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Protein

Band 4.1-like protein 2

Gene

EPB41L2

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

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Band 4.1-like protein 2
Alternative name(s):
Generally expressed protein 4.1
Short name:
4.1G
Gene namesi
Name:EPB41L2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:3379. EPB41L2.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: HPA
  • extracellular exosome Source: UniProtKB
  • extrinsic component of membrane Source: InterPro
  • focal adhesion Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: HPA
  • plasma membrane Source: HPA
  • spectrin Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27812.

Polymorphism and mutation databases

BioMutaiEPB41L2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 10051004Band 4.1-like protein 2PRO_0000219397Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineCombined sources1 Publication
Modified residuei39 – 391PhosphoserineCombined sources
Modified residuei58 – 581PhosphoserineCombined sources
Modified residuei87 – 871PhosphoserineCombined sources
Modified residuei89 – 891PhosphothreonineCombined sources
Cross-linki144 – 144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei208 – 2081PhosphoserineBy similarity
Modified residuei386 – 3861PhosphoserineCombined sources
Modified residuei402 – 4021PhosphoserineBy similarity
Modified residuei499 – 4991PhosphoserineCombined sources
Modified residuei550 – 5501PhosphoserineCombined sources
Modified residuei562 – 5621PhosphoserineBy similarity
Modified residuei575 – 5751PhosphoserineBy similarity
Modified residuei598 – 5981PhosphoserineBy similarity
Modified residuei614 – 6141PhosphoserineCombined sources
Modified residuei623 – 6231PhosphotyrosineBy similarity
Modified residuei627 – 6271PhosphoserineBy similarity
Modified residuei647 – 6471PhosphoserineBy similarity
Modified residuei715 – 7151PhosphoserineCombined sources
Modified residuei718 – 7181PhosphoserineCombined sources
Modified residuei763 – 7631PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO43491.
MaxQBiO43491.
PaxDbiO43491.
PRIDEiO43491.
TopDownProteomicsiO43491-3. [O43491-3]

PTM databases

iPTMnetiO43491.
PhosphoSiteiO43491.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiO43491.
CleanExiHS_EPB41L2.
ExpressionAtlasiO43491. baseline and differential.
GenevisibleiO43491. HS.

Organism-specific databases

HPAiHPA005730.
HPA006642.

Interactioni

Subunit structurei

Interacts with FCGR1A. Interacts with TRPC4. The CTD domain interacts with FKBP2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi108351. 50 interactions.
DIPiDIP-17034N.
IntActiO43491. 26 interactions.
MINTiMINT-5003841.
STRINGi9606.ENSP00000338481.

Structurei

3D structure databases

ProteinModelPortaliO43491.
SMRiO43491. Positions 216-498.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini218 – 499282FERMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni502 – 610109HydrophilicAdd
BLAST
Regioni611 – 67666Spectrin--actin-bindingAdd
BLAST
Regioni855 – 1005151C-terminal (CTD)Add
BLAST

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3527. Eukaryota.
ENOG410Y7NQ. LUCA.
GeneTreeiENSGT00760000118823.
HOGENOMiHOG000228841.
HOVERGENiHBG007777.
InParanoidiO43491.
KOiK06107.
OMAiQAEVGKD.
OrthoDBiEOG7Z69BP.
PhylomeDBiO43491.
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.
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_dom-like.
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]
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
SM01195. FA. 1 hit.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O43491-1) [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
MTTEVGSVSE VKKDSSQLGT DATKEKPKEV AENQQNQSSD PEEEKGSQPP
60 70 80 90 100
PAAESQSSLR RQKREKETSE SRGISRFIPP WLKKQKSYTL VVAKDGGDKK
110 120 130 140 150
EPTQAVVEEQ VLDKEEPLPE EQRQAKGDAE EMAQKKQEIK VEVKEEKPSV
160 170 180 190 200
SKEEKPSVSK VEMQPTELVS KEREEKVKET QEDKLEGGAA KRETKEVQTN
210 220 230 240 250
ELKAEKASQK VTKKTKTVQC KVTLLDGTEY SCDLEKHAKG QVLFDKVCEH
260 270 280 290 300
LNLLEKDYFG LLFQESPEQK NWLDPAKEIK RQLRNLPWLF TFNVKFYPPD
310 320 330 340 350
PSQLTEDITR YFLCLQLRQD IASGRLPCSF VTHALLGSYT LQAELGDYDP
360 370 380 390 400
EEHGSIDLSE FQFAPTQTKE LEEKVAELHK THRGLSPAQA DSQFLENAKR
410 420 430 440 450
LSMYGVDLHH AKDSEGVDIK LGVCANGLLI YKDRLRINRF AWPKILKISY
460 470 480 490 500
KRSNFYIKVR PAELEQFEST IGFKLPNHRA AKRLWKVCVE HHTFYRLVSP
510 520 530 540 550
EQPPKAKFLT LGSKFRYSGR TQAQTRQAST LIDRPAPHFE RTSSKRVSRS
560 570 580 590 600
LDGAPIGVMD QSLMKDFPGA AGEISAYGPG LVSIAVVQDG DGRREVRSPT
610 620 630 640 650
KAPHLQLIEG KKNSLRVEGD NIYVRHSNLM LEELDKAQED ILKHQASISE
660 670 680 690 700
LKRNFMESTP EPRPNEWEKR RITPLSLQTQ GSSHETLNIV EEKKRAEVGK
710 720 730 740 750
DERVITEEMN GKEISPGSGP GEIRKVEPVT QKDSTSLSSE SSSSSSESEE
760 770 780 790 800
EDVGEYRPHH RVTEGTIREE QEYEEEVEEE PRPAAKVVER EEAVPEASPV
810 820 830 840 850
TQAGASVITV ETVIQENVGA QKIPGEKSVH EGALKQDMGE EAEEEPQKVN
860 870 880 890 900
GEVSHVDIDV LPQIICCSEP PVVKTEMVTI SDASQRTEIS TKEVPIVQTE
910 920 930 940 950
TKTITYESPQ IDGGAGGDSG TLLTAQTITS ESVSTTTTTH ITKTVKGGIS
960 970 980 990 1000
ETRIEKRIVI TGDGDIDHDQ ALAQAIREAR EQHPDMSVTR VVVHKETELA

EEGED
Length:1,005
Mass (Da):112,588
Last modified:June 1, 1998 - v1
Checksum:iE86CB17488F6045F
GO
Isoform 2 (identifier: O43491-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     612-943: Missing.

Note: No experimental confirmation available.
Show »
Length:673
Mass (Da):76,053
Checksum:iFE88398B4AC18A0B
GO
Isoform 3 (identifier: O43491-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     612-869: Missing.

Note: No experimental confirmation available.
Show »
Length:747
Mass (Da):83,803
Checksum:iB5F08A014E5AD5A9
GO
Isoform 4 (identifier: O43491-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     612-681: Missing.
     787-869: Missing.

Note: No experimental confirmation available. Gene prediction based on cDNA data.
Show »
Length:852
Mass (Da):95,542
Checksum:iCACB03447C7ED78B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171Q → H.
Corresponds to variant rs2297852 [ dbSNP | Ensembl ].
VAR_020145

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei612 – 943332Missing in isoform 2. 1 PublicationVSP_042910Add
BLAST
Alternative sequencei612 – 869258Missing in isoform 3. 1 PublicationVSP_045090Add
BLAST
Alternative sequencei612 – 68170Missing in isoform 4. CuratedVSP_047181Add
BLAST
Alternative sequencei787 – 86983Missing in isoform 4. CuratedVSP_047182Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027299 mRNA. Translation: AAC16923.1.
AY047584 mRNA. Translation: AAK95850.1.
AK295124 mRNA. Translation: BAG58150.1.
CR749262 mRNA. Translation: CAH18118.1.
AL109938 Genomic DNA. No translation available.
AL357496 Genomic DNA. No translation available.
AL358943, AL355360 Genomic DNA. Translation: CAI20310.1.
AL590014 Genomic DNA. No translation available.
CH471051 Genomic DNA. Translation: EAW48062.1.
CCDSiCCDS47474.1. [O43491-2]
CCDS5141.1. [O43491-1]
CCDS56450.1. [O43491-4]
CCDS59037.1. [O43491-3]
RefSeqiNP_001129026.1. NM_001135554.1. [O43491-2]
NP_001129027.1. NM_001135555.3. [O43491-2]
NP_001239589.1. NM_001252660.1. [O43491-3]
NP_001422.1. NM_001431.3. [O43491-1]
XP_011533832.1. XM_011535530.1. [O43491-4]
XP_011533836.1. XM_011535534.1. [O43491-3]
UniGeneiHs.486470.
Hs.708219.

Genome annotation databases

EnsembliENST00000337057; ENSP00000338481; ENSG00000079819. [O43491-1]
ENST00000368128; ENSP00000357110; ENSG00000079819. [O43491-1]
ENST00000392427; ENSP00000376222; ENSG00000079819. [O43491-2]
ENST00000445890; ENSP00000402041; ENSG00000079819. [O43491-3]
ENST00000525271; ENSP00000432803; ENSG00000079819. [O43491-2]
ENST00000528282; ENSP00000434308; ENSG00000079819. [O43491-3]
ENST00000530481; ENSP00000434576; ENSG00000079819. [O43491-4]
GeneIDi2037.
KEGGihsa:2037.
UCSCiuc003qcg.2. human. [O43491-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027299 mRNA. Translation: AAC16923.1.
AY047584 mRNA. Translation: AAK95850.1.
AK295124 mRNA. Translation: BAG58150.1.
CR749262 mRNA. Translation: CAH18118.1.
AL109938 Genomic DNA. No translation available.
AL357496 Genomic DNA. No translation available.
AL358943, AL355360 Genomic DNA. Translation: CAI20310.1.
AL590014 Genomic DNA. No translation available.
CH471051 Genomic DNA. Translation: EAW48062.1.
CCDSiCCDS47474.1. [O43491-2]
CCDS5141.1. [O43491-1]
CCDS56450.1. [O43491-4]
CCDS59037.1. [O43491-3]
RefSeqiNP_001129026.1. NM_001135554.1. [O43491-2]
NP_001129027.1. NM_001135555.3. [O43491-2]
NP_001239589.1. NM_001252660.1. [O43491-3]
NP_001422.1. NM_001431.3. [O43491-1]
XP_011533832.1. XM_011535530.1. [O43491-4]
XP_011533836.1. XM_011535534.1. [O43491-3]
UniGeneiHs.486470.
Hs.708219.

3D structure databases

ProteinModelPortaliO43491.
SMRiO43491. Positions 216-498.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108351. 50 interactions.
DIPiDIP-17034N.
IntActiO43491. 26 interactions.
MINTiMINT-5003841.
STRINGi9606.ENSP00000338481.

PTM databases

iPTMnetiO43491.
PhosphoSiteiO43491.

Polymorphism and mutation databases

BioMutaiEPB41L2.

Proteomic databases

EPDiO43491.
MaxQBiO43491.
PaxDbiO43491.
PRIDEiO43491.
TopDownProteomicsiO43491-3. [O43491-3]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337057; ENSP00000338481; ENSG00000079819. [O43491-1]
ENST00000368128; ENSP00000357110; ENSG00000079819. [O43491-1]
ENST00000392427; ENSP00000376222; ENSG00000079819. [O43491-2]
ENST00000445890; ENSP00000402041; ENSG00000079819. [O43491-3]
ENST00000525271; ENSP00000432803; ENSG00000079819. [O43491-2]
ENST00000528282; ENSP00000434308; ENSG00000079819. [O43491-3]
ENST00000530481; ENSP00000434576; ENSG00000079819. [O43491-4]
GeneIDi2037.
KEGGihsa:2037.
UCSCiuc003qcg.2. human. [O43491-1]

Organism-specific databases

CTDi2037.
GeneCardsiEPB41L2.
HGNCiHGNC:3379. EPB41L2.
HPAiHPA005730.
HPA006642.
MIMi603237. gene.
neXtProtiNX_O43491.
PharmGKBiPA27812.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3527. Eukaryota.
ENOG410Y7NQ. LUCA.
GeneTreeiENSGT00760000118823.
HOGENOMiHOG000228841.
HOVERGENiHBG007777.
InParanoidiO43491.
KOiK06107.
OMAiQAEVGKD.
OrthoDBiEOG7Z69BP.
PhylomeDBiO43491.
TreeFamiTF351626.

Miscellaneous databases

ChiTaRSiEPB41L2. human.
GeneWikiiEPB41L2.
GenomeRNAii2037.
NextBioi8273.
PROiO43491.
SOURCEiSearch...

Gene expression databases

BgeeiO43491.
CleanExiHS_EPB41L2.
ExpressionAtlasiO43491. baseline and differential.
GenevisibleiO43491. HS.

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.
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_dom-like.
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]
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
SM01195. FA. 1 hit.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of 4.1G (EPB41L2), a new member of the skeletal protein 4.1 (EPB41) gene family."
    Parra M., Gascard P., Walensky L.D., Snyder S.H., Mohandas N., Conboy J.G.
    Genomics 49:298-306(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain and Heart.
  2. Liu J., Zhou Y., Zhang B., Peng X., Yuan J., Qiang B.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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 2).
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Retina.
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: PROTEIN SEQUENCE OF 2-13; 161-171; 508-514 AND 875-886, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma and Pre-B cell.
  8. "Activation of the endothelial store-operated ISOC Ca2+ channel requires interaction of protein 4.1 with TRPC4."
    Cioffi D.L., Wu S., Alexeyev M., Goodman S.R., Zhu M.X., Stevens T.
    Circ. Res. 97:1164-1172(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRPC4.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: INTERACTION WITH FCGR1A.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550 AND SER-614, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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-87; THR-89; SER-499; SER-550; SER-715 AND SER-718, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-39; SER-87; THR-89 AND SER-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Systematic validation of antibody binding and protein subcellular localization using siRNA and confocal microscopy."
    Stadler C., Hjelmare M., Neumann B., Jonasson K., Pepperkok R., Uhlen M., Lundberg E.
    J. Proteomics 75:2236-2251(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  19. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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-58; SER-550 AND SER-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-144, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiE41L2_HUMAN
AccessioniPrimary (citable) accession number: O43491
Secondary accession number(s): B4DHI8
, E9PPD9, Q5T4F0, Q68DV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 154 of the entry and version 1 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 6
    Human chromosome 6: 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.