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Protein

Microtubule-associated protein 4

Gene

MAP4

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

Functioni

Non-neuronal microtubule-associated protein. Promotes microtubule assembly.1 Publication

GO - Molecular functioni

  • microtubule binding Source: GO_Central
  • poly(A) RNA binding Source: UniProtKB
  • structural molecule activity Source: ProtInc

GO - Biological processi

  • cell division Source: MGI
  • establishment of spindle orientation Source: MGI
  • microtubule sliding Source: MGI
  • mitotic spindle organization Source: MGI
  • negative regulation of nonmotile primary cilium assembly Source: GO_Central
  • neuron projection development Source: GO_Central
Complete GO annotation...

Enzyme and pathway databases

SIGNORiP27816.

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein 4
Short name:
MAP-4
Gene namesi
Name:MAP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:6862. MAP4.

Subcellular locationi

GO - Cellular componenti

  • axoneme Source: GO_Central
  • cytoplasm Source: HPA
  • extracellular exosome Source: UniProtKB
  • microtubule Source: UniProtKB-KW
  • microtubule associated complex Source: ProtInc
  • microtubule cytoskeleton Source: HPA
  • mitotic spindle Source: MGI
  • neuronal postsynaptic density Source: Ensembl
  • neuron projection Source: GO_Central
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi696 – 6961S → E: No change in microtubule binding; no change in microtubule polymerization activity. 1 Publication
Mutagenesisi787 – 7871S → E: No change in microtubule binding; reduced microtubule polymerization activity. 1 Publication

Organism-specific databases

PharmGKBiPA30608.

Chemistry

DrugBankiDB01248. Docetaxel.
DB01229. Paclitaxel.

Polymorphism and mutation databases

BioMutaiMAP4.
DMDMi269849673.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 11521151Microtubule-associated protein 4PRO_0000072751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication
Modified residuei5 – 51PhosphoserineCombined sources
Modified residuei14 – 141PhosphoserineCombined sources
Modified residuei60 – 601PhosphoserineCombined sources
Modified residuei99 – 991PhosphoserineCombined sources
Modified residuei253 – 2531PhosphoserineBy similarity
Cross-linki269 – 269Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei280 – 2801PhosphoserineCombined sources
Modified residuei282 – 2821PhosphothreonineCombined sources
Modified residuei354 – 3541PhosphothreonineCombined sources
Modified residuei358 – 3581PhosphoserineCombined sources
Modified residuei380 – 3801PhosphothreonineCombined sources
Modified residuei384 – 3841PhosphoserineCombined sources
Modified residuei440 – 4401PhosphoserineCombined sources
Modified residuei442 – 4421PhosphothreonineCombined sources
Modified residuei507 – 5071PhosphoserineCombined sources
Modified residuei510 – 5101PhosphoserineCombined sources
Modified residuei521 – 5211PhosphothreonineCombined sources
Modified residuei526 – 5261PhosphothreonineCombined sources
Modified residuei571 – 5711PhosphothreonineCombined sources
Modified residuei580 – 5801PhosphoserineCombined sources
Modified residuei585 – 5851PhosphothreonineCombined sources
Modified residuei624 – 6241Phosphoserine; in variant Ile-628Combined sources
Modified residuei636 – 6361PhosphoserineCombined sources
Modified residuei643 – 6431PhosphoserineBy similarity
Modified residuei687 – 6871PhosphothreonineBy similarity
Modified residuei696 – 6961PhosphoserineCombined sources1 Publication
Modified residuei713 – 7131PhosphoserineCombined sources
Modified residuei723 – 7231PhosphoserineCombined sources
Modified residuei787 – 7871PhosphoserineCombined sources1 Publication
Modified residuei797 – 7971PhosphoserineCombined sources
Modified residuei825 – 8251PhosphoserineCombined sources
Modified residuei827 – 8271PhosphoserineCombined sources
Modified residuei853 – 8531PhosphoserineCombined sources
Modified residuei928 – 9281PhosphoserineCombined sources
Modified residuei941 – 9411PhosphoserineCombined sources
Modified residuei942 – 9421PhosphothreonineCombined sources
Modified residuei1000 – 10001PhosphoserineCombined sources
Modified residuei1073 – 10731PhosphoserineCombined sources
Modified residuei1145 – 11451PhosphoserineCombined sources
Modified residuei1151 – 11511PhosphoserineCombined sources
Isoform 4 (identifier: P27816-4)
Modified residuei28 – 281PhosphothreonineCombined sources
Modified residuei269 – 2691PhosphoserineCombined sources
Isoform 3 (identifier: P27816-3)
Modified residuei337 – 3371PhosphoserineCombined sources
Modified residuei338 – 3381PhosphoserineCombined sources
Isoform 5 (identifier: P27816-5)
Modified residuei803 – 8031PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing detachment from microtubules, and their disassembly (By similarity). Phosphorylation on Ser-787 negatively regulates MAP4 activity to promote microtubule assembly. Isoform 3 is phosphorylated on Ser-337 and Ser-338.By similarity1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP27816.
MaxQBiP27816.
PaxDbiP27816.
PeptideAtlasiP27816.
PRIDEiP27816.

PTM databases

iPTMnetiP27816.
PhosphoSiteiP27816.
SwissPalmiP27816.

Miscellaneous databases

PMAP-CutDBP27816.

Expressioni

Gene expression databases

BgeeiP27816.
CleanExiHS_MAP4.
ExpressionAtlasiP27816. baseline and differential.
GenevisibleiP27816. HS.

Organism-specific databases

HPAiHPA038149.
HPA038150.

Interactioni

Subunit structurei

Interacts with SEPT2; this interaction impedes tubulin-binding. Interacts with TRAF3IP1 (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163332EBI-715255,EBI-389883

GO - Molecular functioni

Protein-protein interaction databases

BioGridi110306. 60 interactions.
IntActiP27816. 22 interactions.
MINTiMINT-1425668.
STRINGi9606.ENSP00000353375.

Structurei

3D structure databases

ProteinModelPortaliP27816.
SMRiP27816. Positions 985-1056.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati248 – 261141Add
BLAST
Repeati262 – 275142Add
BLAST
Repeati276 – 289143Add
BLAST
Repeati290 – 303144Add
BLAST
Repeati304 – 317145Add
BLAST
Repeati318 – 331146Add
BLAST
Repeati332 – 345147Add
BLAST
Repeati346 – 35168; truncated
Repeati352 – 3772626 residues 1Add
BLAST
Repeati378 – 4032626 residues 2Add
BLAST
Repeati408 – 421149Add
BLAST
Repeati422 – 4331210Add
BLAST
Repeati434 – 4471411Add
BLAST
Repeati448 – 4611412Add
BLAST
Repeati462 – 4751413Add
BLAST
Repeati476 – 4891414Add
BLAST
Repeati490 – 5031415Add
BLAST
Repeati504 – 5171416Add
BLAST
Repeati532 – 5451417Add
BLAST
Repeati923 – 95331Tau/MAP 1Add
BLAST
Repeati992 – 102231Tau/MAP 2Add
BLAST
Repeati1023 – 105331Tau/MAP 3Add
BLAST
Repeati1054 – 108532Tau/MAP 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni248 – 54529817 X 14 AA tandem repeatsAdd
BLAST

Sequence similaritiesi

Contains 4 Tau/MAP repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IG6M. Eukaryota.
ENOG4111J07. LUCA.
GeneTreeiENSGT00530000063491.
HOGENOMiHOG000139406.
HOVERGENiHBG006323.
InParanoidiP27816.
KOiK10431.
OrthoDBiEOG7FFMR7.
PhylomeDBiP27816.
TreeFamiTF316358.

Family and domain databases

InterProiIPR027324. MAP2/MAP4/Tau.
IPR027323. MAP4.
IPR001084. MAP_tubulin-bd_rpt.
[Graphical view]
PANTHERiPTHR11501. PTHR11501. 2 hits.
PTHR11501:SF16. PTHR11501:SF16. 2 hits.
PfamiPF00418. Tubulin-binding. 4 hits.
[Graphical view]
PROSITEiPS00229. TAU_MAP_1. 4 hits.
PS51491. TAU_MAP_2. 4 hits.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

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

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P27816-1) [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
MADLSLADAL TEPSPDIEGE IKRDFIATLE AEAFDDVVGE TVGKTDYIPL
60 70 80 90 100
LDVDEKTGNS ESKKKPCSET SQIEDTPSSK PTLLANGGHG VEGSDTTGSP
110 120 130 140 150
TEFLEEKMAY QEYPNSQNWP EDTNFCFQPE QVVDPIQTDP FKMYHDDDLA
160 170 180 190 200
DLVFPSSATA DTSIFAGQND PLKDSYGMSP CNTAVVPQGW SVEALNSPHS
210 220 230 240 250
ESFVSPEAVA EPPQPTAVPL ELAKEIEMAS EERPPAQALE IMMGLKTTDM
260 270 280 290 300
APSKETEMAL AKDMALATKT EVALAKDMES PTKLDVTLAK DMQPSMESDM
310 320 330 340 350
ALVKDMELPT EKEVALVKDV RWPTETDVSS AKNVVLPTET EVAPAKDVTL
360 370 380 390 400
LKETERASPI KMDLAPSKDM GPPKENKKET ERASPIKMDL APSKDMGPPK
410 420 430 440 450
ENKIVPAKDL VLLSEIEVAQ ANDIISSTEI SSAEKVALSS ETEVALARDM
460 470 480 490 500
TLPPETNVIL TKDKALPLEA EVAPVKDMAQ LPETEIAPAK DVAPSTVKEV
510 520 530 540 550
GLLKDMSPLS ETEMALGKDV TPPPETEVVL IKNVCLPPEM EVALTEDQVP
560 570 580 590 600
ALKTEAPLAK DGVLTLANNV TPAKDVPPLS ETEATPVPIK DMEIAQTQKG
610 620 630 640 650
ISEDSHLESL QDVGQSAAPT FMISPETVTG TGKKCSLPAE EDSVLEKLGE
660 670 680 690 700
RKPCNSQPSE LSSETSGIAR PEEGRPVVSG TGNDITTPPN KELPPSPEKK
710 720 730 740 750
TKPLATTQPA KTSTSKAKTQ PTSLPKQPAP TTIGGLNKKP MSLASGLVPA
760 770 780 790 800
APPKRPAVAS ARPSILPSKD VKPKPIADAK APEKRASPSK PASAPASRSG
810 820 830 840 850
SKSTQTVAKT TTAAAVASTG PSSRSPSTLL PKKPTAIKTE GKPAEVKKMT
860 870 880 890 900
AKSVPADLSR PKSTSTSSMK KTTTLSGTAP AAGVVPSRVK ATPMPSRPST
910 920 930 940 950
TPFIDKKPTS AKPSSTTPRL SRLATNTSAP DLKNVRSKVG STENIKHQPG
960 970 980 990 1000
GGRAKVEKKT EAAATTRKPE SNAVTKTAGP IASAQKQPAG KVQIVSKKVS
1010 1020 1030 1040 1050
YSHIQSKCGS KDNIKHVPGG GNVQIQNKKV DISKVSSKCG SKANIKHKPG
1060 1070 1080 1090 1100
GGDVKIESQK LNFKEKAQAK VGSLDNVGHL PAGGAVKTEG GGSEAPLCPG
1110 1120 1130 1140 1150
PPAGEEPAIS EAAPEAGAPT SASGLNGHPT LSGGGDQREA QTLDSQIQET

SI
Length:1,152
Mass (Da):121,005
Last modified:November 24, 2009 - v3
Checksum:i061A69AC18593339
GO
Isoform 2 (identifier: P27816-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     558-730: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:979
Mass (Da):102,906
Checksum:i04F3054281DA91E7
GO
Isoform 3 (identifier: P27816-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-151: Missing.
     152-437: LVFPSSATAD...TEISSAEKVA → MSLSDKQTAS...IRDHDKELEK
     441-631: ETEVALARDM...MISPETVTGT → TEEAVLNQAP...EKQPGQTALA
     635-666: CSLPAEEDSVLEKLGERKPCNSQPSELSSETS → EIEVTATQSTPSFLFEKPPRD
     703-716: PLATTQPAKTSTSK → VGARMVVIFYCHNF
     717-1152: Missing.

Show »
Length:539
Mass (Da):58,557
Checksum:i6B67BBE02C4F946D
GO
Isoform 4 (identifier: P27816-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-82: Missing.
     83-221: LLANGGHGVE...PPQPTAVPLE → METTGDQGIE...VKEGDSFPDT
     225-271: EIEMASEERP...KDMALATKTE → NGQEIAPAQI...AVVPSTSTGG
     275-666: AKDMESPTKL...QPSELSSETS → PITTAIETVN...QERHKQLKSA
     939-953: Missing.

Show »
Length:872
Mass (Da):91,154
Checksum:i777E25AE88E22090
GO
Isoform 5 (identifier: P27816-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     322-666: WPTETDVSSA...QPSELSSETS → LPEPKDKILE...QERHKQLKSA
     954-1022: Missing.
     1151-1152: SI → N

Show »
Length:809
Mass (Da):85,252
Checksum:iF259E4B688F2B44F
GO
Isoform 6 (identifier: P27816-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1088-1152: TEGGGSEAPL...LDSQIQETSI → IETYRLTFRA...VLGPLSRAVH

Note: No experimental confirmation available.
Show »
Length:1,135
Mass (Da):119,958
Checksum:i9FDE4697ADAD05D5
GO
Isoform 7 (identifier: P27816-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     98-99: GS → EA
     100-1152: Missing.

Note: No experimental confirmation available.
Show »
Length:99
Mass (Da):10,441
Checksum:i2D295214DAA6FB37
GO

Sequence cautioni

The sequence BAD92614.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti160 – 1601A → R in AAA59553 (PubMed:1718985).Curated
Sequence conflicti319 – 3191D → G in CAH18346 (PubMed:17974005).Curated
Sequence conflicti1109 – 11091I → V in CAH18346 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231R → Q.
Corresponds to variant rs11711953 [ dbSNP | Ensembl ].
VAR_039566
Natural varianti366 – 3661P → L.
Corresponds to variant rs13097415 [ dbSNP | Ensembl ].
VAR_039567
Natural varianti367 – 3671S → P.
Corresponds to variant rs13096947 [ dbSNP | Ensembl ].
VAR_039568
Natural varianti409 – 4091D → G.
Corresponds to variant rs13076542 [ dbSNP | Ensembl ].
VAR_039569
Natural varianti427 – 4271S → Y.1 Publication
Corresponds to variant rs1060407 [ dbSNP | Ensembl ].
VAR_020361
Natural varianti441 – 4411E → Q.
Corresponds to variant rs2230169 [ dbSNP | Ensembl ].
VAR_020362
Natural varianti628 – 6281V → I.Combined sources1 Publication
Corresponds to variant rs1137524 [ dbSNP | Ensembl ].
VAR_039570
Natural varianti994 – 9941I → V.
Corresponds to variant rs35736893 [ dbSNP | Ensembl ].
VAR_039571

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 151151Missing in isoform 3. 1 PublicationVSP_032065Add
BLAST
Alternative sequencei1 – 8282Missing in isoform 4. 1 PublicationVSP_032066Add
BLAST
Alternative sequencei83 – 221139LLANG…AVPLE → METTGDQGIEGMAYMDENRN ITFTCPRTPSELINKSSPLE VLGSAACEKLPTPTPQVVKE GDSFPDT in isoform 4. 1 PublicationVSP_032067Add
BLAST
Alternative sequencei98 – 992GS → EA in isoform 7. 1 PublicationVSP_043240
Alternative sequencei100 – 11521053Missing in isoform 7. 1 PublicationVSP_043241Add
BLAST
Alternative sequencei152 – 437286LVFPS…AEKVA → MSLSDKQTASLTAAYGQLSK GKPAECRMDSPKEISQAGFE WQRTEGKLNEIGLNVSMDGQ PKDGLVKNASFLEQNKLCFF EGKLDKELSIEMQDKDCQEA SGHLESRYVISETCHPLEGN SVHQKTSEFHLGLIEGPDKN KTIPVQGKVAGKNGLETKSQ SDLDFPGAADIPTRYVKEQE TSVWNPSFHPVAQGSLGSRE ATPGEMENSITPGCPVIGVV NDNSEQLKCESPLLVSLAHP APIIEHSPTTIPPITMVFTQ EHLNASCHIRDHDKELEK in isoform 3. 1 PublicationVSP_032068Add
BLAST
Alternative sequencei225 – 27147EIEMA…ATKTE → NGQEIAPAQISKSLMVDNYT KDGVPGQERPKGPSAVVPST STGG in isoform 4. 1 PublicationVSP_032069Add
BLAST
Alternative sequencei275 – 666392AKDME…SSETS → PITTAIETVNIHGDHSLKNK AELADSMKNEAGIDEGHVIG ESESVHSGASKHSVEKVTEL AKGHLLPGVPVEDQSLPGEA RALEGYADRGNFPAHPVNEE KETKEGSVAVQIPDLLEDKA QKLSFCEDQNAQDRNSKGSD SLNKKVDLTLLSPKSENDKL KEISLACKITELESVSLPTP EIQSDFLHSKVEAPPSEVAD TLVIMTASKGVRLPEPKDKI LETPQKMTEKSESKTPGEGK KEDKSRMAEPMKGYMRPTKS RGLTPLLPKSTIQEQERHKQ LKSA in isoform 4. 1 PublicationVSP_032070Add
BLAST
Alternative sequencei322 – 666345WPTET…SSETS → LPEPKDKILETPQKMTEKSE SKTPGEGKKEDKSRMAEPMK GYMRPTKSRGLTPLLPKSTI QEQERHKQLKSA in isoform 5. 1 PublicationVSP_032071Add
BLAST
Alternative sequencei441 – 631191ETEVA…TVTGT → TEEAVLNQAPQQKKAVRRAL SECSHLSVPPAVNLADKYPE LPAREEPSSGLLPPPSSPMP SPTPGKLGAPAMKRSMTVGE EQTASYKLSPGKLPILSTKE IPPFICEEPVAKKREELAHF SNSSSNSGKKELGTAGLYLH SKLEQIPEGSSKEKGQEDFS ETRIDSCSQVCQRGEKQPGQ TALA in isoform 3. 1 PublicationVSP_032072Add
BLAST
Alternative sequencei558 – 730173Missing in isoform 2. 1 PublicationVSP_003200Add
BLAST
Alternative sequencei635 – 66632CSLPA…SSETS → EIEVTATQSTPSFLFEKPPR D in isoform 3. 1 PublicationVSP_032073Add
BLAST
Alternative sequencei703 – 71614PLATT…TSTSK → VGARMVVIFYCHNF in isoform 3. 1 PublicationVSP_032074Add
BLAST
Alternative sequencei717 – 1152436Missing in isoform 3. 1 PublicationVSP_032075Add
BLAST
Alternative sequencei939 – 95315Missing in isoform 4. 1 PublicationVSP_032076Add
BLAST
Alternative sequencei954 – 102269Missing in isoform 5. 1 PublicationVSP_032077Add
BLAST
Alternative sequencei1088 – 115265TEGGG…QETSI → IETYRLTFRANARARTDHGA DIVSRPPHFPGGPNSGSRVL GPLSRAVH in isoform 6. 1 PublicationVSP_032078Add
BLAST
Alternative sequencei1151 – 11522SI → N in isoform 5. 1 PublicationVSP_032079

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64571 mRNA. Translation: AAA59553.1.
U19727 mRNA. Translation: AAA67361.1.
AK054696 mRNA. Translation: BAB70795.1.
AK125245 mRNA. Translation: BAC86099.1.
AB209377 mRNA. Translation: BAD92614.1. Different initiation.
AC124916 Genomic DNA. No translation available.
AC139667 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64839.1.
BC008715 mRNA. Translation: AAH08715.1.
BC012794 mRNA. Translation: AAH12794.1.
BC015149 mRNA. Translation: AAH15149.1.
BC051843 mRNA. Translation: AAH51843.1.
CR749544 mRNA. Translation: CAH18346.1.
CCDSiCCDS33750.1. [P27816-1]
CCDS46818.1. [P27816-6]
CCDS46821.1. [P27816-7]
PIRiA41206. A33183.
RefSeqiNP_001127836.1. NM_001134364.1. [P27816-6]
NP_002366.2. NM_002375.4. [P27816-1]
NP_112147.2. NM_030885.3. [P27816-7]
UniGeneiHs.517949.

Genome annotation databases

EnsembliENST00000360240; ENSP00000353375; ENSG00000047849. [P27816-1]
ENST00000395734; ENSP00000379083; ENSG00000047849. [P27816-6]
ENST00000434267; ENSP00000402767; ENSG00000047849. [P27816-7]
ENST00000439356; ENSP00000397414; ENSG00000047849. [P27816-7]
GeneIDi4134.
KEGGihsa:4134.
UCSCiuc003csb.3. human. [P27816-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64571 mRNA. Translation: AAA59553.1.
U19727 mRNA. Translation: AAA67361.1.
AK054696 mRNA. Translation: BAB70795.1.
AK125245 mRNA. Translation: BAC86099.1.
AB209377 mRNA. Translation: BAD92614.1. Different initiation.
AC124916 Genomic DNA. No translation available.
AC139667 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64839.1.
BC008715 mRNA. Translation: AAH08715.1.
BC012794 mRNA. Translation: AAH12794.1.
BC015149 mRNA. Translation: AAH15149.1.
BC051843 mRNA. Translation: AAH51843.1.
CR749544 mRNA. Translation: CAH18346.1.
CCDSiCCDS33750.1. [P27816-1]
CCDS46818.1. [P27816-6]
CCDS46821.1. [P27816-7]
PIRiA41206. A33183.
RefSeqiNP_001127836.1. NM_001134364.1. [P27816-6]
NP_002366.2. NM_002375.4. [P27816-1]
NP_112147.2. NM_030885.3. [P27816-7]
UniGeneiHs.517949.

3D structure databases

ProteinModelPortaliP27816.
SMRiP27816. Positions 985-1056.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110306. 60 interactions.
IntActiP27816. 22 interactions.
MINTiMINT-1425668.
STRINGi9606.ENSP00000353375.

Chemistry

DrugBankiDB01248. Docetaxel.
DB01229. Paclitaxel.

PTM databases

iPTMnetiP27816.
PhosphoSiteiP27816.
SwissPalmiP27816.

Polymorphism and mutation databases

BioMutaiMAP4.
DMDMi269849673.

Proteomic databases

EPDiP27816.
MaxQBiP27816.
PaxDbiP27816.
PeptideAtlasiP27816.
PRIDEiP27816.

Protocols and materials databases

DNASUi4134.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360240; ENSP00000353375; ENSG00000047849. [P27816-1]
ENST00000395734; ENSP00000379083; ENSG00000047849. [P27816-6]
ENST00000434267; ENSP00000402767; ENSG00000047849. [P27816-7]
ENST00000439356; ENSP00000397414; ENSG00000047849. [P27816-7]
GeneIDi4134.
KEGGihsa:4134.
UCSCiuc003csb.3. human. [P27816-1]

Organism-specific databases

CTDi4134.
GeneCardsiMAP4.
HGNCiHGNC:6862. MAP4.
HPAiHPA038149.
HPA038150.
MIMi157132. gene.
neXtProtiNX_P27816.
PharmGKBiPA30608.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IG6M. Eukaryota.
ENOG4111J07. LUCA.
GeneTreeiENSGT00530000063491.
HOGENOMiHOG000139406.
HOVERGENiHBG006323.
InParanoidiP27816.
KOiK10431.
OrthoDBiEOG7FFMR7.
PhylomeDBiP27816.
TreeFamiTF316358.

Enzyme and pathway databases

SIGNORiP27816.

Miscellaneous databases

ChiTaRSiMAP4. human.
GeneWikiiMAP4.
GenomeRNAii4134.
PMAP-CutDBP27816.
PROiP27816.
SOURCEiSearch...

Gene expression databases

BgeeiP27816.
CleanExiHS_MAP4.
ExpressionAtlasiP27816. baseline and differential.
GenevisibleiP27816. HS.

Family and domain databases

InterProiIPR027324. MAP2/MAP4/Tau.
IPR027323. MAP4.
IPR001084. MAP_tubulin-bd_rpt.
[Graphical view]
PANTHERiPTHR11501. PTHR11501. 2 hits.
PTHR11501:SF16. PTHR11501:SF16. 2 hits.
PfamiPF00418. Tubulin-binding. 4 hits.
[Graphical view]
PROSITEiPS00229. TAU_MAP_1. 4 hits.
PS51491. TAU_MAP_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A model for microtubule-associated protein 4 structure. Domains defined by comparisons of human, mouse, and bovine sequences."
    West R.R., Tenbarge K.M., Olmsted J.B.
    J. Biol. Chem. 266:21886-21896(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS TYR-427 AND ILE-628.
  2. "Differential expression of alternatively spliced forms of MAP4: a repertoire of structurally different microtubule-binding domains."
    Chapin S.J., Lue C.M., Yu M.T., Bulinski J.C.
    Biochemistry 34:2289-2301(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-996 (ISOFORM 4).
    Tissue: Cerebellum and Heart.
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
    Tissue: Brain.
  5. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 7).
    Tissue: Eye and Muscle.
  8. Bienvenut W.V., Ramsay A., Leung H.Y., Zebisch A., Kolch W.
    Submitted (OCT-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-23; 322-356; 436-448; 561-574; 727-738; 810-832; 853-862; 872-888 AND 923-933, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma and Prostatic adenocarcinoma.
  9. "Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4) contains a domain homologous to the microtubule-binding domains of neuronal MAP2 and tau."
    Chapin S.J., Bulinski J.C.
    J. Cell Sci. 98:27-36(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 102-1152 (ISOFORM 1).
    Tissue: Brain.
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-1151 (ISOFORM 5).
    Tissue: Liver.
  11. "Ser787 in the proline-rich region of human MAP4 is a critical phosphorylation site that reduces its activity to promote tubulin polymerization."
    Kitazawa H., Iida J., Uchida A., Haino-Fukushima K., Itoh T.J., Hotani H., Ookata K., Murofushi H., Bulinski J.C., Kishimoto T., Hisanaga S.
    Cell Struct. Funct. 25:33-39(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-696 AND SER-787, FUNCTION, MUTAGENESIS OF SER-696 AND SER-787.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
  14. "Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4."
    Kremer B.E., Haystead T., Macara I.G.
    Mol. Biol. Cell 16:4648-4659(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SEPT2.
  15. "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-507; THR-521; THR-571 AND SER-1073, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-571 AND SER-827, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  18. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358 AND SER-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
    Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
    Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND SER-338 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-99; SER-280; SER-358; SER-384; SER-507; THR-521; THR-571; SER-580; THR-585; SER-636; SER-825; SER-941 AND SER-1151, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-28 AND SER-269 (ISOFORM 4), VARIANT [LARGE SCALE ANALYSIS] ILE-628, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "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].
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1073, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "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-507; THR-521; THR-571; THR-585 AND SER-1151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  25. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-280; THR-282; THR-354; SER-358; THR-380; SER-384; SER-507; SER-510; THR-521; THR-526; THR-571; THR-585; SER-636; SER-787; SER-797; SER-825; SER-928; SER-941; SER-1073 AND SER-1151, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624 (VARIANT ILE-628), VARIANT [LARGE SCALE ANALYSIS] ILE-628, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "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; THR-282; SER-358; SER-384; SER-507; THR-521; THR-526; THR-571; SER-636; SER-787; SER-941; THR-942; SER-1000; SER-1073; SER-1145 AND SER-1151, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-60; SER-280; SER-358; SER-384; SER-440; THR-442; SER-507; SER-510; THR-521; THR-571; SER-580; THR-585; SER-636; SER-696; SER-713; SER-723; SER-787; SER-825; SER-853; SER-928 AND SER-1073, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  30. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-358; SER-384; SER-636 AND SER-1000, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  31. "Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli."
    Impens F., Radoshevich L., Cossart P., Ribet D.
    Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMAP4_HUMAN
AccessioniPrimary (citable) accession number: P27816
Secondary accession number(s): Q13082
, Q59FT2, Q68D74, Q6ZUW9, Q86V26, Q96A76, Q96NS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 24, 2009
Last modified: July 6, 2016
This is version 168 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.