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P11171 (41_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein 4.1
Short name=P4.1
Alternative name(s):
4.1R
Band 4.1
EPB4.1
Gene names
Name:EPB41
Synonyms:E41P
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length864 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Cytoplasm › cytoskeleton. Cytoplasm › cell cortex. Nucleus Ref.19.

Post-translational modification

Phosphorylated at multiple sites by different protein kinases and each phosphorylation event selectively modulates the protein's functions. Ref.11 Ref.14 Ref.20

Phosphorylation on Tyr-660 reduces the ability of 4.1 to promote the assembly of the spectrin/actin/4.1 ternary complex.

O-glycosylated; contains N-acetylglucosamine side chains in the C-terminal domain. Ref.13

Involvement in disease

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.

Sequence similarities

Contains 1 FERM domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseElliptocytosis
Hereditary hemolytic anemia
Pyropoikilocytosis
   LigandActin-binding
Calmodulin-binding
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Non-traceable author statement PubMed 8434260. Source: UniProtKB

blood circulation

Traceable author statement PubMed 6894932. Source: ProtInc

cortical actin cytoskeleton organization

Inferred from electronic annotation. Source: InterPro

positive regulation of protein binding

Inferred from direct assay PubMed 3693401. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

extrinsic to membrane

Inferred from electronic annotation. Source: InterPro

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

protein complex

Inferred from direct assay PubMed 16060676. Source: UniProtKB

spectrin

Traceable author statement PubMed 6894932. Source: ProtInc

spectrin-associated cytoskeleton

Traceable author statement PubMed 3693401. Source: BHF-UCL

   Molecular_function1-phosphatidylinositol binding

Inferred from direct assay PubMed 16669616. Source: UniProtKB

spectrin binding

Traceable author statement PubMed 3693401. Source: BHF-UCL

structural constituent of cytoskeleton

Traceable author statement PubMed 6894932. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P11171-1)

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: P11171-2)

The sequence of this isoform differs from the canonical sequence as follows:
     616-648: Missing.
Isoform 3 (identifier: P11171-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-209: Missing.
     635-648: Missing.
Isoform 4 (identifier: P11171-4)

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.
Isoform 5 (identifier: P11171-5)

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.
Isoform 6 (identifier: P11171-6)

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.
Isoform 7 (identifier: P11171-7)

The sequence of this isoform differs from the canonical sequence as follows:
     635-648: Missing.
     729-733: PPLVK → VSTLS
     734-864: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 864864Protein 4.1
PRO_0000219390

Regions

Domain210 – 491282FERM
Region494 – 614121Hydrophilic
Region615 – 71399Spectrin--actin-binding
Region714 – 864151C-terminal (CTD)

Amino acid modifications

Modified residue141Phosphoserine Ref.11 Ref.25
Modified residue601Phosphothreonine; by CDK1 Ref.11 Ref.20
Modified residue841Phosphoserine Ref.11 Ref.23
Modified residue851Phosphoserine Ref.11 Ref.23
Modified residue1491Phosphoserine Ref.11 Ref.25
Modified residue1511Phosphoserine Ref.11 Ref.25
Modified residue1521Phosphoserine Ref.11 Ref.25
Modified residue1881Phosphoserine Ref.11 Ref.21 Ref.23
Modified residue1911Phosphoserine Ref.11 Ref.21
Modified residue2221Phosphotyrosine By similarity
Modified residue5401Phosphoserine By similarity
Modified residue5421Phosphoserine By similarity
Modified residue5551Phosphoserine Ref.11 Ref.21
Modified residue6601Phosphotyrosine; by EGFR Ref.11 Ref.14
Modified residue6741Phosphoserine By similarity
Modified residue7121Phosphoserine; by CDK1 Ref.11 Ref.20 Ref.21 Ref.23

Natural variations

Alternative sequence1 – 209209Missing in isoform 3, isoform 4 and isoform 6.
VSP_000468
Alternative sequence228 – 26235Missing in isoform 5 and isoform 6.
VSP_000469
Alternative sequence616 – 64833Missing in isoform 2, isoform 4, isoform 5 and isoform 6.
VSP_000470
Alternative sequence635 – 64814Missing in isoform 3 and isoform 7.
VSP_000471
Alternative sequence649 – 66921Missing in isoform 5 and isoform 6.
VSP_000472
Alternative sequence729 – 7335PPLVK → VSTLS in isoform 7.
VSP_012872
Alternative sequence734 – 864131Missing in isoform 7.
VSP_012873
Alternative sequence772 – 80534Missing in isoform 4.
VSP_000473
Natural variant2141V → I. Ref.9
VAR_009122

Experimental info

Mutagenesis601T → A: Loss of CDK1-mediated phosphorylation. Abolishes targeting onto the mitotic spindle; when associated with A-712. Ref.20
Mutagenesis7121S → A: Loss of CDK1-mediated phosphorylation. Abolishes targeting onto the mitotic spindle; when associated with A-60. Ref.20
Sequence conflict511Q → H in AAD42222. Ref.5
Sequence conflict761S → N in AAD42222. Ref.5
Sequence conflict1681F → S in AAD42223. Ref.9
Sequence conflict2591A → T in AAD42222. Ref.5
Sequence conflict6651N → S in AAD42222. Ref.5
Sequence conflict6691E → K no nucleotide entry Ref.10
Sequence conflict6791K → E in AAD42222. Ref.5
Sequence conflict8021Q → K no nucleotide entry Ref.2
Sequence conflict8021Q → K in AAA35793. Ref.3
Sequence conflict8021Q → K in AAA35794. Ref.3
Sequence conflict8521K → L no nucleotide entry Ref.10
Sequence conflict8631D → E no nucleotide entry Ref.10

Secondary structure

1 ..................................................... 864
Helix Strand Turn

Details...

Sequences

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

Last modified March 7, 2006. Version 4.
Checksum: B466E7A9D7FBF12B

FASTA86497,017
        10         20         30         40         50         60 
MTTEKSLVTE AENSQHQQKE EGEEAINSGQ QEPQQEESCQ TAAEGDNWCE QKLKASNGDT 

        70         80         90        100        110        120 
PTHEDLTKNK ERTSESRGLS RLFSSFLKRP KSQVSEEEGK EVESDKEKGE GGQKEIEFGT 

       130        140        150        160        170        180 
SLDEEIILKA PIAAPEPELK TDPSLDLHSL SSAETQPAQE ELREDPDFEI KEGEGLEECS 

       190        200        210        220        230        240 
KIEVKEESPQ SKAETELKAS QKPIRKHRNM HCKVSLLDDT VYECVVEKHA KGQDLLKRVC 

       250        260        270        280        290        300 
EHLNLLEEDY FGLAIWDNAT SKTWLDSAKE IKKQVRGVPW NFTFNVKFYP PDPAQLTEDI 

       310        320        330        340        350        360 
TRYYLCLQLR QDIVAGRLPC SFATLALLGS YTIQSELGDY DPELHGVDYV SDFKLAPNQT 

       370        380        390        400        410        420 
KELEEKVMEL HKSYRSMTPA QADLEFLENA KKLSMYGVDL HKAKDLEGVD IILGVCSSGL 

       430        440        450        460        470        480 
LVYKDKLRIN RFPWPKVLKI SYKRSSFFIK IRPGEQEQYE STIGFKLPSY RAAKKLWKVC 

       490        500        510        520        530        540 
VEHHTFFRLT STDTIPKSKF LALGSKFRYS GRTQAQTRQA SALIDRPAPH FERTASKRAS 

       550        560        570        580        590        600 
RSLDGAAAVD SADRSPRPTS APAITQGQVA EGGVLDASAK KTVVPKAQKE TVKAEVKKED 

       610        620        630        640        650        660 
EPPEQAEPEP TEAWKVEKTH IEVTVPTSNG DQTQKLAEKT EDLIRMRKKK RERLDGENIY 

       670        680        690        700        710        720 
IRHSNLMLED LDKSQEEIKK HHASISELKK NFMESVPEPR PSEWDKRLST HSPFRTLNIN 

       730        740        750        760        770        780 
GQIPTGEGPP LVKTQTVTIS DNANAVKSEI PTKDVPIVHT ETKTITYEAA QTDDNSGDLD 

       790        800        810        820        830        840 
PGVLLTAQTI TSETPSSTTT TQITKTVKGG ISETRIEKRI VITGDADIDH DQVLVQAIKE 

       850        860 
AKEQHPDMSV TKVVVHQETE IADE

« Hide

Isoform 2 [UniParc].

Checksum: E09038E1654F9248
Show »

FASTA83193,239
Isoform 3 [UniParc].

Checksum: 0350A4E7EF6E8AE8
Show »

FASTA64171,955
Isoform 4 (Erythroid) [UniParc].

Checksum: D14399077034CFD5
Show »

FASTA58866,399
Isoform 5 (Non-erythroid A) [UniParc].

Checksum: 4A2D98E32CF8552C
Show »

FASTA77586,603
Isoform 6 (Non-erythroid B) [UniParc].

Checksum: 288A47844D5CCE62
Show »

FASTA56663,255
Isoform 7 [UniParc].

Checksum: B2E72F2EB1833585
Show »

FASTA71981,134

References

« Hide 'large scale' references
[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]"Selective expression of an erythroid-specific isoform of protein 4.1."
Tang T.K., Leto T.L., Correas I., Alonso M.A., Marchesi V.T., Benz E.J. Jr.
Proc. Natl. Acad. Sci. U.S.A. 85:3713-3717(1988) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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 SERINE RESIDUES.
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-191; SER-555 AND SER-712, MASS SPECTROMETRY.
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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[24]"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].
[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, MASS SPECTROMETRY.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00003921.
IPI00218697.
IPI00218698.
IPI00218699.
IPI00218700.
IPI00218701.
IPI00553103.
PIRMMHUE4. A39810.
RefSeqNP_001159477.1. NM_001166005.1.
NP_001159478.1. NM_001166006.1.
NP_004428.1. NM_004437.3.
NP_976217.1. NM_203342.2.
UniGeneHs.175437.
Hs.708933.
Hs.712722.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GG3X-ray2.80A/B/C210-488[»]
2RQ1NMR-A292-396[»]
3QIJX-ray1.80A/B211-488[»]
ProteinModelPortalP11171.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-17032N.
IntActP11171. 3 interactions.
MINTMINT-1208648.

PTM databases

GlycoSuiteDBP11171.
PhosphoSiteP11171.

Polymorphism databases

DMDM90101808.

Proteomic databases

PaxDbP11171.
PRIDEP11171.

Protocols and materials databases

DNASU2035.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343067; ENSP00000345259; ENSG00000159023.
ENST00000347529; ENSP00000290100; ENSG00000159023.
ENST00000349460; ENSP00000317597; ENSG00000159023.
ENST00000356093; ENSP00000348397; ENSG00000159023.
ENST00000373797; ENSP00000362903; ENSG00000159023.
ENST00000373798; ENSP00000362904; ENSG00000159023.
ENST00000373800; ENSP00000362906; ENSG00000159023.
GeneID2035.
KEGGhsa:2035.
UCSCuc001brg.2. human.
uc001brh.2. human.
uc001bri.2. human.
uc001brk.3. human.
uc001brl.2. human.
uc001brm.2. human.
uc009vtm.2. human.

Organism-specific databases

CTD2035.
GeneCardsGC01P029213.
HGNCHGNC:3377. EPB41.
HPAHPA028414.
MIM130500. gene.
266140. phenotype.
611804. phenotype.
neXtProtNX_P11171.
Orphanet288. Hereditary elliptocytosis.
PharmGKBPA27810.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG242913.
HOVERGENHBG007777.
InParanoidP11171.
KOK06107.
OMAHEDLTKN.
OrthoDBEOG4K3KVZ.
PhylomeDBP11171.

Enzyme and pathway databases

Pathway_Interaction_DBsyndecan_2_pathway. Syndecan-2-mediated signaling events.

Gene expression databases

ArrayExpressP11171.
BgeeP11171.
CleanExHS_EPB41.
GenevestigatorP11171.
GermOnlineENSG00000159023. Homo sapiens.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR008379. 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.
[Graphical view]
PfamPF05902. 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]
PIRSFPIRSF002304. Membrane_skeletal_4_1. 1 hit.
PRINTSPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTSM00295. B41. 1 hit.
[Graphical view]
SUPFAMSSF47031. FERM_3-hlx. 1 hit.
PROSITEPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEPB41. human.
EvolutionaryTraceP11171.
GenomeRNAi2035.
NextBio8259.
PMAP-CutDBB1ALH9.
SOURCESearch...

Entry information

Entry name41_HUMAN
AccessionPrimary (citable) accession number: P11171
Secondary accession number(s): B1ALH8 expand/collapse secondary AC list , B1ALH9, D3DPM9, D3DPN0, P11176, Q14245, Q5TB35, Q5VXN8, Q8IXV9, Q9Y578, Q9Y579
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 7, 2006
Last modified: May 29, 2013
This is version 159 of the entry and version 4 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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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