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Protein

La-related protein 4

Gene

LARP4

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

Functioni

Plays a role in the regulation of cell morphology and cytoskeletal organization.1 Publication

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • cytoskeleton organization Source: UniProtKB
  • regulation of cell morphogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
La-related protein 4
Alternative name(s):
La ribonucleoprotein domain family member 4
Gene namesi
Name:LARP4
ORF Names:PP13296
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:24320. LARP4.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671566.

Polymorphism and mutation databases

BioMutaiLARP4.
DMDMi189047131.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 724724La-related protein 4PRO_0000207611Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources1 Publication
Modified residuei392 – 3921PhosphoserineCombined sources
Modified residuei505 – 5051PhosphoserineCombined sources
Modified residuei578 – 5781PhosphothreonineCombined sources
Modified residuei579 – 5791PhosphothreonineCombined sources
Modified residuei583 – 5831PhosphoserineCombined sources
Modified residuei597 – 5971PhosphoserineCombined sources
Modified residuei647 – 6471PhosphoserineCombined sources
Modified residuei649 – 6491PhosphothreonineCombined sources
Modified residuei722 – 7221PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ71RC2.
MaxQBiQ71RC2.
PaxDbiQ71RC2.
PeptideAtlasiQ71RC2.
PRIDEiQ71RC2.

PTM databases

iPTMnetiQ71RC2.
PhosphoSiteiQ71RC2.

Miscellaneous databases

PMAP-CutDBQ71RC2.

Expressioni

Gene expression databases

BgeeiQ71RC2.
CleanExiHS_LARP4.
ExpressionAtlasiQ71RC2. baseline and differential.
GenevisibleiQ71RC2. HS.

Organism-specific databases

HPAiHPA039306.
HPA039673.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
BHLHE40O145033EBI-10255841,EBI-711810
CRXO431863EBI-10255841,EBI-748171

Protein-protein interaction databases

BioGridi125238. 24 interactions.
IntActiQ71RC2. 16 interactions.
STRINGi9606.ENSP00000381490.

Structurei

Secondary structure

1
724
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi116 – 13015Combined sources
Helixi133 – 1386Combined sources
Helixi140 – 1456Combined sources
Helixi154 – 1596Combined sources
Helixi161 – 1666Combined sources
Helixi170 – 17910Combined sources
Beta strandi180 – 1856Combined sources
Beta strandi187 – 1948Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQKNMR-A113-200[»]
3PKNX-ray1.80B13-26[»]
ProteinModelPortaliQ71RC2.
SMRiQ71RC2. Positions 113-200.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ71RC2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini113 – 20290HTH La-type RNA-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini203 – 28179RRMAdd
BLAST

Sequence similaritiesi

Contains 1 HTH La-type RNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2591. Eukaryota.
ENOG410XTHK. LUCA.
GeneTreeiENSGT00530000063417.
HOGENOMiHOG000004803.
HOVERGENiHBG055137.
InParanoidiQ71RC2.
KOiK18763.
OMAiPPCTAEL.
OrthoDBiEOG74J971.
PhylomeDBiQ71RC2.
TreeFamiTF321960.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR006630. Lupus_La_RNA-bd.
IPR012677. Nucleotide-bd_a/b_plait.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05383. La. 1 hit.
[Graphical view]
SMARTiSM00715. LA. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS50961. HTH_LA. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q71RC2-1) [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
MLLFVEQVAS KGTGLNPNAK VWQEIAPGNT DATPVTHGTE SSWHEIAATS
60 70 80 90 100
GAHPEGNAEL SEDICKEYEV MYSSSCETTR NTTGIEESTD GMILGPEDLS
110 120 130 140 150
YQIYDVSGES NSAVSTEDLK ECLKKQLEFC FSRENLSKDL YLISQMDSDQ
160 170 180 190 200
FIPIWTVANM EEIKKLTTDP DLILEVLRSS PMVQVDEKGE KVRPSHKRCI
210 220 230 240 250
VILREIPETT PIEEVKGLFK SENCPKVISC EFAHNSNWYI TFQSDTDAQQ
260 270 280 290 300
AFKYLREEVK TFQGKPIMAR IKAINTFFAK NGYRLMDSSI YSHPIQTQAQ
310 320 330 340 350
YASPVFMQPV YNPHQQYSVY SIVPQSWSPN PTPYFETPLA PFPNGSFVNG
360 370 380 390 400
FNSPGSYKTN AAAMNMGRPF QKNRVKPQFR SSGGSEHSTE GSVSLGDGQL
410 420 430 440 450
NRYSSRNFPA ERHNPTVTGH QEQTYLQKET STLQVEQNGD YGRGRRTLFR
460 470 480 490 500
GRRRREDDRI SRPHPSTAES KAPTPKFDLL ASNFPPLPGS SSRMPGELVL
510 520 530 540 550
ENRMSDVVKG VYKEKDNEEL TISCPVPADE QTECTSAQQL NMSTSSPCAA
560 570 580 590 600
ELTALSTTQQ EKDLIEDSSV QKDGLNQTTI PVSPPSTTKP SRASTASPCN
610 620 630 640 650
NNINAATAVA LQEPRKLSYA EVCQKPPKEP SSVLVQPLRE LRSNVVSPTK
660 670 680 690 700
NEDNGAPENS VEKPHEKPEA RASKDYSGFR GNIIPRGAAG KIREQRRQFS
710 720
HRAIPQGVTR RNGKEQYVPP RSPK
Length:724
Mass (Da):80,596
Last modified:May 20, 2008 - v3
Checksum:i93B8C2D8CB3CDAEF
GO
Isoform 2 (identifier: Q71RC2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     7-7: Missing.
     97-194: Missing.
     593-612: Missing.

Note: No experimental confirmation available.
Show »
Length:605
Mass (Da):67,280
Checksum:i8BBA0DFC9487ACD1
GO
Isoform 3 (identifier: Q71RC2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     7-7: Missing.

Note: May be due to competing acceptor splice site. No experimental confirmation available.
Show »
Length:723
Mass (Da):80,468
Checksum:i3FD2F26A384908DB
GO
Isoform 4 (identifier: Q71RC2-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     55-55: E → EVSVFNT

Note: No experimental confirmation available.
Show »
Length:730
Mass (Da):81,244
Checksum:i0E1FED65589E925A
GO
Isoform 5 (identifier: Q71RC2-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     269-339: Missing.

Note: No experimental confirmation available.
Show »
Length:653
Mass (Da):72,400
Checksum:iD425781E3C7E9015
GO
Isoform 6 (identifier: Q71RC2-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     374-444: Missing.

Note: No experimental confirmation available.
Show »
Length:653
Mass (Da):72,734
Checksum:iF31AAD0535BF93B1
GO
Isoform 7 (identifier: Q71RC2-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     446-724: Missing.

Note: No experimental confirmation available.
Show »
Length:445
Mass (Da):49,952
Checksum:iE1E0BF43FCEAC2B0
GO

Sequence cautioni

The sequence BAC86052.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti422 – 4221E → G in BX647457 (PubMed:17974005).Curated
Sequence conflicti529 – 5291D → G in BX647457 (PubMed:17974005).Curated
Sequence conflicti639 – 6391R → Q in BAF84435 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti351 – 3511F → L.
Corresponds to variant rs17124706 [ dbSNP | Ensembl ].
VAR_055936
Natural varianti502 – 5021N → T.1 Publication
Corresponds to variant rs17124715 [ dbSNP | Ensembl ].
VAR_055937

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei7 – 71Missing in isoform 2 and isoform 3. 2 PublicationsVSP_033811
Alternative sequencei55 – 551E → EVSVFNT in isoform 4. 1 PublicationVSP_033812
Alternative sequencei97 – 19498Missing in isoform 2. 1 PublicationVSP_014611Add
BLAST
Alternative sequencei269 – 33971Missing in isoform 5. 1 PublicationVSP_045677Add
BLAST
Alternative sequencei374 – 44471Missing in isoform 6. CuratedVSP_046780Add
BLAST
Alternative sequencei446 – 724279Missing in isoform 7. CuratedVSP_046781Add
BLAST
Alternative sequencei593 – 61220Missing in isoform 2. 1 PublicationVSP_014612Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK055521 mRNA. Translation: BAB70940.1.
AK125113 mRNA. Translation: BAC86052.1. Different initiation.
AK291746 mRNA. Translation: BAF84435.1.
AF370416 mRNA. Translation: AAQ15252.1.
BX647457 mRNA. No translation available.
CR936626 mRNA. Translation: CAI56769.1.
AC090058 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW58146.1.
CH471111 Genomic DNA. Translation: EAW58148.1.
CCDSiCCDS41782.1. [Q71RC2-1]
CCDS44879.2. [Q71RC2-3]
CCDS44880.1. [Q71RC2-5]
CCDS53789.1. [Q71RC2-7]
CCDS53790.1. [Q71RC2-6]
RefSeqiNP_001164279.1. NM_001170808.1. [Q71RC2-6]
NP_443111.4. NM_052879.4. [Q71RC2-1]
NP_954658.2. NM_199188.2. [Q71RC2-3]
NP_954660.1. NM_199190.2. [Q71RC2-5]
XP_005268670.1. XM_005268613.1.
XP_011536132.1. XM_011537830.1. [Q71RC2-4]
XP_011536139.1. XM_011537837.1.
XP_011536140.1. XM_011537838.1.
XP_011536141.1. XM_011537839.1.
XP_011536142.1. XM_011537840.1.
XP_011536143.1. XM_011537841.1.
XP_011536144.1. XM_011537842.1.
UniGeneiHs.26613.

Genome annotation databases

EnsembliENST00000293618; ENSP00000293618; ENSG00000161813. [Q71RC2-6]
ENST00000347328; ENSP00000340901; ENSG00000161813. [Q71RC2-5]
ENST00000398473; ENSP00000381490; ENSG00000161813. [Q71RC2-1]
ENST00000429001; ENSP00000415464; ENSG00000161813. [Q71RC2-4]
ENST00000518444; ENSP00000429077; ENSG00000161813. [Q71RC2-3]
ENST00000522085; ENSP00000429781; ENSG00000161813. [Q71RC2-7]
GeneIDi113251.
KEGGihsa:113251.
UCSCiuc001rwm.4. human. [Q71RC2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK055521 mRNA. Translation: BAB70940.1.
AK125113 mRNA. Translation: BAC86052.1. Different initiation.
AK291746 mRNA. Translation: BAF84435.1.
AF370416 mRNA. Translation: AAQ15252.1.
BX647457 mRNA. No translation available.
CR936626 mRNA. Translation: CAI56769.1.
AC090058 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW58146.1.
CH471111 Genomic DNA. Translation: EAW58148.1.
CCDSiCCDS41782.1. [Q71RC2-1]
CCDS44879.2. [Q71RC2-3]
CCDS44880.1. [Q71RC2-5]
CCDS53789.1. [Q71RC2-7]
CCDS53790.1. [Q71RC2-6]
RefSeqiNP_001164279.1. NM_001170808.1. [Q71RC2-6]
NP_443111.4. NM_052879.4. [Q71RC2-1]
NP_954658.2. NM_199188.2. [Q71RC2-3]
NP_954660.1. NM_199190.2. [Q71RC2-5]
XP_005268670.1. XM_005268613.1.
XP_011536132.1. XM_011537830.1. [Q71RC2-4]
XP_011536139.1. XM_011537837.1.
XP_011536140.1. XM_011537838.1.
XP_011536141.1. XM_011537839.1.
XP_011536142.1. XM_011537840.1.
XP_011536143.1. XM_011537841.1.
XP_011536144.1. XM_011537842.1.
UniGeneiHs.26613.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQKNMR-A113-200[»]
3PKNX-ray1.80B13-26[»]
ProteinModelPortaliQ71RC2.
SMRiQ71RC2. Positions 113-200.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125238. 24 interactions.
IntActiQ71RC2. 16 interactions.
STRINGi9606.ENSP00000381490.

PTM databases

iPTMnetiQ71RC2.
PhosphoSiteiQ71RC2.

Polymorphism and mutation databases

BioMutaiLARP4.
DMDMi189047131.

Proteomic databases

EPDiQ71RC2.
MaxQBiQ71RC2.
PaxDbiQ71RC2.
PeptideAtlasiQ71RC2.
PRIDEiQ71RC2.

Protocols and materials databases

DNASUi113251.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000293618; ENSP00000293618; ENSG00000161813. [Q71RC2-6]
ENST00000347328; ENSP00000340901; ENSG00000161813. [Q71RC2-5]
ENST00000398473; ENSP00000381490; ENSG00000161813. [Q71RC2-1]
ENST00000429001; ENSP00000415464; ENSG00000161813. [Q71RC2-4]
ENST00000518444; ENSP00000429077; ENSG00000161813. [Q71RC2-3]
ENST00000522085; ENSP00000429781; ENSG00000161813. [Q71RC2-7]
GeneIDi113251.
KEGGihsa:113251.
UCSCiuc001rwm.4. human. [Q71RC2-1]

Organism-specific databases

CTDi113251.
GeneCardsiLARP4.
HGNCiHGNC:24320. LARP4.
HPAiHPA039306.
HPA039673.
neXtProtiNX_Q71RC2.
PharmGKBiPA142671566.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2591. Eukaryota.
ENOG410XTHK. LUCA.
GeneTreeiENSGT00530000063417.
HOGENOMiHOG000004803.
HOVERGENiHBG055137.
InParanoidiQ71RC2.
KOiK18763.
OMAiPPCTAEL.
OrthoDBiEOG74J971.
PhylomeDBiQ71RC2.
TreeFamiTF321960.

Miscellaneous databases

ChiTaRSiLARP4. human.
EvolutionaryTraceiQ71RC2.
GeneWikiiLARP4.
GenomeRNAii113251.
PMAP-CutDBQ71RC2.
PROiQ71RC2.

Gene expression databases

BgeeiQ71RC2.
CleanExiHS_LARP4.
ExpressionAtlasiQ71RC2. baseline and differential.
GenevisibleiQ71RC2. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR006630. Lupus_La_RNA-bd.
IPR012677. Nucleotide-bd_a/b_plait.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05383. La. 1 hit.
[Graphical view]
SMARTiSM00715. LA. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS50961. HTH_LA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1 AND 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-724 (ISOFORM 4).
    Tissue: Placenta and Tongue.
  2. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT THR-502.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
    Tissue: Bone marrow and Cervix.
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-11; 166-178; 205-216 AND 494-503, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  7. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-722, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392; SER-583 AND SER-722, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-392, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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-583 AND SER-722, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
    Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
    BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  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-583; SER-647 AND THR-649, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392; SER-505; SER-583; SER-597 AND SER-722, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  19. "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 THR-578; THR-579 AND SER-722, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. "Solution structure of the La domain of c-mpl binding protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 112-199.

Entry informationi

Entry nameiLARP4_HUMAN
AccessioniPrimary (citable) accession number: Q71RC2
Secondary accession number(s): A8K6T1
, E9PDG5, G3XAA8, G5E976, Q5CZ97, Q6ZV14, Q96NF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: May 20, 2008
Last modified: July 6, 2016
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.