130       1140 
EGLTGCTIQL LPAQDKAIVF EIMEAGEPTG PILGAEALPG GLRTLPQEPG KPQKDEVLRY 

      1150       1160       1170       1180       1190       1200 
PDRSLSPEDA ESLSVLSVPS PDTANQEPTP KSPCGLTEQY LHKDRWPEVS PEDTQSLSLS 

      1210       1220       1230       1240       1250       1260 
EESPSKETSL DVSSKQLSPE SLGTLQFGEL NLGKEEMGHL MQAEDTSHHT APMSVPEPHA 

      1270       1280       1290       1300       1310       1320 
ATASPPTDGT TRYSAQTDIT DDSLDRKSPA SSFSHSTPSG NGKYLPGAIT SPDEHILTPD 

      1330       1340       1350       1360       1370       1380 
SSFSKSPESL PGPALEDIAI KWEDKVPGLK DRTSEQKKEP EPKDEVLQQK DKTLEHKEVV 

      1390       1400       1410       1420       1430       1440 
EPKDTAIYQK DEALHVKNEA VKQQDKALEQ KGRDLEQKDT ALEQKDKALE PKDKDLEEKD 

      1450       1460       1470       1480       1490       1500 
KALEQKDKIP EEKDKALEQK DTALEQKDKA LEPKDKDLEQ KDRVLEQKEK IPEEKDKALD 

      1510       1520       1530       1540       1550       1560 
QKVRSVEHKA PEDTVAEMKD RDLEQTDKAP EQKHQAQEQK DKVSEKKDQA LEQKYWALGQ 

      1570       1580       1590       1600       1610       1620 
KDEALEQNIQ ALEENHQTQE QESLVQEDKT RKPKMLEEKS PEKVKAMEEK LEALLEKTKA 

      1630       1640       1650       1660       1670       1680 
LGLEESLVQE GRAREQEEKY WRGQDVVQEW QETSPTREEP AGEQKELAPA WEDTSPEQDN 

      1690       1700       1710       1720       1730       1740 
RYWRGREDVA LEQDTYWREL SCERKVWFPH ELDGQGARPH YTEERESTFL DEGPDDEQEV 

      1750       1760       1770       1780       1790       1800 
PLREHATRSP WASDFKDFQE SSPQKGLEVE RWLAESPVGL PPEEEDKLTR SPFEIISPPA 

      1810       1820       1830       1840       1850       1860 
SPPEMVGQRV PSAPGQESPI PDPKLMPHMK NEPTTPSWLA DIPPWVPKDR PLPPAPLSPA 

      1870       1880       1890       1900       1910       1920 
PGPPTPAPES HTPAPFSWGT AEYDSVVAAV QEGAAELEGG PYSPLGKDYR KAEGEREEEG 

      1930       1940       1950       1960       1970       1980 
RAEAPDKSSH SSKVPEASKS HATTEPEQTE PEQREPTPYP DERSFQYADI YEQMMLTGLG 

      1990       2000       2010       2020       2030       2040 
PACPTREPPL GAAGDWPPCL STKEAAAGRN TSAEKELSSP ISPKSLQSDT PTFSYAALAG 

      2050       2060       2070       2080       2090       2100 
PTVPPRPEPG PSMEPSLTPP AVPPRAPILS KGPSPPLNGN ILSCSPDRRS PSPKESGRSH 

      2110       2120       2130       2140       2150       2160 
WDDSTSDSEL EKGAREQPEK EAQSPSPPHP IPMGSPTLWP ETEAHVSPPL DSHLGPARPS 

      2170       2180       2190       2200       2210       2220 
LDFPASAFGF SSLQPAPPQL PSPAEPRSAP CGSLAFSGDR ALALAPGPPT RTRHDEYLEV 

      2230       2240       2250       2260       2270       2280 
TKAPSLDSSL PQLPSPSSPG APLLSNLPRP ASPALSEGSS SEATTPVISS VAERFSPSLE 

      2290       2300       2310       2320       2330       2340 
AAEQESGELD PGMEPAAHSL WDLTPLSPAP PASLDLALAP APSLPGDMGD GILPCHLECS 

      2350       2360       2370       2380       2390       2400 
EAATEKPSPF QVPSEDCAAN GPTETSPNPP GPAPAKAENE EAAACPAWER GAWPEGAERS 

      2410       2420       2430       2440       2450       2460 
SRPDTLLSPE QPVCPAGGSG GPPSSASPEV EAGPQGCATE PRPHRGELSP SFLNPPLPPS 

      2470       2480       2490       2500       2510       2520 
IDDRDLSTEE VRLVGRGGRR RVGGPGTTGG PCPVTDETPP TSASDSGSSQ SDSDVPPETE 

      2530       2540       2550       2560       2570       2580 
ECPSITAEAA LDSDEDGDFL PVDKAGGVSG THHPRPGHDP PPLPQPDPRP SPPRPDVCMA 

      2590       2600       2610       2620       2630       2640 
DPEGLSSESG RVERLREKEK VQGRVGRRAP GKAKPASPAR RLDLRGKRSP TPGKGPADRA 

      2650       2660       2670       2680       2690       2700 
SRAPPRPRST TSQVTPAEEK DGHSPMSKGL VNGLKAGPMA LSSKGSSGAP VYVDLAYIPN 

      2710       2720       2730       2740       2750       2760 
HCSGKTADLD FFRRVRASYY VVSGNDPANG EPSRAVLDAL LEGKAQWGEN LQVTLIPTHD 

      2770       2780       2790       2800 
TEVTREWYQQ THEQQQQLNV LVLASSSTVV MQDESFPACK IEF 

« Hide

Isoform 2 [UniParc].

Checksum: 28E9817E8116EF8A
Show »

FASTA2,805305,671

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI38857.
RefSeqNP_002364.5. NM_002373.5.
UniGeneHs.194301.
Hs.619338.

3D structure databases

ProteinModelPortalP78559.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110303. 20 interactions.
IntActP78559. 10 interactions.
MINTMINT-1203375.
STRING9606.ENSP00000300231.

Chemistry

DrugBankDB01196. Estramustine.

PTM databases

PhosphoSiteP78559.

Polymorphism databases

DMDM313104325.

Proteomic databases

PaxDbP78559.
PRIDEP78559.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300231; ENSP00000300231; ENSG00000166963. [P78559-1]
GeneID4130.
KEGGhsa:4130.
UCSCuc001zrt.3. human. [P78559-1]

Organism-specific databases

CTD4130.
GeneCardsGC15P043803.
HGNCHGNC:6835. MAP1A.
HPAHPA039063.
HPA039064.
MIM600178. gene.
neXtProtNX_P78559.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000231839.
HOVERGENHBG052408.
KOK10429.
PhylomeDBP78559.
TreeFamTF350229.

Gene expression databases

ArrayExpressP78559.
BgeeP78559.
CleanExHS_MAP1A.
GenevestigatorP78559.

Family and domain databases

Gene3D3.60.15.10. 2 hits.
InterProIPR001279. Beta-lactamas-like.
IPR026074. MAP1.
IPR015656. MAP1A.
[Graphical view]
PANTHERPTHR13843. PTHR13843. 1 hit.
PTHR13843:SF6. PTHR13843:SF6. 1 hit.
SUPFAMSSF56281. SSF56281. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMAP1A. human.
GeneWikiMAP1A.
GenomeRNAi4130.
NextBio16214.
PROP78559.
SOURCESearch...

Entry information

Entry nameMAP1A_HUMAN
AccessionPrimary (citable) accession number: P78559
Secondary accession number(s): O95643 expand/collapse secondary AC list , Q12973, Q15882, Q9UJT4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 122 of the entry and version 6 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM