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Protein

Kin of IRRE-like protein 1

Gene

KIRREL

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

Functioni

Plays a significant role in the normal development and function of the glomerular permeability. Signaling protein that needs the presence of TEC kinases to fully trans-activate the transcription factor AP-1 (By similarity).By similarity

GO - Molecular functioni

  • myosin binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-373753. Nephrin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Kin of IRRE-like protein 1
Alternative name(s):
Kin of irregular chiasm-like protein 1
Nephrin-like protein 1
Gene namesi
Name:KIRREL
Synonyms:KIRREL1, NEPH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:15734. KIRREL.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini17 – 499483ExtracellularSequence analysisAdd
BLAST
Transmembranei500 – 52021HelicalSequence analysisAdd
BLAST
Topological domaini521 – 757237CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell-cell junction Source: UniProtKB
  • cell projection membrane Source: Ensembl
  • dendritic shaft Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • membrane raft Source: Ensembl
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30126.

Polymorphism and mutation databases

DMDMi54036152.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Chaini17 – 757741Kin of IRRE-like protein 1PRO_0000015093Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 100PROSITE-ProRule annotation
Glycosylationi46 – 461N-linked (GlcNAc...)Sequence analysis
Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence analysis
Disulfide bondi143 ↔ 200PROSITE-ProRule annotation
Disulfide bondi244 ↔ 287PROSITE-ProRule annotation
Glycosylationi297 – 2971N-linked (GlcNAc...)1 Publication
Disulfide bondi329 ↔ 371PROSITE-ProRule annotation
Disulfide bondi413 ↔ 472PROSITE-ProRule annotation
Glycosylationi471 – 4711N-linked (GlcNAc...)Sequence analysis
Modified residuei574 – 5741PhosphoserineCombined sources
Modified residuei605 – 6051Phosphotyrosine; by FYNBy similarity
Modified residuei606 – 6061Phosphotyrosine; by FYNBy similarity
Modified residuei622 – 6221PhosphotyrosineCombined sources
Modified residuei625 – 6251PhosphotyrosineCombined sources
Modified residuei724 – 7241PhosphotyrosineCombined sources

Post-translational modificationi

Phosphorylation probably regulates the interaction with NSH2. Phosphorylated at Tyr-605 and Tyr-606 by FYN, leading to GRB2 binding (By similarity).By similarity
N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ96J84.
MaxQBiQ96J84.
PaxDbiQ96J84.
PeptideAtlasiQ96J84.
PRIDEiQ96J84.

PTM databases

iPTMnetiQ96J84.
PhosphoSiteiQ96J84.

Expressioni

Tissue specificityi

Abundantly expressed in kidney. Specifically expressed in podocytes of kidney glomeruli.1 Publication

Gene expression databases

BgeeiQ96J84.
CleanExiHS_KIRREL.
ExpressionAtlasiQ96J84. baseline and differential.
GenevisibleiQ96J84. HS.

Organism-specific databases

HPAiHPA003501.
HPA030458.

Interactioni

Subunit structurei

Interacts with TJP1/ZO-1 and with NPHS2/podocin (via the C-terminus). Interacts with NPHS1/nephrin (via the Ig-like domains); this interaction is dependent on KIRREL glycosylation. Homodimer (via the Ig-like domains). Interacts when tyrosine-phosphorylated with GRB2 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
TJP1Q071577EBI-3988456,EBI-79553

GO - Molecular functioni

  • myosin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120534. 25 interactions.
IntActiQ96J84. 5 interactions.
STRINGi9606.ENSP00000352138.

Structurei

3D structure databases

ProteinModelPortaliQ96J84.
SMRiQ96J84. Positions 19-503.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 11595Ig-like C2-type 1Add
BLAST
Domaini120 – 21697Ig-like C2-type 2Add
BLAST
Domaini223 – 29977Ig-like C2-type 3Add
BLAST
Domaini308 – 38780Ig-like C2-type 4Add
BLAST
Domaini392 – 48897Ig-like C2-type 5Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi405 – 4073Cell attachment siteSequence analysis

Sequence similaritiesi

Belongs to the immunoglobulin superfamily.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3510. Eukaryota.
ENOG410XPX0. LUCA.
GeneTreeiENSGT00550000074545.
HOVERGENiHBG052260.
InParanoidiQ96J84.
OMAiWILTLSD.
PhylomeDBiQ96J84.
TreeFamiTF327139.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamiPF08205. C2-set_2. 1 hit.
PF07679. I-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 5 hits.
SM00408. IGc2. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 5 hits.
PROSITEiPS50835. IG_LIKE. 5 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96J84-1) [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
MLSLLVWILT LSDTFSQGTQ TRFSQEPADQ TVVAGQRAVL PCVLLNYSGI
60 70 80 90 100
VQWTKDGLAL GMGQGLKAWP RYRVVGSADA GQYNLEITDA ELSDDASYEC
110 120 130 140 150
QATEAALRSR RAKLTVLIPP EDTRIDGGPV ILLQAGTPHN LTCRAFNAKP
160 170 180 190 200
AATIIWFRDG TQQEGAVAST ELLKDGKRET TVSQLLINPT DLDIGRVFTC
210 220 230 240 250
RSMNEAIPSG KETSIELDVH HPPTVTLSIE PQTVQEGERV VFTCQATANP
260 270 280 290 300
EILGYRWAKG GFLIEDAHES RYETNVDYSF FTEPVSCEVH NKVGSTNVST
310 320 330 340 350
LVNVHFAPRI VVDPKPTTTD IGSDVTLTCV WVGNPPLTLT WTKKDSNMVL
360 370 380 390 400
SNSNQLLLKS VTQADAGTYT CRAIVPRIGV AEREVPLYVN GPPIISSEAV
410 420 430 440 450
QYAVRGDGGK VECFIGSTPP PDRIAWAWKE NFLEVGTLER YTVERTNSGS
460 470 480 490 500
GVLSTLTINN VMEADFQTHY NCTAWNSFGP GTAIIQLEER EVLPVGIIAG
510 520 530 540 550
ATIGASILLI FFFIALVFFL YRRRKGSRKD VTLRKLDIKV ETVNREPLTM
560 570 580 590 600
HSDREDDTAS VSTATRVMKA IYSSFKDDVD LKQDLRCDTI DTREEYEMKD
610 620 630 640 650
PTNGYYNVRA HEDRPSSRAV LYADYRAPGP ARFDGRPSSR LSHSSGYAQL
660 670 680 690 700
NTYSRGPASD YGPEPTPPGP AAPAGTDTTS QLSYENYEKF NSHPFPGAAG
710 720 730 740 750
YPTYRLGYPQ APPSGLERTP YEAYDPIGKY ATATRFSYTS QHSDYGQRFQ

QRMQTHV
Length:757
Mass (Da):83,536
Last modified:October 11, 2004 - v2
Checksum:iB937421970447FC2
GO
Isoform 2 (identifier: Q96J84-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     348-348: M → MGPRPPGSPPEAALSAQ

Show »
Length:773
Mass (Da):85,049
Checksum:i15E52EBB96E962F2
GO
Isoform 3 (identifier: Q96J84-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     118-221: IPPEDTRIDG...ETSIELDVHH → N

Note: No experimental confirmation available.
Show »
Length:654
Mass (Da):72,360
Checksum:iD85531AFF726E5B6
GO

Sequence cautioni

The sequence AAP59845.1 differs from that shown. Reason: Frameshift at position 19. Curated
The sequence BAA91850.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB14192.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti591 – 60515DTREE…PTNGY → ERPRIRGRLNTSYSD (PubMed:11416156).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti78 – 781A → T.
Corresponds to variant rs35927201 [ dbSNP | Ensembl ].
VAR_059428

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei118 – 221104IPPED…LDVHH → N in isoform 3. 1 PublicationVSP_011732Add
BLAST
Alternative sequencei348 – 3481M → MGPRPPGSPPEAALSAQ in isoform 2. 2 PublicationsVSP_011733

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY017369 mRNA. Translation: AAK00529.1.
AY302131 mRNA. Translation: AAP59845.1. Frameshift.
AL139010 Genomic DNA. Translation: CAH73881.1.
CH471121 Genomic DNA. Translation: EAW52853.1.
BC025268 mRNA. Translation: AAH25268.1.
BC051356 mRNA. Translation: AAH51356.1.
BC067097 mRNA. Translation: AAH67097.1.
BC082969 mRNA. Translation: AAH82969.1.
BC109192 mRNA. Translation: AAI09193.1.
BC109193 mRNA. Translation: AAI09194.1.
AK001707 mRNA. Translation: BAA91850.1. Different initiation.
AK022708 mRNA. Translation: BAB14192.1. Different initiation.
CCDSiCCDS1172.2. [Q96J84-1]
RefSeqiNP_001273278.1. NM_001286349.1.
NP_060710.3. NM_018240.6. [Q96J84-1]
XP_005245362.1. XM_005245305.3. [Q96J84-2]
UniGeneiHs.272234.
Hs.609291.
Hs.657006.

Genome annotation databases

EnsembliENST00000359209; ENSP00000352138; ENSG00000183853. [Q96J84-1]
GeneIDi55243.
KEGGihsa:55243.
UCSCiuc001frn.6. human. [Q96J84-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY017369 mRNA. Translation: AAK00529.1.
AY302131 mRNA. Translation: AAP59845.1. Frameshift.
AL139010 Genomic DNA. Translation: CAH73881.1.
CH471121 Genomic DNA. Translation: EAW52853.1.
BC025268 mRNA. Translation: AAH25268.1.
BC051356 mRNA. Translation: AAH51356.1.
BC067097 mRNA. Translation: AAH67097.1.
BC082969 mRNA. Translation: AAH82969.1.
BC109192 mRNA. Translation: AAI09193.1.
BC109193 mRNA. Translation: AAI09194.1.
AK001707 mRNA. Translation: BAA91850.1. Different initiation.
AK022708 mRNA. Translation: BAB14192.1. Different initiation.
CCDSiCCDS1172.2. [Q96J84-1]
RefSeqiNP_001273278.1. NM_001286349.1.
NP_060710.3. NM_018240.6. [Q96J84-1]
XP_005245362.1. XM_005245305.3. [Q96J84-2]
UniGeneiHs.272234.
Hs.609291.
Hs.657006.

3D structure databases

ProteinModelPortaliQ96J84.
SMRiQ96J84. Positions 19-503.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120534. 25 interactions.
IntActiQ96J84. 5 interactions.
STRINGi9606.ENSP00000352138.

PTM databases

iPTMnetiQ96J84.
PhosphoSiteiQ96J84.

Polymorphism and mutation databases

DMDMi54036152.

Proteomic databases

EPDiQ96J84.
MaxQBiQ96J84.
PaxDbiQ96J84.
PeptideAtlasiQ96J84.
PRIDEiQ96J84.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359209; ENSP00000352138; ENSG00000183853. [Q96J84-1]
GeneIDi55243.
KEGGihsa:55243.
UCSCiuc001frn.6. human. [Q96J84-1]

Organism-specific databases

CTDi55243.
GeneCardsiKIRREL.
HGNCiHGNC:15734. KIRREL.
HPAiHPA003501.
HPA030458.
MIMi607428. gene.
neXtProtiNX_Q96J84.
PharmGKBiPA30126.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3510. Eukaryota.
ENOG410XPX0. LUCA.
GeneTreeiENSGT00550000074545.
HOVERGENiHBG052260.
InParanoidiQ96J84.
OMAiWILTLSD.
PhylomeDBiQ96J84.
TreeFamiTF327139.

Enzyme and pathway databases

ReactomeiR-HSA-373753. Nephrin interactions.

Miscellaneous databases

ChiTaRSiKIRREL. human.
GeneWikiiKIRREL.
GenomeRNAii55243.
PROiQ96J84.
SOURCEiSearch...

Gene expression databases

BgeeiQ96J84.
CleanExiHS_KIRREL.
ExpressionAtlasiQ96J84. baseline and differential.
GenevisibleiQ96J84. HS.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamiPF08205. C2-set_2. 1 hit.
PF07679. I-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 5 hits.
SM00408. IGc2. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 5 hits.
PROSITEiPS50835. IG_LIKE. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-606 (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Kidney.
  2. Shan Y.X., Huang C.Q., Yu L.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 251-757 (ISOFORM 2).
    Tissue: Ovary.
  6. "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] OF 199-757 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 303-757 (ISOFORM 1).
  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 TYR-622; TYR-625 AND TYR-724, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-297.
    Tissue: Liver.
  9. "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.
  10. "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-574, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiKIRR1_HUMAN
AccessioniPrimary (citable) accession number: Q96J84
Secondary accession number(s): Q5W0F8
, Q5XKC6, Q7Z696, Q7Z7N8, Q8TB15, Q9H9N1, Q9NVA5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 6, 2016
This is version 134 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.