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

Names and origin

Protein names

Recommended name:
    Protein 4.1
Alternative name(s):
    Band 4.1
    P4.1
    EPB4.1
    4.1R

Gene names

Name:	EPB41
Synonyms:	E41P

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	864 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.18
Post-translational modification	Phosphorylated at multiple sites by different protein kinases and each phosphorylation event selectively modulates the protein's functions. Ref.10 Ref.13 Ref.19 Ref.20 Ref.21 Ref.22 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.12
Involvement in disease	Defects in EPB41 are the cause of elliptocytosis type 1 (EL1) [MIM:611804]. EL1 is 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. Defects in EPB41 are a cause of hereditary pyropoikilocytosis (HPP) [MIM:266140]. HPP is an autosomal recessive hematologic disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells.
Sequence similarities	Contains 1 FERM domain.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Elliptocytosis Hereditary hemolytic anemia Pyropoikilocytosis
Ligand	Actin-binding
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	blood circulation Traceable author statement. Source: ProtInc cortical actin cytoskeleton organization Inferred from electronic annotation. Source: InterPro positive regulation of protein binding Inferred from direct assay. Source: UniProtKB
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: InterPro nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Traceable author statement. Source: ProtInc protein complex Inferred from direct assay. Source: UniProtKB spectrin Traceable author statement. Source: ProtInc spectrin-associated cytoskeleton Traceable author statement. Source: UniProtKB
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol binding Inferred from direct assay. Source: UniProtKB spectrin binding Traceable author statement. Source: UniProtKB structural constituent of cytoskeleton Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CACYBP	Q9HB71	1	EBI-1050906,EBI-1047302
CALR	P27797	1	EBI-1050906,EBI-1049597
CASK	O14936	1	EBI-1050906,EBI-1215506
CDK2	P24941	1	EBI-1050906,EBI-375096
ECHS1	P30084	1	EBI-1050906,EBI-719602
MYH9	P35579	1	EBI-1050906,EBI-350338
PAICS	P22234	1	EBI-1050906,EBI-712261
PFAS	O15067	1	EBI-1050906,EBI-1052653
TAGLN2	P37802	1	EBI-1050906,EBI-1056740
VARS	P26640	1	EBI-1050906,EBI-355765

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 864

864

Protein 4.1

PRO_0000219390

Regions

Domain

210 – 491

282

FERM

Region

494 – 614

121

Hydrophilic

Region

615 – 713

99

Spectrin--actin-binding

Region

714 – 864

151

Carboxyl-terminal (CTD)

Amino acid modifications

Modified residue

60

1

Phosphothreonine; by CDC2 Ref.10 Ref.19

Modified residue

92

1

Phosphoserine Ref.10 Ref.20

Modified residue

188

1

Phosphoserine Ref.10 Ref.22

Modified residue

191

1

Phosphoserine Ref.10 Ref.22

Modified residue

222

1

Phosphotyrosine By similarity

Modified residue

540

1

Phosphoserine By similarity

Modified residue

542

1

Phosphoserine By similarity

Modified residue

555

1

Phosphoserine Ref.10 Ref.22

Modified residue

660

1

Phosphotyrosine; by EGFR Ref.10 Ref.13

Modified residue

674

1

Phosphoserine By similarity

Modified residue

712

1

Phosphoserine; by CDC2 Ref.10 Ref.19 Ref.21 Ref.22

Natural variations

Alternative sequence

1 – 209

209

Missing in isoform 3, isoform 4 and isoform 6.

VSP_000468

Alternative sequence

228 – 262

35

Missing in isoform 5 and isoform 6.

VSP_000469

Alternative sequence

616 – 648

33

Missing in isoform 2, isoform 4, isoform 5 and isoform 6.

VSP_000470

Alternative sequence

635 – 648

14

Missing in isoform 3 and isoform 7.

VSP_000471

Alternative sequence

649 – 669

21

Missing in isoform 5 and isoform 6.

VSP_000472

Alternative sequence

729 – 733

5

PPLVK → VSTLS in isoform 7.

VSP_012872

Alternative sequence

734 – 864

131

Missing in isoform 7.

VSP_012873

Alternative sequence

772 – 805

34

Missing in isoform 4.

VSP_000473

Natural variant

214

1

V → I Ref.8

VAR_009122

Experimental info

Mutagenesis

60

1

T → A: Loss of CDC2-mediated phosphorylation. Abolishes targeting onto the mitotic spindle; when associated with A-712. Ref.19

Mutagenesis

712

1

S → A: Loss of CDC2-mediated phosphorylation. Abolishes targeting onto the mitotic spindle; when associated with A-60. Ref.19

Sequence conflict

51

1

Q → H in AAD42222. Ref.5

Sequence conflict

76

1

S → N in AAD42222. Ref.5

Sequence conflict

168

1

F → S in AAD42223. Ref.8

Sequence conflict

259

1

A → T in AAD42222. Ref.5

Sequence conflict

665

1

N → S in AAD42222. Ref.5

Sequence conflict

669

1

E → K Ref.9

Sequence conflict

679

1

K → E in AAD42222. Ref.5

Sequence conflict

802

1

Q → K Ref.2

Sequence conflict

802

1

Q → K Ref.3

Sequence conflict

802

1

Q → K Ref.7

Sequence conflict

802

1

Q → K Ref.9

Sequence conflict

852

1

K → L Ref.9

Sequence conflict

863

1

D → E Ref.9

Secondary structure

1

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864

Helix Strand Turn

Details...

Beta strand

211 – 215

5

Beta strand

221 – 225

5

Helix

232 – 243

12

Beta strand

250 – 252

3

Beta strand

254 – 256

3

Beta strand

259 – 261

3

Helix

271 – 274

4

Turn

275 – 277

3

Beta strand

280 – 285

6

Helix

293 – 295

3

Helix

299 – 314

16

Helix

322 – 337

16

Helix

350 – 352

3

Helix

361 – 373

13

Helix

379 – 392

14

Turn

394 – 397

4

Beta strand

399 – 402

4

Beta strand

412 – 426

15

Beta strand

430 – 433

4

Helix

434 – 436

3

Beta strand

439 – 443

5

Beta strand

446 – 450

5

Beta strand

454 – 458

5

Beta strand

462 – 466

5

Helix

470 – 486

17

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 7, 2006. Version 4. Checksum: B466E7A9D7FBF12B	FASTA	864	97,017
	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
	Isoform 2. Checksum: E09038E1654F9248	FASTA	831	93,239
	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 TEAWKKKRER LDGENIYIRH SNLMLEDLDK SQEEIKKHHA SISELKKNFM 670 680 690 700 710 720 ESVPEPRPSE WDKRLSTHSP FRTLNINGQI PTGEGPPLVK TQTVTISDNA NAVKSEIPTK 730 740 750 760 770 780 DVPIVHTETK TITYEAAQTD DNSGDLDPGV LLTAQTITSE TPSSTTTTQI TKTVKGGISE 790 800 810 820 830 TRIEKRIVIT GDADIDHDQV LVQAIKEAKE QHPDMSVTKV VVHQETEIAD E
	Isoform 3. Checksum: 0350A4E7EF6E8AE8	FASTA	641	71,955
	10 20 30 40 50 60 MHCKVSLLDD TVYECVVEKH AKGQDLLKRV CEHLNLLEED YFGLAIWDNA TSKTWLDSAK 70 80 90 100 110 120 EIKKQVRGVP WNFTFNVKFY PPDPAQLTED ITRYYLCLQL RQDIVAGRLP CSFATLALLG 130 140 150 160 170 180 SYTIQSELGD YDPELHGVDY VSDFKLAPNQ TKELEEKVME LHKSYRSMTP AQADLEFLEN 190 200 210 220 230 240 AKKLSMYGVD LHKAKDLEGV DIILGVCSSG LLVYKDKLRI NRFPWPKVLK ISYKRSSFFI 250 260 270 280 290 300 KIRPGEQEQY ESTIGFKLPS YRAAKKLWKV CVEHHTFFRL TSTDTIPKSK FLALGSKFRY 310 320 330 340 350 360 SGRTQAQTRQ ASALIDRPAP HFERTASKRA SRSLDGAAAV DSADRSPRPT SAPAITQGQV 370 380 390 400 410 420 AEGGVLDASA KKTVVPKAQK ETVKAEVKKE DEPPEQAEPE PTEAWKVEKT HIEVTVPTSN 430 440 450 460 470 480 GDQTQKKRER LDGENIYIRH SNLMLEDLDK SQEEIKKHHA SISELKKNFM ESVPEPRPSE 490 500 510 520 530 540 WDKRLSTHSP FRTLNINGQI PTGEGPPLVK TQTVTISDNA NAVKSEIPTK DVPIVHTETK 550 560 570 580 590 600 TITYEAAQTD DNSGDLDPGV LLTAQTITSE TPSSTTTTQI TKTVKGGISE TRIEKRIVIT 610 620 630 640 GDADIDHDQV LVQAIKEAKE QHPDMSVTKV VVHQETEIAD E
	Isoform 4 (Erythroid). Checksum: D14399077034CFD5	FASTA	588	66,399
	10 20 30 40 50 60 MHCKVSLLDD TVYECVVEKH AKGQDLLKRV CEHLNLLEED YFGLAIWDNA TSKTWLDSAK 70 80 90 100 110 120 EIKKQVRGVP WNFTFNVKFY PPDPAQLTED ITRYYLCLQL RQDIVAGRLP CSFATLALLG 130 140 150 160 170 180 SYTIQSELGD YDPELHGVDY VSDFKLAPNQ TKELEEKVME LHKSYRSMTP AQADLEFLEN 190 200 210 220 230 240 AKKLSMYGVD LHKAKDLEGV DIILGVCSSG LLVYKDKLRI NRFPWPKVLK ISYKRSSFFI 250 260 270 280 290 300 KIRPGEQEQY ESTIGFKLPS YRAAKKLWKV CVEHHTFFRL TSTDTIPKSK FLALGSKFRY 310 320 330 340 350 360 SGRTQAQTRQ ASALIDRPAP HFERTASKRA SRSLDGAAAV DSADRSPRPT SAPAITQGQV 370 380 390 400 410 420 AEGGVLDASA KKTVVPKAQK ETVKAEVKKE DEPPEQAEPE PTEAWKKKRE RLDGENIYIR 430 440 450 460 470 480 HSNLMLEDLD KSQEEIKKHH ASISELKKNF MESVPEPRPS EWDKRLSTHS PFRTLNINGQ 490 500 510 520 530 540 IPTGEGPPLV KTQTVTISDN ANAVKSEIPT KDVPIVHTET KTITYEAAQT VKGGISETRI 550 560 570 580 EKRIVITGDA DIDHDQVLVQ AIKEAKEQHP DMSVTKVVVH QETEIADE
	Isoform 5 (Non-erythroid A). Checksum: 4A2D98E32CF8552C	FASTA	775	86,603
	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 VYECVVETWL DSAKEIKKQV 250 260 270 280 290 300 RGVPWNFTFN VKFYPPDPAQ LTEDITRYYL CLQLRQDIVA GRLPCSFATL ALLGSYTIQS 310 320 330 340 350 360 ELGDYDPELH GVDYVSDFKL APNQTKELEE KVMELHKSYR SMTPAQADLE FLENAKKLSM 370 380 390 400 410 420 YGVDLHKAKD LEGVDIILGV CSSGLLVYKD KLRINRFPWP KVLKISYKRS SFFIKIRPGE 430 440 450 460 470 480 QEQYESTIGF KLPSYRAAKK LWKVCVEHHT FFRLTSTDTI PKSKFLALGS KFRYSGRTQA 490 500 510 520 530 540 QTRQASALID RPAPHFERTA SKRASRSLDG AAAVDSADRS PRPTSAPAIT QGQVAEGGVL 550 560 570 580 590 600 DASAKKTVVP KAQKETVKAE VKKEDEPPEQ AEPEPTEAWK DLDKSQEEIK KHHASISELK 610 620 630 640 650 660 KNFMESVPEP RPSEWDKRLS THSPFRTLNI NGQIPTGEGP PLVKTQTVTI SDNANAVKSE 670 680 690 700 710 720 IPTKDVPIVH TETKTITYEA AQTDDNSGDL DPGVLLTAQT ITSETPSSTT TTQITKTVKG 730 740 750 760 770 GISETRIEKR IVITGDADID HDQVLVQAIK EAKEQHPDMS VTKVVVHQET EIADE
	Isoform 6 (Non-erythroid B). Checksum: 288A47844D5CCE62	FASTA	566	63,255
	10 20 30 40 50 60 MHCKVSLLDD TVYECVVETW LDSAKEIKKQ VRGVPWNFTF NVKFYPPDPA QLTEDITRYY 70 80 90 100 110 120 LCLQLRQDIV AGRLPCSFAT LALLGSYTIQ SELGDYDPEL HGVDYVSDFK LAPNQTKELE 130 140 150 160 170 180 EKVMELHKSY RSMTPAQADL EFLENAKKLS MYGVDLHKAK DLEGVDIILG VCSSGLLVYK 190 200 210 220 230 240 DKLRINRFPW PKVLKISYKR SSFFIKIRPG EQEQYESTIG FKLPSYRAAK KLWKVCVEHH 250 260 270 280 290 300 TFFRLTSTDT IPKSKFLALG SKFRYSGRTQ AQTRQASALI DRPAPHFERT ASKRASRSLD 310 320 330 340 350 360 GAAAVDSADR SPRPTSAPAI TQGQVAEGGV LDASAKKTVV PKAQKETVKA EVKKEDEPPE 370 380 390 400 410 420 QAEPEPTEAW KDLDKSQEEI KKHHASISEL KKNFMESVPE PRPSEWDKRL STHSPFRTLN 430 440 450 460 470 480 INGQIPTGEG PPLVKTQTVT ISDNANAVKS EIPTKDVPIV HTETKTITYE AAQTDDNSGD 490 500 510 520 530 540 LDPGVLLTAQ TITSETPSST TTTQITKTVK GGISETRIEK RIVITGDADI DHDQVLVQAI 550 560 KEAKEQHPDM SVTKVVVHQE TEIADE
	Isoform 7. Checksum: B2E72F2EB1833585	FASTA	719	81,134
	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 DQTQKKRERL DGENIYIRHS NLMLEDLDKS 670 680 690 700 710 QEEIKKHHAS ISELKKNFME SVPEPRPSEW DKRLSTHSPF RTLNINGQIP TGEGVSTLS

References

	« Hide 'large scale' referencesShow '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: 3467321] [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: 3223413] [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: 3375238] [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: 2022644] [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: 16710414] [Abstract] 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). Tissue: Brain.
[8]	"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.
[9]	"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: 3194408] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 669-864 (ISOFORM 4), ALTERNATIVE SPLICING.
[10]	"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: 2171679] [Abstract] Cited for: PROTEIN SEQUENCE OF 534-541; 693-701 AND 793-794, PHOSPHORYLATION AT SERINE RESIDUES.
[11]	"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: 3531202] [Abstract] Cited for: PROTEIN SEQUENCE OF 648-714.
[12]	"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: 2808371] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATES.
[13]	"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: 1647028] [Abstract] Cited for: PHOSPHORYLATION AT TYR-660.
[14]	"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: 7937897] [Abstract] Cited for: INTERACTION WITH DLG1.
[15]	"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: 10692436] [Abstract] Cited for: INTERACTION WITH CALMODULIN.
[16]	"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: 11003675] [Abstract] Cited for: INTERACTION WITH CENPJ.
[17]	"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: 11432737] [Abstract] Cited for: CHARACTERIZATION OF C-TERMINAL DOMAIN.
[18]	"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: 12427749] [Abstract] Cited for: SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
[19]	"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: 15525677] [Abstract] Cited for: MUTAGENESIS OF THR-60 AND SER-712, PHOSPHORYLATION AT THR-60 AND SER-712.
[20]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, MASS SPECTROMETRY.
[21]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-712, MASS SPECTROMETRY.
[22]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-191; SER-555 AND SER-712, MASS SPECTROMETRY.
[23]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[24]	"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: 11017195] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 210-488.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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: 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.
BC039079 mRNA. Translation: AAH39079.1.
AF156226 Genomic DNA. Translation: AAD42223.1.

IPI

IPI00003921.
IPI00218697.
IPI00218698.
IPI00218699.
IPI00218700.
IPI00218701.
IPI00553103.

PIR

MMHUE4. A39810.

RefSeq

NP_004428.1.
NP_976217.1.

UniGene

Hs.175437
Hs.708933

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GG3	X-ray	2.80	A/B/C	210-488	[»]
2RQ1	NMR	-	A	292-396	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:17032N.

IntAct

P11171. 100 interactions.

PTM databases

GlycoSuiteDB

P11171.

PhosphoSite

P11171.

Proteomic databases

PRIDE

P11171.

Genome annotation databases

Ensembl

ENSG00000159023. Homo sapiens. [Contig view]

GeneID

2035.

KEGG

hsa:2035.

NMPDR

fig|9606.3.peg.705.

UCSC

uc001brg.1. human.
uc001brh.1. human.
uc001bri.1. human.
uc001brk.2. human.
uc001brm.1. human.

Organism-specific databases

GeneCards

GC01P029034.

H-InvDB

HIX0000342.

HGNC

HGNC:3377. EPB41.

MIM

130500. gene.
266140. phenotype.
611804. phenotype.

Orphanet

288. Elliptocytosis, hereditary.

PharmGKB

PA27810.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P11171.

OMA

P11171. GEGLEEC.

Enzyme and pathway databases

Pathway_Interaction_DB

syndecan_2_pathway. Syndecan-2-mediated signaling events.

Gene expression databases

ArrayExpress

P11171.

Bgee

P11171.

CleanEx

HS_EPB41.

GermOnline

ENSG00000159023. Homo sapiens.

Family and domain databases

InterPro

IPR008379. Band_4.1_C.
IPR019749. Band_41_domain.
IPR019750. Band_41_sg.
IPR000798. Ez/rad/moesin.
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_type.
IPR007477. SAB.
[Graphical view]

Gene3D

G3DSA:1.20.80.10. ACBP. 1 hit.
G3DSA:2.30.29.30. PH_type. 1 hit.

Pfam

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]

PRINTS

PR00935. BAND41.
PR00661. ERMFAMILY.

SMART

SM00295. B41. 1 hit.
[Graphical view]

PROSITE

PS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

8259.

PMAP-CutDB

P11171.

SOURCE

Search...

Entry information

Entry name

41_HUMAN

Accession

Primary (citable) accession number: P11171
Secondary accession number(s): B1ALH8 , 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:	July 7, 2009
This is version 122 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)