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P11171

- 41_HUMAN

UniProt

P11171 - 41_HUMAN

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Protein

Protein 4.1

Gene

EPB41

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

Functioni

Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes.

GO - Molecular functioni

  1. 1-phosphatidylinositol binding Source: UniProtKB
  2. spectrin binding Source: BHF-UCL
  3. structural constituent of cytoskeleton Source: ProtInc

GO - Biological processi

  1. actin cytoskeleton organization Source: UniProtKB
  2. blood circulation Source: ProtInc
  3. cortical actin cytoskeleton organization Source: InterPro
  4. positive regulation of protein binding Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calmodulin-binding

Protein family/group databases

TCDBi8.A.25.1.2. the ezrin/radixin/moesin (ezrin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein 4.1
Short name:
P4.1
Alternative name(s):
4.1R
Band 4.1
EPB4.1
Gene namesi
Name:EPB41
Synonyms:E41P
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3377. EPB41.

Subcellular locationi

Cytoplasmcytoskeleton 1 Publication. Cytoplasmcell cortex 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cortical cytoskeleton Source: UniProtKB
  2. extrinsic component of membrane Source: InterPro
  3. nucleus Source: UniProtKB-KW
  4. plasma membrane Source: ProtInc
  5. protein complex Source: UniProtKB
  6. spectrin Source: ProtInc
  7. spectrin-associated cytoskeleton Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

Elliptocytosis 1 (EL1) [MIM:611804]: A Rhesus-linked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape.
Note: The disease is caused by mutations affecting the gene represented in this entry.
Hereditary pyropoikilocytosis (HPP) [MIM:266140]: Autosomal recessive hematologic disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi60 – 601T → A: Loss of CDK1-mediated phosphorylation. Abolishes targeting onto the mitotic spindle; when associated with A-712. 1 Publication
Mutagenesisi712 – 7121S → A: Loss of CDK1-mediated phosphorylation. Abolishes targeting onto the mitotic spindle; when associated with A-60. 1 Publication

Keywords - Diseasei

Elliptocytosis, Hereditary hemolytic anemia, Pyropoikilocytosis

Organism-specific databases

MIMi266140. phenotype.
611804. phenotype.
Orphaneti288. Hereditary elliptocytosis.
PharmGKBiPA27810.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 864864Protein 4.1PRO_0000219390Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141Phosphoserine1 Publication
Modified residuei60 – 601Phosphothreonine; by CDK11 Publication
Modified residuei84 – 841Phosphoserine1 Publication
Modified residuei85 – 851Phosphoserine1 Publication
Modified residuei149 – 1491Phosphoserine1 Publication
Modified residuei151 – 1511Phosphoserine1 Publication
Modified residuei152 – 1521Phosphoserine1 Publication
Modified residuei188 – 1881Phosphoserine2 Publications
Modified residuei191 – 1911Phosphoserine1 Publication
Modified residuei222 – 2221PhosphotyrosineBy similarity
Modified residuei540 – 5401Phosphoserine1 Publication
Modified residuei542 – 5421PhosphoserineBy similarity
Modified residuei555 – 5551Phosphoserine1 Publication
Modified residuei660 – 6601Phosphotyrosine; by EGFR1 Publication
Modified residuei709 – 7091Phosphoserine1 Publication
Modified residuei712 – 7121Phosphoserine; by CDK13 Publications

Post-translational modificationi

Phosphorylated at multiple sites by different protein kinases and each phosphorylation event selectively modulates the protein's functions.
Phosphorylation on Tyr-660 reduces the ability of 4.1 to promote the assembly of the spectrin/actin/4.1 ternary complex.1 Publication
O-glycosylated; contains N-acetylglucosamine side chains in the C-terminal domain.

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP11171.
PaxDbiP11171.
PRIDEiP11171.

PTM databases

PhosphoSiteiP11171.
UniCarbKBiP11171.

Miscellaneous databases

PMAP-CutDBB1ALH9.

Expressioni

Gene expression databases

BgeeiP11171.
CleanExiHS_EPB41.
ExpressionAtlasiP11171. baseline and differential.
GenevestigatoriP11171.

Organism-specific databases

HPAiHPA028414.

Interactioni

Subunit structurei

Binds with a high affinity to glycophorin and with lower affinity to band III protein. Associates with the nuclear mitotic apparatus. Binds calmodulin, CENPJ and DLG1. Also found to associate with contractile apparatus and tight junctions.

Protein-protein interaction databases

BioGridi108349. 24 interactions.
DIPiDIP-17032N.
IntActiP11171. 5 interactions.
MINTiMINT-1208648.

Structurei

Secondary structure

1
864
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi211 – 2155Combined sources
Beta strandi221 – 2255Combined sources
Helixi232 – 24312Combined sources
Helixi248 – 2503Combined sources
Beta strandi251 – 2588Combined sources
Beta strandi261 – 2644Combined sources
Helixi271 – 2744Combined sources
Turni275 – 2773Combined sources
Beta strandi281 – 2888Combined sources
Helixi293 – 2953Combined sources
Helixi299 – 31416Combined sources
Helixi322 – 33716Combined sources
Helixi342 – 3454Combined sources
Helixi350 – 3523Combined sources
Beta strandi356 – 3583Combined sources
Helixi361 – 37212Combined sources
Helixi379 – 39012Combined sources
Turni394 – 3974Combined sources
Beta strandi399 – 4046Combined sources
Beta strandi410 – 4156Combined sources
Beta strandi417 – 4248Combined sources
Beta strandi427 – 4337Combined sources
Helixi434 – 4363Combined sources
Beta strandi437 – 4437Combined sources
Beta strandi446 – 4516Combined sources
Beta strandi454 – 4585Combined sources
Beta strandi461 – 4666Combined sources
Helixi470 – 48617Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GG3X-ray2.80A/B/C210-488[»]
2RQ1NMR-A292-396[»]
3QIJX-ray1.80A/B211-488[»]
DisProtiDP00678.
ProteinModelPortaliP11171.
SMRiP11171. Positions 208-519.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11171.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini210 – 491282FERMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni494 – 614121HydrophilicAdd
BLAST
Regioni615 – 71399Spectrin--actin-bindingAdd
BLAST
Regioni714 – 864151C-terminal (CTD)Add
BLAST

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG242913.
GeneTreeiENSGT00760000118823.
HOVERGENiHBG007777.
InParanoidiP11171.
KOiK06107.
OMAiHEDLTKN.
OrthoDBiEOG7Z69BP.
PhylomeDBiP11171.
TreeFamiTF351626.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR008379. Band_4.1_C.
IPR019749. Band_41_domain.
IPR019750. Band_41_fam.
IPR021187. Band_41_protein.
IPR000798. Ez/rad/moesin_like.
IPR014847. FERM-adjacent.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR011993. PH_like_dom.
IPR007477. SAB_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF05902. 4_1_CTD. 1 hit.
PF08736. FA. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF04382. SAB. 1 hit.
[Graphical view]
PIRSFiPIRSF002304. Membrane_skeletal_4_1. 1 hit.
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P11171-1) [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
MTTEKSLVTE AENSQHQQKE EGEEAINSGQ QEPQQEESCQ TAAEGDNWCE
60 70 80 90 100
QKLKASNGDT PTHEDLTKNK ERTSESRGLS RLFSSFLKRP KSQVSEEEGK
110 120 130 140 150
EVESDKEKGE GGQKEIEFGT SLDEEIILKA PIAAPEPELK TDPSLDLHSL
160 170 180 190 200
SSAETQPAQE ELREDPDFEI KEGEGLEECS KIEVKEESPQ SKAETELKAS
210 220 230 240 250
QKPIRKHRNM HCKVSLLDDT VYECVVEKHA KGQDLLKRVC EHLNLLEEDY
260 270 280 290 300
FGLAIWDNAT SKTWLDSAKE IKKQVRGVPW NFTFNVKFYP PDPAQLTEDI
310 320 330 340 350
TRYYLCLQLR QDIVAGRLPC SFATLALLGS YTIQSELGDY DPELHGVDYV
360 370 380 390 400
SDFKLAPNQT KELEEKVMEL HKSYRSMTPA QADLEFLENA KKLSMYGVDL
410 420 430 440 450
HKAKDLEGVD IILGVCSSGL LVYKDKLRIN RFPWPKVLKI SYKRSSFFIK
460 470 480 490 500
IRPGEQEQYE STIGFKLPSY RAAKKLWKVC VEHHTFFRLT STDTIPKSKF
510 520 530 540 550
LALGSKFRYS GRTQAQTRQA SALIDRPAPH FERTASKRAS RSLDGAAAVD
560 570 580 590 600
SADRSPRPTS APAITQGQVA EGGVLDASAK KTVVPKAQKE TVKAEVKKED
610 620 630 640 650
EPPEQAEPEP TEAWKVEKTH IEVTVPTSNG DQTQKLAEKT EDLIRMRKKK
660 670 680 690 700
RERLDGENIY IRHSNLMLED LDKSQEEIKK HHASISELKK NFMESVPEPR
710 720 730 740 750
PSEWDKRLST HSPFRTLNIN GQIPTGEGPP LVKTQTVTIS DNANAVKSEI
760 770 780 790 800
PTKDVPIVHT ETKTITYEAA QTDDNSGDLD PGVLLTAQTI TSETPSSTTT
810 820 830 840 850
TQITKTVKGG ISETRIEKRI VITGDADIDH DQVLVQAIKE AKEQHPDMSV
860
TKVVVHQETE IADE
Length:864
Mass (Da):97,017
Last modified:March 7, 2006 - v4
Checksum:iB466E7A9D7FBF12B
GO
Isoform 2 (identifier: P11171-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     616-648: Missing.

Show »
Length:831
Mass (Da):93,239
Checksum:iE09038E1654F9248
GO
Isoform 3 (identifier: P11171-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-209: Missing.
     635-648: Missing.

Show »
Length:641
Mass (Da):71,955
Checksum:i0350A4E7EF6E8AE8
GO
Isoform 4 (identifier: P11171-4) [UniParc]FASTAAdd to Basket

Also known as: Erythroid

The sequence of this isoform differs from the canonical sequence as follows:
     1-209: Missing.
     616-648: Missing.
     772-805: Missing.

Show »
Length:588
Mass (Da):66,399
Checksum:iD14399077034CFD5
GO
Isoform 5 (identifier: P11171-5) [UniParc]FASTAAdd to Basket

Also known as: Non-erythroid A

The sequence of this isoform differs from the canonical sequence as follows:
     228-262: Missing.
     616-648: Missing.
     649-669: Missing.

Show »
Length:775
Mass (Da):86,603
Checksum:i4A2D98E32CF8552C
GO
Isoform 6 (identifier: P11171-6) [UniParc]FASTAAdd to Basket

Also known as: Non-erythroid B

The sequence of this isoform differs from the canonical sequence as follows:
     1-209: Missing.
     228-262: Missing.
     616-648: Missing.
     649-669: Missing.

Show »
Length:566
Mass (Da):63,255
Checksum:i288A47844D5CCE62
GO
Isoform 7 (identifier: P11171-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     635-648: Missing.
     729-734: PPLVKT → VSTLST
     735-864: Missing.

Show »
Length:720
Mass (Da):81,235
Checksum:iAE02E72F2EB18335
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511Q → H in AAD42222. 1 PublicationCurated
Sequence conflicti76 – 761S → N in AAD42222. 1 PublicationCurated
Sequence conflicti168 – 1681F → S in AAD42223. 1 PublicationCurated
Sequence conflicti259 – 2591A → T in AAD42222. 1 PublicationCurated
Sequence conflicti665 – 6651N → S in AAD42222. 1 PublicationCurated
Sequence conflicti669 – 6691E → K no nucleotide entry (PubMed:3194408)Curated
Sequence conflicti679 – 6791K → E in AAD42222. 1 PublicationCurated
Sequence conflicti802 – 8021Q → K no nucleotide entry (PubMed:3223413)Curated
Sequence conflicti802 – 8021Q → K in AAA35793. (PubMed:3375238)Curated
Sequence conflicti802 – 8021Q → K in AAA35794. (PubMed:3375238)Curated
Sequence conflicti852 – 8521K → L no nucleotide entry (PubMed:3194408)Curated
Sequence conflicti863 – 8631D → E no nucleotide entry (PubMed:3194408)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti214 – 2141V → I.1 Publication
Corresponds to variant rs111642750 [ dbSNP | Ensembl ].
VAR_009122

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 209209Missing in isoform 3, isoform 4 and isoform 6. 4 PublicationsVSP_000468Add
BLAST
Alternative sequencei228 – 26235Missing in isoform 5 and isoform 6. 2 PublicationsVSP_000469Add
BLAST
Alternative sequencei616 – 64833Missing in isoform 2, isoform 4, isoform 5 and isoform 6. 3 PublicationsVSP_000470Add
BLAST
Alternative sequencei635 – 64814Missing in isoform 3 and isoform 7. 2 PublicationsVSP_000471Add
BLAST
Alternative sequencei649 – 66921Missing in isoform 5 and isoform 6. 2 PublicationsVSP_000472Add
BLAST
Alternative sequencei729 – 7346PPLVKT → VSTLST in isoform 7. 1 PublicationVSP_012872
Alternative sequencei735 – 864130Missing in isoform 7. 1 PublicationVSP_012873Add
BLAST
Alternative sequencei772 – 80534Missing in isoform 4. 1 PublicationVSP_000473Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14993 mRNA. Translation: AAA35795.1.
J03796 mRNA. Translation: AAA35793.1.
J03796 mRNA. Translation: AAA35794.1.
M61733 mRNA. Translation: AAA35797.1.
AF156225 mRNA. Translation: AAD42222.1.
AL138785, AL357500 Genomic DNA. Translation: CAI21967.1.
AL138785, AL357500 Genomic DNA. Translation: CAI21966.1.
AL138785 Genomic DNA. Translation: CAI21968.1.
AL138785, AL357500 Genomic DNA. Translation: CAI21969.1.
AL138785, AL357500 Genomic DNA. Translation: CAI21970.1.
AL357500, AL138785 Genomic DNA. Translation: CAH71636.1.
AL357500, AL138785 Genomic DNA. Translation: CAH71637.1.
AL357500, AL138785 Genomic DNA. Translation: CAH71638.1.
AL357500, AL138785 Genomic DNA. Translation: CAH71639.1.
CH471059 Genomic DNA. Translation: EAX07663.1.
CH471059 Genomic DNA. Translation: EAX07665.1.
CH471059 Genomic DNA. Translation: EAX07667.1.
CH471059 Genomic DNA. Translation: EAX07668.1.
BC039079 mRNA. Translation: AAH39079.1.
AF156226 Genomic DNA. Translation: AAD42223.1.
CCDSiCCDS330.1. [P11171-5]
CCDS331.1. [P11171-4]
CCDS332.1. [P11171-3]
CCDS53288.1. [P11171-1]
CCDS53289.1. [P11171-7]
PIRiA39810. MMHUE4.
RefSeqiNP_001159477.1. NM_001166005.1. [P11171-1]
NP_001159478.1. NM_001166006.1. [P11171-7]
NP_004428.1. NM_004437.3. [P11171-4]
NP_976217.1. NM_203342.2. [P11171-3]
XP_005245818.1. XM_005245761.1. [P11171-1]
XP_005245821.1. XM_005245764.1. [P11171-2]
UniGeneiHs.175437.
Hs.708933.
Hs.712722.

Genome annotation databases

EnsembliENST00000343067; ENSP00000345259; ENSG00000159023. [P11171-1]
ENST00000347529; ENSP00000290100; ENSG00000159023. [P11171-5]
ENST00000349460; ENSP00000317597; ENSG00000159023. [P11171-3]
ENST00000373797; ENSP00000362903; ENSG00000159023. [P11171-7]
ENST00000373798; ENSP00000362904; ENSG00000159023. [P11171-1]
ENST00000373800; ENSP00000362906; ENSG00000159023. [P11171-4]
GeneIDi2035.
KEGGihsa:2035.
UCSCiuc001brg.2. human. [P11171-3]
uc001brh.2. human. [P11171-4]
uc001bri.2. human. [P11171-5]
uc001brk.3. human. [P11171-7]
uc001brl.2. human. [P11171-2]
uc001brm.2. human. [P11171-1]
uc009vtm.2. human. [P11171-6]

Polymorphism databases

DMDMi90101808.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14993 mRNA. Translation: AAA35795.1 .
J03796 mRNA. Translation: AAA35793.1 .
J03796 mRNA. Translation: AAA35794.1 .
M61733 mRNA. Translation: AAA35797.1 .
AF156225 mRNA. Translation: AAD42222.1 .
AL138785 , AL357500 Genomic DNA. Translation: CAI21967.1 .
AL138785 , AL357500 Genomic DNA. Translation: CAI21966.1 .
AL138785 Genomic DNA. Translation: CAI21968.1 .
AL138785 , AL357500 Genomic DNA. Translation: CAI21969.1 .
AL138785 , AL357500 Genomic DNA. Translation: CAI21970.1 .
AL357500 , AL138785 Genomic DNA. Translation: CAH71636.1 .
AL357500 , AL138785 Genomic DNA. Translation: CAH71637.1 .
AL357500 , AL138785 Genomic DNA. Translation: CAH71638.1 .
AL357500 , AL138785 Genomic DNA. Translation: CAH71639.1 .
CH471059 Genomic DNA. Translation: EAX07663.1 .
CH471059 Genomic DNA. Translation: EAX07665.1 .
CH471059 Genomic DNA. Translation: EAX07667.1 .
CH471059 Genomic DNA. Translation: EAX07668.1 .
BC039079 mRNA. Translation: AAH39079.1 .
AF156226 Genomic DNA. Translation: AAD42223.1 .
CCDSi CCDS330.1. [P11171-5 ]
CCDS331.1. [P11171-4 ]
CCDS332.1. [P11171-3 ]
CCDS53288.1. [P11171-1 ]
CCDS53289.1. [P11171-7 ]
PIRi A39810. MMHUE4.
RefSeqi NP_001159477.1. NM_001166005.1. [P11171-1 ]
NP_001159478.1. NM_001166006.1. [P11171-7 ]
NP_004428.1. NM_004437.3. [P11171-4 ]
NP_976217.1. NM_203342.2. [P11171-3 ]
XP_005245818.1. XM_005245761.1. [P11171-1 ]
XP_005245821.1. XM_005245764.1. [P11171-2 ]
UniGenei Hs.175437.
Hs.708933.
Hs.712722.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GG3 X-ray 2.80 A/B/C 210-488 [» ]
2RQ1 NMR - A 292-396 [» ]
3QIJ X-ray 1.80 A/B 211-488 [» ]
DisProti DP00678.
ProteinModelPortali P11171.
SMRi P11171. Positions 208-519.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108349. 24 interactions.
DIPi DIP-17032N.
IntActi P11171. 5 interactions.
MINTi MINT-1208648.

Protein family/group databases

TCDBi 8.A.25.1.2. the ezrin/radixin/moesin (ezrin) family.

PTM databases

PhosphoSitei P11171.
UniCarbKBi P11171.

Polymorphism databases

DMDMi 90101808.

Proteomic databases

MaxQBi P11171.
PaxDbi P11171.
PRIDEi P11171.

Protocols and materials databases

DNASUi 2035.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000343067 ; ENSP00000345259 ; ENSG00000159023 . [P11171-1 ]
ENST00000347529 ; ENSP00000290100 ; ENSG00000159023 . [P11171-5 ]
ENST00000349460 ; ENSP00000317597 ; ENSG00000159023 . [P11171-3 ]
ENST00000373797 ; ENSP00000362903 ; ENSG00000159023 . [P11171-7 ]
ENST00000373798 ; ENSP00000362904 ; ENSG00000159023 . [P11171-1 ]
ENST00000373800 ; ENSP00000362906 ; ENSG00000159023 . [P11171-4 ]
GeneIDi 2035.
KEGGi hsa:2035.
UCSCi uc001brg.2. human. [P11171-3 ]
uc001brh.2. human. [P11171-4 ]
uc001bri.2. human. [P11171-5 ]
uc001brk.3. human. [P11171-7 ]
uc001brl.2. human. [P11171-2 ]
uc001brm.2. human. [P11171-1 ]
uc009vtm.2. human. [P11171-6 ]

Organism-specific databases

CTDi 2035.
GeneCardsi GC01P029213.
HGNCi HGNC:3377. EPB41.
HPAi HPA028414.
MIMi 130500. gene.
266140. phenotype.
611804. phenotype.
neXtProti NX_P11171.
Orphaneti 288. Hereditary elliptocytosis.
PharmGKBi PA27810.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG242913.
GeneTreei ENSGT00760000118823.
HOVERGENi HBG007777.
InParanoidi P11171.
KOi K06107.
OMAi HEDLTKN.
OrthoDBi EOG7Z69BP.
PhylomeDBi P11171.
TreeFami TF351626.

Miscellaneous databases

ChiTaRSi EPB41. human.
EvolutionaryTracei P11171.
GeneWikii EPB41.
GenomeRNAii 2035.
NextBioi 8259.
PMAP-CutDB B1ALH9.
PROi P11171.
SOURCEi Search...

Gene expression databases

Bgeei P11171.
CleanExi HS_EPB41.
ExpressionAtlasi P11171. baseline and differential.
Genevestigatori P11171.

Family and domain databases

Gene3Di 1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProi IPR008379. Band_4.1_C.
IPR019749. Band_41_domain.
IPR019750. Band_41_fam.
IPR021187. Band_41_protein.
IPR000798. Ez/rad/moesin_like.
IPR014847. FERM-adjacent.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR011993. PH_like_dom.
IPR007477. SAB_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF05902. 4_1_CTD. 1 hit.
PF08736. FA. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF04382. SAB. 1 hit.
[Graphical view ]
PIRSFi PIRSF002304. Membrane_skeletal_4_1. 1 hit.
PRINTSi PR00935. BAND41.
PR00661. ERMFAMILY.
SMARTi SM00295. B41. 1 hit.
[Graphical view ]
SUPFAMi SSF47031. SSF47031. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEi PS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton."
    Conboy J.G., Kan Y.W., Shohet S.B., Mohandas N.
    Proc. Natl. Acad. Sci. U.S.A. 83:9512-9516(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), PROTEIN SEQUENCE OF 378-393.
    Tissue: Reticulocyte.
  2. "Expression of specific isoforms of protein 4.1 in erythroid and non-erythroid tissues."
    Tang T.K., Leto T.L., Marchesi V.T., Benz E.J. Jr.
    Adv. Exp. Med. Biol. 241:81-95(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
  4. "Tissue- and development-specific alternative RNA splicing regulates expression of multiple isoforms of erythroid membrane protein 4.1."
    Conboy J.G., Chan J.Y.C., Chasis J.A., Kan Y.W., Mohandas N.
    J. Biol. Chem. 266:8273-8280(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  5. "Sequence of protein 4.1 from a human neuroblastoma cell line: LAN5."
    Huang S.C., Wang C., Lichtenauer U., Vortmeyer A., Zhuang Z.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 7).
    Tissue: Brain.
  9. "Valine to isoleucine polymorphism in exon 4 of human protein 4.1."
    Lichtenauer U., Huang S.C., Vortmeyer A., Zhuang Z.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 157-227, VARIANT ILE-214.
  10. "Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells."
    Conboy J.G., Chan J., Mohandas N., Kan Y.W.
    Proc. Natl. Acad. Sci. U.S.A. 85:9062-9065(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 669-864 (ISOFORM 4), ALTERNATIVE SPLICING.
  11. "Identification of two cAMP-dependent phosphorylation sites on erythrocyte protein 4.1."
    Horne W.C., Prinz W.C., Tang E.K.
    Biochim. Biophys. Acta 1055:87-92(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 534-541; 693-701 AND 793-794, PHOSPHORYLATION AT SER-540 AND SER-709.
  12. "Structure of the spectrin-actin binding site of erythrocyte protein 4.1."
    Correas I., Speicher D.W., Marchesi V.T.
    J. Biol. Chem. 261:13362-13366(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 648-714.
  13. "O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways."
    Inaba M., Maede Y.
    J. Biol. Chem. 264:18149-18155(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF CARBOHYDRATES.
  14. "Phosphorylation of protein 4.1 on tyrosine-418 modulates its function in vitro."
    Subrahmanyan G., Bertics P.J., Anderson R.A.
    Proc. Natl. Acad. Sci. U.S.A. 88:5222-5226(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-660 BY EGFR.
  15. "Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1."
    Lue R.A., Marfatia S.M., Branton D., Chishti A.H.
    Proc. Natl. Acad. Sci. U.S.A. 91:9818-9822(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DLG1.
  16. "Ca(2+)-dependent and Ca(2+)-independent calmodulin binding sites in erythrocyte protein 4.1. Implications for regulation of protein 4.1 interactions with transmembrane proteins."
    Nunomura W., Takakuwa Y., Parra M., Conboy J.G., Mohandas N.
    J. Biol. Chem. 275:6360-6367(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CALMODULIN.
  17. "Protein 4.1 R-135 interacts with a novel centrosomal protein (CPAP) which is associated with the gamma-tubulin complex."
    Hung L.-Y., Tang C.J., Tang T.K.
    Mol. Cell. Biol. 20:7813-7825(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CENPJ.
  18. "Properties of the C-terminal domain of 4.1 proteins."
    Scott C., Phillips G.W., Baines A.J.
    Eur. J. Biochem. 268:3709-3717(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF C-TERMINAL DOMAIN.
  19. "An alternative domain containing a leucine-rich sequence regulates nuclear cytoplasmic localization of protein 4.1R."
    Luque C.M., Perez-Ferreiro C.M., Perez-Gonzalez A., Englmeier L., Koffa M.D., Correas I.
    J. Biol. Chem. 278:2686-2691(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
  20. "Mitotic regulation of protein 4.1R involves phosphorylation by cdc2 kinase."
    Huang S.-C., Liu E.S., Chan S.-H., Munagala I.D., Cho H.T., Jagadeeswaran R., Benz E.J. Jr.
    Mol. Biol. Cell 16:117-127(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF THR-60 AND SER-712, PHOSPHORYLATION AT THR-60 AND SER-712.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-191; SER-555 AND SER-712, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  23. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-85; SER-188 AND SER-712, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "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-14; SER-149; SER-151 AND SER-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Protein 4.1R core domain structure and insights into regulation of cytoskeletal organization."
    Han B.-G., Nunomura W., Takakuwa Y., Mohandas N., Jap B.K.
    Nat. Struct. Biol. 7:871-875(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 210-488.

Entry informationi

Entry namei41_HUMAN
AccessioniPrimary (citable) accession number: P11171
Secondary accession number(s): B1ALH8
, B1ALH9, D3DPM9, D3DPN0, P11176, Q14245, Q5TB35, Q5VXN8, Q8IXV9, Q9Y578, Q9Y579
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 7, 2006
Last modified: November 26, 2014
This is version 175 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3