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Protein

Pro-interleukin-16

Gene

IL16

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

Functioni

Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4.
Isoform 1 may act as a scaffolding protein that anchors ion channels in the membrane.
Isoform 3 is involved in cell cycle progression in T-cells. Appears to be involved in transcriptional regulation of SKP2 and is probably part of a transcriptional repression complex on the core promoter of the SKP2 gene. May act as a scaffold for GABPB1 (the DNA-binding subunit the GABP transcription factor complex) and HDAC3 thus maintaining transcriptional repression and blocking cell cycle progression in resting T-cells.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Chemotaxis, Host-virus interaction, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Pro-interleukin-16
Cleaved into the following chain:
Interleukin-16
Short name:
IL-16
Alternative name(s):
Lymphocyte chemoattractant factor
Short name:
LCF
Gene namesi
Name:IL16
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:5980. IL16.

Subcellular locationi

Isoform 1 :

GO - Cellular componenti

  • cytoplasm Source: HPA
  • extracellular space Source: ProtInc
  • nucleus Source: HPA
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi743 – 7431S → A: Reduces phosphorylation and nuclear localization. 1 Publication
Mutagenesisi757 – 7571T → A: Reduces phosphorylation. Enhances nuclear localization. 1 Publication
Mutagenesisi780 – 7812KK → AA: Reduces nuclear localization of pro-interleukin-16; when associated with 797-AGLANA-802. 1 Publication
Mutagenesisi797 – 8026KGLRNR → AGLANA: Reduces nuclear localization of pro-interleukin-16; when associated with 780-AA-781. 1 Publication
Mutagenesisi1211 – 12111D → A: Abolishes proteolytic cleavage. 1 Publication

Organism-specific databases

PharmGKBiPA29793.

Polymorphism and mutation databases

BioMutaiIL16.
DMDMi239938922.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13321332Pro-interleukin-16PRO_0000377543Add
BLAST
Chaini1212 – 1332121Interleukin-16PRO_0000015412Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei922 – 9221PhosphoserineCombined sources

Post-translational modificationi

Isoform 3 is synthesized as a chemo-attractant inactive precursor in hemopoietic tissues and is proteolytically cleaved by caspase-3 to yield IL-16.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ14005.
MaxQBiQ14005.
PaxDbiQ14005.
PRIDEiQ14005.

PTM databases

iPTMnetiQ14005.
PhosphoSiteiQ14005.

Miscellaneous databases

PMAP-CutDBQ14005.

Expressioni

Tissue specificityi

Isoform 3 is expressed in hemopoietic tissues, such as resting T-cells, but is undetectable during active T-cell proliferation.

Inductioni

Isoform 3 is down-regulated in T-cells after TCR activation.1 Publication

Gene expression databases

BgeeiQ14005.
CleanExiHS_IL16.
ExpressionAtlasiQ14005. baseline and differential.
GenevisibleiQ14005. HS.

Organism-specific databases

HPAiCAB005247.
HPA018467.

Interactioni

Subunit structurei

Homotetramer (Probable). According to PubMed:9699630, the formation of a homotetrameric protein complex is not required for the chemo-attractant function. Isoform 3 interacts (via PDZ 3 domain) with PPP1R12A, PPP1R12B and PPP1R12C. Isoform 1 interacts with PPP1R12B. Isoform 3 interacts with GRIN2A. Isoform 3 interacts with GABPB1. Isoform 3 interacts (via PDZ 3 domain) with HDAC3. Isoform 1 interacts with GRIN2D, KCNJ10, KCNJ15 and CACNA1C (By similarity). Isoform 3 interacts with HTLV-1 tax.By similarityCurated4 Publications

Protein-protein interaction databases

BioGridi109816. 25 interactions.
DIPiDIP-6006N.
IntActiQ14005. 8 interactions.
MINTiMINT-7006013.
STRINGi9606.ENSP00000302935.

Structurei

Secondary structure

1
1332
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1111 – 11177Combined sources
Beta strandi1125 – 11295Combined sources
Beta strandi1132 – 11354Combined sources
Beta strandi1140 – 11445Combined sources
Beta strandi1146 – 11483Combined sources
Helixi1149 – 11535Combined sources
Helixi1175 – 118410Combined sources
Beta strandi1187 – 119610Combined sources
Beta strandi1200 – 12023Combined sources
Beta strandi1209 – 12124Combined sources
Beta strandi1227 – 123812Combined sources
Beta strandi1241 – 12433Combined sources
Beta strandi1246 – 12494Combined sources
Beta strandi1255 – 12573Combined sources
Beta strandi1262 – 12665Combined sources
Beta strandi1273 – 12753Combined sources
Beta strandi1284 – 12863Combined sources
Helixi1292 – 12943Combined sources
Helixi1297 – 13059Combined sources
Beta strandi1309 – 132113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I16NMR-A1203-1332[»]
1X6DNMR-A1103-1208[»]
ProteinModelPortaliQ14005.
SMRiQ14005. Positions 1103-1332.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14005.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini216 – 30287PDZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini355 – 44086PDZ 2PROSITE-ProRule annotationAdd
BLAST
Domaini1112 – 119786PDZ 3PROSITE-ProRule annotationAdd
BLAST
Domaini1234 – 131986PDZ 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni183 – 452270Interaction with GRIN2AAdd
BLAST
Regioni1034 – 111885Interaction with HTLV-1 taxAdd
BLAST
Regioni1106 – 120297Interaction with PPP1R12A, PPP1R12B and PPP1R12CAdd
BLAST

Sequence similaritiesi

Contains 4 PDZ (DHR) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3528. Eukaryota.
ENOG4110362. LUCA.
GeneTreeiENSGT00760000119017.
HOVERGENiHBG000100.
InParanoidiQ14005.
OMAiAVIVTRK.
OrthoDBiEOG79W94J.
PhylomeDBiQ14005.
TreeFamiTF326303.

Family and domain databases

Gene3Di2.30.42.10. 4 hits.
InterProiIPR020450. IL-16.
IPR001478. PDZ.
[Graphical view]
PfamiPF00595. PDZ. 3 hits.
[Graphical view]
PRINTSiPR01931. INTRLEUKIN16.
SMARTiSM00228. PDZ. 4 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 4 hits.
PROSITEiPS50106. PDZ. 4 hits.
[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 promoter usage and alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14005-1) [UniParc]FASTAAdd to basket

Also known as: nPro-IL-16

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
MESHSRAGKS RKSAKFRSIS RSLMLCNAKT SDDGSSPDEK YPDPFEISLA
60 70 80 90 100
QGKEGIFHSS VQLADTSEAG PSSVPDLALA SEAAQLQAAG NDRGKTCRRI
110 120 130 140 150
FFMKESSTAS SREKPGKLEA QSSNFLFPKA CHQRARSNST SVNPYCTREI
160 170 180 190 200
DFPMTKKSAA PTDRQPYSLC SNRKSLSQQL DCPAGKAAGT SRPTRSLSTA
210 220 230 240 250
QLVQPSGGLQ ASVISNIVLM KGQAKGLGFS IVGGKDSIYG PIGIYVKTIF
260 270 280 290 300
AGGAAAADGR LQEGDEILEL NGESMAGLTH QDALQKFKQA KKGLLTLTVR
310 320 330 340 350
TRLTAPPSLC SHLSPPLCRS LSSSTCITKD SSSFALESPS APISTAKPNY
360 370 380 390 400
RIMVEVSLQK EAGVGLGIGL CSVPYFQCIS GIFVHTLSPG SVAHLDGRLR
410 420 430 440 450
CGDEIVEISD SPVHCLTLNE VYTILSHCDP GPVPIIVSRH PDPQVSEQQL
460 470 480 490 500
KEAVAQAVEN TKFGKERHQW SLEGVKRLES SWHGRPTLEK EREKNSAPPH
510 520 530 540 550
RRAQKVMIRS SSDSSYMSGS PGGSPGSGSA EKPSSDVDIS THSPSLPLAR
560 570 580 590 600
EPVVLSIASS RLPQESPPLP ESRDSHPPLR LKKSFEILVR KPMSSKPKPP
610 620 630 640 650
PRKYFKSDSD PQKSLEEREN SSCSSGHTPP TCGQEARELL PLLLPQEDTA
660 670 680 690 700
GRSPSASAGC PGPGIGPQTK SSTEGEPGWR RASPVTQTSP IKHPLLKRQA
710 720 730 740 750
RMDYSFDTTA EDPWVRISDC IKNLFSPIMS ENHGHMPLQP NASLNEEEGT
760 770 780 790 800
QGHPDGTPPK LDTANGTPKV YKSADSSTVK KGPPVAPKPA WFRQSLKGLR
810 820 830 840 850
NRASDPRGLP DPALSTQPAP ASREHLGSHI RASSSSSSIR QRISSFETFG
860 870 880 890 900
SSQLPDKGAQ RLSLQPSSGE AAKPLGKHEE GRFSGLLGRG AAPTLVPQQP
910 920 930 940 950
EQVLSSGSPA ASEARDPGVS ESPPPGRQPN QKTLPPGPDP LLRLLSTQAE
960 970 980 990 1000
ESQGPVLKMP SQRARSFPLT RSQSCETKLL DEKTSKLYSI SSQVSSAVMK
1010 1020 1030 1040 1050
SLLCLPSSIS CAQTPCIPKE GASPTSSSNE DSAANGSAET SALDTGFSLN
1060 1070 1080 1090 1100
LSELREYTEG LTEAKEDDDG DHSSLQSGQS VISLLSSEEL KKLIEEVKVL
1110 1120 1130 1140 1150
DEATLKQLDG IHVTILHKEE GAGLGFSLAG GADLENKVIT VHRVFPNGLA
1160 1170 1180 1190 1200
SQEGTIQKGN EVLSINGKSL KGTTHHDALA ILRQAREPRQ AVIVTRKLTP
1210 1220 1230 1240 1250
EAMPDLNSST DSAASASAAS DVSVESTAEA TVCTVTLEKM SAGLGFSLEG
1260 1270 1280 1290 1300
GKGSLHGDKP LTINRIFKGA ASEQSETVQP GDEILQLGGT AMQGLTRFEA
1310 1320 1330
WNIIKALPDG PVTIVIRRKS LQSKETTAAG DS
Note: Produced by alternative promoter usage. Is probably proteolytically processed to yield IL-16.
Length:1,332
Mass (Da):141,752
Last modified:June 16, 2009 - v4
Checksum:iEDF68567B2AF120C
GO
Isoform 2 (identifier: Q14005-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1228-1228: Missing.

Note: Produced by alternative splicing of isoform 1. Is probably proteolytically processed to yield IL-16.
Show »
Length:1,331
Mass (Da):141,681
Checksum:i245A4B513846E265
GO
Isoform 3 (identifier: Q14005-3) [UniParc]FASTAAdd to basket

Also known as: Pro-IL-16

The sequence of this isoform differs from the canonical sequence as follows:
     1-701: Missing.

Note: Produced by alternative promoter usage. Is proteolytically processed to yield IL-16.
Show »
Length:631
Mass (Da):66,646
Checksum:i49CC7EC488869F2D
GO
Isoform 4 (identifier: Q14005-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-701: Missing.
     1228-1228: Missing.
     1239-1332: KMSAGLGFSL...SKETTAAGDS → DVGRAGLQPGRREGLPTRRQASHH

Show »
Length:560
Mass (Da):59,345
Checksum:iF5346D25E57F8C4E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti273 – 2731E → G in AAQ86961 (PubMed:12923170).Curated
Sequence conflicti427 – 4271H → R in AAI36661 (PubMed:15489334).Curated
Sequence conflicti805 – 8051D → E in AAD04636 (PubMed:12923170).Curated
Sequence conflicti934 – 9341L → F in AAD04636 (PubMed:12923170).Curated
Sequence conflicti942 – 9443LRL → PRE (PubMed:16572171).Curated
Sequence conflicti1020 – 10201E → A in AAD04636 (PubMed:12923170).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti434 – 4341P → S.
Corresponds to variant rs4072111 [ dbSNP | Ensembl ].
VAR_058310
Natural varianti889 – 8891R → Q.1 Publication
Corresponds to variant rs17875512 [ dbSNP | Ensembl ].
VAR_019203
Natural varianti906 – 9061S → L.1 Publication
Corresponds to variant rs17875513 [ dbSNP | Ensembl ].
VAR_019204
Natural varianti1027 – 10271S → T.
Corresponds to variant rs34101586 [ dbSNP | Ensembl ].
VAR_034013
Natural varianti1147 – 11471N → K.1 Publication
Corresponds to variant rs11556218 [ dbSNP | Ensembl ].
VAR_019205
Natural varianti1176 – 11761H → R.
Corresponds to variant rs34159341 [ dbSNP | Ensembl ].
VAR_053372

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 701701Missing in isoform 3 and isoform 4. 2 PublicationsVSP_037458Add
BLAST
Alternative sequencei1228 – 12281Missing in isoform 2 and isoform 4. 3 PublicationsVSP_037459
Alternative sequencei1239 – 133294KMSAG…AAGDS → DVGRAGLQPGRREGLPTRRQ ASHH in isoform 4. 1 PublicationVSP_057192Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY324389 mRNA. Translation: AAQ86961.1.
FJ032370 mRNA. Translation: ACI00236.1.
M90391 mRNA. Translation: AAD04636.1.
AK131530 mRNA. Translation: BAD18668.1.
AC036196 Genomic DNA. No translation available.
AC103858 Genomic DNA. No translation available.
KF456108 Genomic DNA. No translation available.
BC136660 mRNA. Translation: AAI36661.1.
AF077011 Genomic DNA. Translation: AAD15990.1.
AY497901 Genomic DNA. Translation: AAR89904.1.
S81601 mRNA. Translation: AAB36371.2.
AF053412 mRNA. Translation: AAC12732.1.
CCDSiCCDS10317.1. [Q14005-3]
CCDS42069.1. [Q14005-1]
CCDS53966.1. [Q14005-2]
PIRiI59298.
RefSeqiNP_001165599.1. NM_001172128.1. [Q14005-2]
NP_004504.3. NM_004513.5. [Q14005-3]
NP_757366.2. NM_172217.3. [Q14005-1]
XP_005254403.1. XM_005254346.3. [Q14005-3]
XP_011519822.1. XM_011521520.1. [Q14005-1]
UniGeneiHs.459095.

Genome annotation databases

EnsembliENST00000302987; ENSP00000302935; ENSG00000172349. [Q14005-1]
ENST00000394652; ENSP00000378147; ENSG00000172349. [Q14005-3]
ENST00000394660; ENSP00000378155; ENSG00000172349. [Q14005-2]
ENST00000559388; ENSP00000458125; ENSG00000172349. [Q14005-4]
GeneIDi3603.
KEGGihsa:3603.
UCSCiuc002bgg.4. human. [Q14005-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY324389 mRNA. Translation: AAQ86961.1.
FJ032370 mRNA. Translation: ACI00236.1.
M90391 mRNA. Translation: AAD04636.1.
AK131530 mRNA. Translation: BAD18668.1.
AC036196 Genomic DNA. No translation available.
AC103858 Genomic DNA. No translation available.
KF456108 Genomic DNA. No translation available.
BC136660 mRNA. Translation: AAI36661.1.
AF077011 Genomic DNA. Translation: AAD15990.1.
AY497901 Genomic DNA. Translation: AAR89904.1.
S81601 mRNA. Translation: AAB36371.2.
AF053412 mRNA. Translation: AAC12732.1.
CCDSiCCDS10317.1. [Q14005-3]
CCDS42069.1. [Q14005-1]
CCDS53966.1. [Q14005-2]
PIRiI59298.
RefSeqiNP_001165599.1. NM_001172128.1. [Q14005-2]
NP_004504.3. NM_004513.5. [Q14005-3]
NP_757366.2. NM_172217.3. [Q14005-1]
XP_005254403.1. XM_005254346.3. [Q14005-3]
XP_011519822.1. XM_011521520.1. [Q14005-1]
UniGeneiHs.459095.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I16NMR-A1203-1332[»]
1X6DNMR-A1103-1208[»]
ProteinModelPortaliQ14005.
SMRiQ14005. Positions 1103-1332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109816. 25 interactions.
DIPiDIP-6006N.
IntActiQ14005. 8 interactions.
MINTiMINT-7006013.
STRINGi9606.ENSP00000302935.

PTM databases

iPTMnetiQ14005.
PhosphoSiteiQ14005.

Polymorphism and mutation databases

BioMutaiIL16.
DMDMi239938922.

Proteomic databases

EPDiQ14005.
MaxQBiQ14005.
PaxDbiQ14005.
PRIDEiQ14005.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302987; ENSP00000302935; ENSG00000172349. [Q14005-1]
ENST00000394652; ENSP00000378147; ENSG00000172349. [Q14005-3]
ENST00000394660; ENSP00000378155; ENSG00000172349. [Q14005-2]
ENST00000559388; ENSP00000458125; ENSG00000172349. [Q14005-4]
GeneIDi3603.
KEGGihsa:3603.
UCSCiuc002bgg.4. human. [Q14005-1]

Organism-specific databases

CTDi3603.
GeneCardsiIL16.
HGNCiHGNC:5980. IL16.
HPAiCAB005247.
HPA018467.
MIMi603035. gene.
neXtProtiNX_Q14005.
PharmGKBiPA29793.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3528. Eukaryota.
ENOG4110362. LUCA.
GeneTreeiENSGT00760000119017.
HOVERGENiHBG000100.
InParanoidiQ14005.
OMAiAVIVTRK.
OrthoDBiEOG79W94J.
PhylomeDBiQ14005.
TreeFamiTF326303.

Miscellaneous databases

EvolutionaryTraceiQ14005.
GeneWikiiInterleukin_16.
GenomeRNAii3603.
NextBioi14079.
PMAP-CutDBQ14005.
PROiQ14005.
SOURCEiSearch...

Gene expression databases

BgeeiQ14005.
CleanExiHS_IL16.
ExpressionAtlasiQ14005. baseline and differential.
GenevisibleiQ14005. HS.

Family and domain databases

Gene3Di2.30.42.10. 4 hits.
InterProiIPR020450. IL-16.
IPR001478. PDZ.
[Graphical view]
PfamiPF00595. PDZ. 3 hits.
[Graphical view]
PRINTSiPR01931. INTRLEUKIN16.
SMARTiSM00228. PDZ. 4 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 4 hits.
PROSITEiPS50106. PDZ. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PDZ domain-mediated interaction of interleukin-16 precursor proteins with myosin phosphatase targeting subunits."
    Bannert N., Vollhardt K., Asomuddinov B., Haag M., Koenig H., Norley S., Kurth R.
    J. Biol. Chem. 278:42190-42199(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PPP1R12A; PPP1R12B; PPP1R12C AND GRIN2A.
  2. "Discovery of novel human transcript variants by analysis of intronic single-block EST with polyadenylation site."
    Wang P., Yu P., Gao P., Shi T., Ma D.
    BMC Genomics 10:518-518(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
  3. Kornfeld H.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Peripheral blood.
  4. "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: Cerebellum.
  5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 2).
    Tissue: Testis.
  7. "GA-binding protein factors, in concert with the coactivator CREB binding protein/p300, control the induction of the interleukin 16 promoter in T lymphocytes."
    Bannert N., Avots A., Baier M., Serfling E., Kurth R.
    Proc. Natl. Acad. Sci. U.S.A. 96:1541-1546(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 685-1332.
  8. SeattleSNPs variation discovery resource
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 685-1332, VARIANTS GLN-889; LEU-906 AND LYS-1147.
  9. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 942-1332.
  10. "Molecular and functional analysis of a lymphocyte chemoattractant factor: association of biologic function with CD4 expression."
    Cruikshank W.W., Center D.M., Nisar N., Wu M., Natke B.C., Theodore A.C., Kornfeld H.
    Proc. Natl. Acad. Sci. U.S.A. 91:5109-5113(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1203-1332, SUBUNIT.
    Tissue: Peripheral blood.
  11. "Cloning, expression and purification of human interleukin-16."
    Du Y., Du G.X., Hou L.H., Wang H.T.
    Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 15:25-27(1999)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1203-1332.
  12. Cited for: PROTEIN SEQUENCE OF 1212-1220, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ASP-1211.
  13. "Nuclear translocation of the N-terminal prodomain of interleukin-16."
    Zhang Y., Kornfeld H., Cruikshank W.W., Kim S., Reardon C.C., Center D.M.
    J. Biol. Chem. 276:1299-1303(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION (PRO-INTERLEUKIN-16), MUTAGENESIS OF 780-LYS-LYS-781 AND 797-LYS--ARG-802.
  14. "Gene regulation mediated by calcium signals in T lymphocytes."
    Feske S., Giltnane J., Dolmetsch R., Staudt L.M., Rao A.
    Nat. Immunol. 2:316-324(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  15. "Prointerleukin-16 contains a functional CcN motif that regulates nuclear localization."
    Wilson K.C., Cruikshank W.W., Center D.M., Zhang Y.
    Biochemistry 41:14306-14312(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, MUTAGENESIS OF SER-743 AND THR-757.
  16. "Binding of HTLV-1 tax oncoprotein to the precursor of interleukin-16, a T cell PDZ domain-containing protein."
    Wilson K.C., Center D.M., Cruikshank W.W., Zhang Y.
    Virology 306:60-67(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTLV-1 TAX, SUBCELLULAR LOCATION.
  17. "Nuclear pro-IL-16 regulation of T cell proliferation: p27(KIP1)-dependent G0/G1 arrest mediated by inhibition of Skp2 transcription."
    Center D.M., Cruikshank W.W., Zhang Y.
    J. Immunol. 172:1654-1660(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (PRO-INTERLEUKIN-16), SUBCELLULAR LOCATION.
  18. "Pro-IL-16 recruits histone deacetylase 3 to the Skp2 core promoter through interaction with transcription factor GABP."
    Zhang Y., Tuzova M., Xiao Z.X., Cruikshank W.W., Center D.M.
    J. Immunol. 180:402-408(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (PRO-INTERLEUKIN-16), SUBCELLULAR LOCATION (PRO-INTERLEUKIN-16), INTERACTION WITH GABPB1 AND HDAC3.
  19. Cited for: 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-922, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. "Structure of interleukin 16 resembles a PDZ domain with an occluded peptide binding site."
    Muehlhahn P., Zweckstetter M., Georgescu J., Ciosto C., Renner C., Lanzendoerfer M., Lang K., Ambrosius D., Baier M., Kurth R., Holak T.A.
    Nat. Struct. Biol. 5:682-686(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1203-1332.
  22. "Solution structures of the PDZ domain of human interleukin-16."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1103-1209.

Entry informationi

Entry nameiIL16_HUMAN
AccessioniPrimary (citable) accession number: Q14005
Secondary accession number(s): A6NM20
, A8MU65, B5TY35, B9EGR6, H3BVH5, Q16435, Q6VVE6, Q6ZMQ7, Q9UP18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 16, 2009
Last modified: May 11, 2016
This is version 159 of the entry and version 4 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 15
    Human chromosome 15: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.